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Conserved domains on  [gi|15235282|ref|NP_195146|]
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D-3-phosphoglycerate dehydrogenase [Arabidopsis thaliana]

Protein Classification

phosphoglycerate dehydrogenase (domain architecture ID 11486731)

phosphoglycerate dehydrogenase catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, the first step in serine biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
62-603 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


:

Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   62 PTILVAEKLGDAGIKLLEDVA--NVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVD 139
Cdd:PRK13581   1 MKVLVSDPISPAGLEILKDAPgvEVDVKTGLDKEELLEIIGDYDALIVRSATKVTAEVLEAA-KNLKVIGRAGVGVDNVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  140 LSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRA 219
Cdd:PRK13581  80 VPAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKWERKKFMGVELYGKTLGIIGLGRIGSEVAKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  220 KGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:PRK13581 160 KAFGMKVIAYDPYISPERAAQLGVELVSLDELLARADFITLHTPLTPETRGLIGAEELAKMKPGVRIINCARGGIIDEAA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  300 LVRALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSA 379
Cdd:PRK13581 240 LAEALKSGKVAGAALDVFEKEPP-TDSPLFELPNVVVTPHLGASTAEAQENVAIQVAEQVIDALRGGPVPNAVNLPSITA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  380 EVLTELKPYVVLAEKLGRLAVQLVagGSGVKNAKITYASARAtdDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQR 459
Cdd:PRK13581 319 EEAEKLKPYLDLAEKLGSLAAQLA--DGPIKSVEITYRGELA--EEDTEPLTAAALKGLLSPVLGERVNYVNAPLLAKER 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  460 GLRLSEERvlldgSPESP--LETITVQLSNveskfasslsESGEVKVEGKV-KDGVPHLTKVGSFEVDVTLEGSIILCRQ 536
Cdd:PRK13581 395 GIEVEESK-----SEESPdySNLITVTVTT----------DDGERSVAGTVfGDGEPRIVEIDGYRVDAKPEGHMLIIRN 459
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235282  537 VDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:PRK13581 460 RDRPGVIGKVGTLLGEAGINIAGMQLGRREAGGEALMVLSVDDPVPEEVLEELRALPGILSAKAVEL 526
 
Name Accession Description Interval E-value
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
62-603 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   62 PTILVAEKLGDAGIKLLEDVA--NVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVD 139
Cdd:PRK13581   1 MKVLVSDPISPAGLEILKDAPgvEVDVKTGLDKEELLEIIGDYDALIVRSATKVTAEVLEAA-KNLKVIGRAGVGVDNVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  140 LSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRA 219
Cdd:PRK13581  80 VPAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKWERKKFMGVELYGKTLGIIGLGRIGSEVAKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  220 KGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:PRK13581 160 KAFGMKVIAYDPYISPERAAQLGVELVSLDELLARADFITLHTPLTPETRGLIGAEELAKMKPGVRIINCARGGIIDEAA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  300 LVRALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSA 379
Cdd:PRK13581 240 LAEALKSGKVAGAALDVFEKEPP-TDSPLFELPNVVVTPHLGASTAEAQENVAIQVAEQVIDALRGGPVPNAVNLPSITA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  380 EVLTELKPYVVLAEKLGRLAVQLVagGSGVKNAKITYASARAtdDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQR 459
Cdd:PRK13581 319 EEAEKLKPYLDLAEKLGSLAAQLA--DGPIKSVEITYRGELA--EEDTEPLTAAALKGLLSPVLGERVNYVNAPLLAKER 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  460 GLRLSEERvlldgSPESP--LETITVQLSNveskfasslsESGEVKVEGKV-KDGVPHLTKVGSFEVDVTLEGSIILCRQ 536
Cdd:PRK13581 395 GIEVEESK-----SEESPdySNLITVTVTT----------DDGERSVAGTVfGDGEPRIVEIDGYRVDAKPEGHMLIIRN 459
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235282  537 VDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:PRK13581 460 RDRPGVIGKVGTLLGEAGINIAGMQLGRREAGGEALMVLSVDDPVPEEVLEELRALPGILSAKAVEL 526
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
64-603 0e+00

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 540.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    64 ILVAEKLGDAGIKLLEDV-ANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSA 142
Cdd:TIGR01327   2 VLIADPISPDGIDILEDVgVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAP-KLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   223 GMRVIAHDPYAPADRAHAIGVDLV-SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALV 301
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   302 RALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSAEV 381
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPP-TDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   382 LTELKPYVVLAEKLGRLAVQLVAGgsGVKNAKITYASARATDdlDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQRGL 461
Cdd:TIGR01327 320 MEKLKPYLDLAEKLGKLAGQLLDG--AVQSVEVTYRGELATE--NSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   462 RLSEERVlldgSPESPLET-ITVQLSNveskfasslsESGEVKVEGKV-KDGVPHLTKVGSFEVDVTLEGSIILCRQVDQ 539
Cdd:TIGR01327 396 TVEESKS----ESSPDYKNyLSVTVTG----------DSGTVSVAGTVfGGFSPRIVEIDGFHVDLEPEGIMLIILHLDK 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282   540 PGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:TIGR01327 462 PGVIGKVGTLLGTAGINIASMQLGRKEKGGEALMLLSLDQPVPDEVLEEIKAIPDILSVFVVDL 525
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
64-366 3.93e-158

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240650  Cd Length: 304  Bit Score: 454.95  E-value: 3.93e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  64 ILVAEKLGDAGIKLLED-VANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSA 142
Cdd:cd12173   2 VLVTDPIDEEGLELLREaGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAP-RLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 223 GMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVR 302
Cdd:cd12173 161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282 303 ALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGE 366
Cdd:cd12173 241 ALKSGKIAGAALDVFEQEPPPADSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
60-382 6.66e-112

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223189  Cd Length: 324  Bit Score: 337.36  E-value: 6.66e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  60 SKPTILVAEKLGDAGIKLLEDVANVDCS--YNMTPEELNIKISLCDALIVrSGTKVGREVFESSHgRLKVVGRAGVGIDN 137
Cdd:COG0111   2 MMIKVLVTDPLAPDALEELLAAYDVEVPdgPDLDEEELLEALADADALIV-SVTPVTEEVLAAAP-NLKAIGRAGAGVDN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 138 VDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVAR 217
Cdd:COG0111  80 IDLEAATKRGILVVNAPGGNAISVAELVLALLLALARRIPDADASQRRGEWDRKAFRGTELAGKTVGIIGLGRIGRAVAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 218 RAKGLGMRVIAHDPYAPADRAHAIGVDLV-SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVID 296
Cdd:COG0111 160 RLKAFGMKVIGYDPYSPRERAGVDGVVGVdSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 297 EDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGElaATAVNAPM 376
Cdd:COG0111 240 EDALLAALDSGKIAGAALDVFEEEPLPADSPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAGG--PVVNNAPE 317

                ....*.
gi 15235282 377 VSAEVL 382
Cdd:COG0111 318 VDLERG 323
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
64-373 2.51e-98

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 334054  Cd Length: 312  Bit Score: 301.90  E-value: 2.51e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    64 ILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVDLSAA 143
Cdd:pfam00389   1 VLITDPLSPEALELLKEAAEVEVHDELLTEELLEKAKGADALIVRSNTPVTAEVLEAA-PKLKVIARAGVGVDNIDLDAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   144 TEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLG 223
Cdd:pfam00389  80 TERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLELYGKTLGVIGGGGIGGGVAAIAKALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   224 MRVIAHDPYAPADRAHAIGVDLVSFDEAL----ATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:pfam00389 160 MGVVAYDPYPNPERAEAGGVYVLSLDLLLldlpESDDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282   300 LVRALDAGIVAqAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVN 373
Cdd:pfam00389 240 LDALLEEGIAA-AADLDVEEEPPPVNSPLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGPPPNAVN 312
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
195-289 8.64e-11

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 60.54  E-value: 8.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    195 GVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-I 271
Cdd:smart00997  18 NVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTeiDPIR-ALEAAMDGFEVMKMEEAAKRADIF-----VTATGNKdV 91
                           90
                   ....*....|....*...
gi 15235282    272 LNDETFAKMKKGVRIVNV 289
Cdd:smart00997  92 ITREHFRAMKDGAILANA 109
 
Name Accession Description Interval E-value
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
62-603 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   62 PTILVAEKLGDAGIKLLEDVA--NVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVD 139
Cdd:PRK13581   1 MKVLVSDPISPAGLEILKDAPgvEVDVKTGLDKEELLEIIGDYDALIVRSATKVTAEVLEAA-KNLKVIGRAGVGVDNVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  140 LSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRA 219
Cdd:PRK13581  80 VPAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKWERKKFMGVELYGKTLGIIGLGRIGSEVAKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  220 KGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:PRK13581 160 KAFGMKVIAYDPYISPERAAQLGVELVSLDELLARADFITLHTPLTPETRGLIGAEELAKMKPGVRIINCARGGIIDEAA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  300 LVRALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSA 379
Cdd:PRK13581 240 LAEALKSGKVAGAALDVFEKEPP-TDSPLFELPNVVVTPHLGASTAEAQENVAIQVAEQVIDALRGGPVPNAVNLPSITA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  380 EVLTELKPYVVLAEKLGRLAVQLVagGSGVKNAKITYASARAtdDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQR 459
Cdd:PRK13581 319 EEAEKLKPYLDLAEKLGSLAAQLA--DGPIKSVEITYRGELA--EEDTEPLTAAALKGLLSPVLGERVNYVNAPLLAKER 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  460 GLRLSEERvlldgSPESP--LETITVQLSNveskfasslsESGEVKVEGKV-KDGVPHLTKVGSFEVDVTLEGSIILCRQ 536
Cdd:PRK13581 395 GIEVEESK-----SEESPdySNLITVTVTT----------DDGERSVAGTVfGDGEPRIVEIDGYRVDAKPEGHMLIIRN 459
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235282  537 VDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:PRK13581 460 RDRPGVIGKVGTLLGEAGINIAGMQLGRREAGGEALMVLSVDDPVPEEVLEELRALPGILSAKAVEL 526
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
64-603 0e+00

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 540.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    64 ILVAEKLGDAGIKLLEDV-ANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSA 142
Cdd:TIGR01327   2 VLIADPISPDGIDILEDVgVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAP-KLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   223 GMRVIAHDPYAPADRAHAIGVDLV-SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALV 301
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   302 RALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSAEV 381
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPP-TDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   382 LTELKPYVVLAEKLGRLAVQLVAGgsGVKNAKITYASARATDdlDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQRGL 461
Cdd:TIGR01327 320 MEKLKPYLDLAEKLGKLAGQLLDG--AVQSVEVTYRGELATE--NSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   462 RLSEERVlldgSPESPLET-ITVQLSNveskfasslsESGEVKVEGKV-KDGVPHLTKVGSFEVDVTLEGSIILCRQVDQ 539
Cdd:TIGR01327 396 TVEESKS----ESSPDYKNyLSVTVTG----------DSGTVSVAGTVfGGFSPRIVEIDGFHVDLEPEGIMLIILHLDK 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282   540 PGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:TIGR01327 462 PGVIGKVGTLLGTAGINIASMQLGRKEKGGEALMLLSLDQPVPDEVLEEIKAIPDILSVFVVDL 525
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
64-366 3.93e-158

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240650  Cd Length: 304  Bit Score: 454.95  E-value: 3.93e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  64 ILVAEKLGDAGIKLLED-VANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSA 142
Cdd:cd12173   2 VLVTDPIDEEGLELLREaGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAP-RLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 223 GMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVR 302
Cdd:cd12173 161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282 303 ALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGE 366
Cdd:cd12173 241 ALKSGKIAGAALDVFEQEPPPADSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
64-363 1.31e-113

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628  Cd Length: 301  Bit Score: 341.05  E-value: 1.31e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  64 ILVAEKLGDAGIKLLEDVA-NVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVDLSA 142
Cdd:cd05303   3 ILITDGIDEIAIEKLEEAGfEVDYEPLIAKEELLEKIKDYDVLIVRSRTKVTKEVIDAA-KNLKIIARAGVGLDNIDVEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:cd05303  82 AKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARAL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 223 GMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVR 302
Cdd:cd05303 162 GMNVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLE 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235282 303 ALDAGIVAQAALDVFTKEPPaKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGAL 363
Cdd:cd05303 242 ALKSGKLAGAALDVFENEPP-PGSKLLELPNVSLTPHIGASTKEAQERIGEELANKIIEFL 301
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
60-382 6.66e-112

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223189  Cd Length: 324  Bit Score: 337.36  E-value: 6.66e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  60 SKPTILVAEKLGDAGIKLLEDVANVDCS--YNMTPEELNIKISLCDALIVrSGTKVGREVFESSHgRLKVVGRAGVGIDN 137
Cdd:COG0111   2 MMIKVLVTDPLAPDALEELLAAYDVEVPdgPDLDEEELLEALADADALIV-SVTPVTEEVLAAAP-NLKAIGRAGAGVDN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 138 VDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVAR 217
Cdd:COG0111  80 IDLEAATKRGILVVNAPGGNAISVAELVLALLLALARRIPDADASQRRGEWDRKAFRGTELAGKTVGIIGLGRIGRAVAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 218 RAKGLGMRVIAHDPYAPADRAHAIGVDLV-SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVID 296
Cdd:COG0111 160 RLKAFGMKVIGYDPYSPRERAGVDGVVGVdSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 297 EDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGElaATAVNAPM 376
Cdd:COG0111 240 EDALLAALDSGKIAGAALDVFEEEPLPADSPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAGG--PVVNNAPE 317

                ....*.
gi 15235282 377 VSAEVL 382
Cdd:COG0111 318 VDLERG 323
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
69-364 2.56e-106

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649  Cd Length: 306  Bit Score: 322.51  E-value: 2.56e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  69 KLGDAGIKLLE----DVANVDCSYNMTPEELNIKISLCDALIVrsGT-KVGREVFESsHGRLKVVGRAGVGIDNVDLSAA 143
Cdd:cd12172  11 KYSEEAKELLEaagfEVVLNPLGRPLTEEELIELLKDADGVIA--GLdPITEEVLAA-APRLKVISRYGVGYDNIDLEAA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 144 TEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRnkYVGVSLVGKTLAVLGFGKVGTEVARRAKGLG 223
Cdd:cd12172  88 KKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWDR--PVGTELYGKTLGIIGLGRIGKAVARRLSGFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 224 MRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRA 303
Cdd:cd12172 166 MKVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEA 245
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235282 304 LDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALN 364
Cdd:cd12172 246 LKSGRIAGAALDVFEEEPPPADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDVLA 306
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
64-373 2.51e-98

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 334054  Cd Length: 312  Bit Score: 301.90  E-value: 2.51e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    64 ILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNVDLSAA 143
Cdd:pfam00389   1 VLITDPLSPEALELLKEAAEVEVHDELLTEELLEKAKGADALIVRSNTPVTAEVLEAA-PKLKVIARAGVGVDNIDLDAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   144 TEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLG 223
Cdd:pfam00389  80 TERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLELYGKTLGVIGGGGIGGGVAAIAKALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   224 MRVIAHDPYAPADRAHAIGVDLVSFDEAL----ATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:pfam00389 160 MGVVAYDPYPNPERAEAGGVYVLSLDLLLldlpESDDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282   300 LVRALDAGIVAqAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVN 373
Cdd:pfam00389 240 LDALLEEGIAA-AADLDVEEEPPPVNSPLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGPPPNAVN 312
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
91-361 3.32e-93

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624  Cd Length: 312  Bit Score: 288.64  E-value: 3.32e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  91 TPEELNIKISLCDALIVRSgTKVGREVFESSHgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMA 170
Cdd:cd05299  34 TEDELIEAAADADALLVQY-APVTAEVIEALP-RLKVIVRYGVGVDNVDVAAATERGIPVCNVPDYCTEEVADHALALIL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 171 AMARNVAQADASVKAGEWKRNKYVGV-SLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFD 249
Cdd:cd05299 112 ALARKLPFLDRAVRAGGWDWTVGGPIrRLRGLTLGLVGFGRIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGVRVVSLD 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 250 EALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLV 329
Cdd:cd05299 192 ELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGGLVDEAALARALKSGRIAGAALDVLEEEPPPADSPLL 271
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15235282 330 QHERVTVTPHLG----ASTMEAQEGVAIEIAEAVVG 361
Cdd:cd05299 272 SAPNVILTPHAAwyseESLAELRRKAAEEVVRVLRG 307
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
63-360 1.04e-92

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622  Cd Length: 302  Bit Score: 287.22  E-value: 1.04e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  63 TILVAEKLG-DAGIKLLED-VANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDL 140
Cdd:cd05198   1 KVLVLEPLFpPEALEALEAtGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAP-KLKFIQVAGAGVDNIDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 141 SAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGE-WKRNKYVGVSLVGKTLAVLGFGKVGTEVARRA 219
Cdd:cd05198  80 DAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWgWLWAGFPGYELEGKTVGIVGLGRIGQRVAKRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 220 KGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDA 299
Cdd:cd05198 160 QAFGMKVLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDA 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235282 300 LVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVV 360
Cdd:cd05198 240 LLRALKSGKIAGAALDVFEPEPLPADHPLLELPNVILTPHIAGYTEEARERMAEIAVENLE 300
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
62-365 3.65e-92

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240626  Cd Length: 309  Bit Score: 285.83  E-value: 3.65e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  62 PTILVAEKLGDAGIKLLEDVANV---DCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESShGRLKVVGRAGVGIDNV 138
Cdd:cd05301   1 PKVLVTRRLPEEALALLREGFEVevwDEDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAA-PPLKVIANYSVGYDHI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 139 DLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNK---YVGVSLVGKTLAVLGFGKVGTEV 215
Cdd:cd05301  80 DVDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSptlLLGTDLHGKTLGIVGMGRIGQAV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 216 ARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVI 295
Cdd:cd05301 160 ARRAKGFGMKILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVV 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 296 DEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNG 365
Cdd:cd05301 240 DEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
61-374 5.84e-91

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223980  Cd Length: 324  Bit Score: 283.35  E-value: 5.84e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  61 KPTILVAEKLGDAGIKLLEDvanvDCSYNMTPEELNIKISL------CDALIVRSGTKVGREVFESShGRLKVVGRAGVG 134
Cdd:COG1052   2 KIVVLSTRKLPPEVLERLKE----KFEVERYEDDLTPDTELaerlkdADAVITFVNDRIDAEVLEKL-PGLKLIATRSAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 135 IDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYV----GVSLVGKTLAVLGFGK 210
Cdd:COG1052  77 YDNVDLEAAKERGITVTNVPGYSTEAVAEHAVALILALARRIHEGDRRVREGNWSLSGGPdpllGFDLRGKTLGIIGLGR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 211 VGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVA 290
Cdd:COG1052 157 IGQAVARRLKGFGMKVLYYDRSPNPEAEKELGARYVDLDELLAESDIISLHCPLTPETRHLINAEELAKMKPGAILVNTA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 291 RGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKL---VQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGEL 367
Cdd:COG1052 237 RGGLVDEQALIDALKSGKIAGAGLDVFENEPALFDHPLlrlDNFPNVVLTPHIASATEEARKAMAELALENLEAFFDGGV 316

                ....*..
gi 15235282 368 AATAVNA 374
Cdd:COG1052 317 PPNEVNP 323
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
76-367 4.20e-87

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652  Cd Length: 311  Bit Score: 272.91  E-value: 4.20e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  76 KLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVfESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPT 155
Cdd:cd12175  18 ALLPPAPGVEVVTAAELDEEAALLADADVLVPGMRKVIDAEL-LAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 156 ANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKY-VGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYA- 233
Cdd:cd12175  97 GNAESVAEHAVMLMLALLRRLPEADRELRAGRWGRPEGrPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRd 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 234 PADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAA 313
Cdd:cd12175 177 PEAEEKDLGVRYVELDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAG 256
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15235282 314 LDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGEL 367
Cdd:cd12175 257 LDVFWQEPLPPDDPLLRLDNVILTPHIAGVTDESYQRMAAIVAENIARLLRGEP 310
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
63-373 1.79e-84

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651  Cd Length: 305  Bit Score: 265.96  E-value: 1.79e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  63 TILVAEKLGDAGIKLLEDVAnvdcsYNMTPEELNIkislCDALIVRSgTKVGREVFESShgrLKVVGRAGVGIDNVDLSA 142
Cdd:cd12174   2 KILTANKISKKGLERFKKDK-----YEVKEDALED----PDALIVRS-DKLHDMDFAPS---LKAIARAGAGVNNIDVDA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQA---------DASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGT 213
Cdd:cd12174  69 ASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAikwvtngdgDDISKGVEKGKKQFVGTELRGKTLGVIGLGNIGR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 214 EVARRAKGLGMRVIAHDPYAPADRAHAIGVDLV---SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVA 290
Cdd:cd12174 149 LVANAALALGMKVIGYDPYLSVEAAWKLSVEVQrvtSLEELLATADYITLHVPLTDETRGLINAELLAKMKPGAILLNFA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 291 RGGVIDEDALVRALDAGIVAQAALDVftkeppAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAAT 370
Cdd:cd12174 229 RGEIVDEEALLEALDEGKLGGYVTDF------PEPALLGHLPNVIATPHLGASTEEAEENCAVMAARQIMDFLETGNITN 302

                ...
gi 15235282 371 AVN 373
Cdd:cd12174 303 SVN 305
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
63-373 3.83e-83

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240655  Cd Length: 317  Bit Score: 262.94  E-value: 3.83e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  63 TILVAEKLGDAGIKLLEDVANVDCS---YNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVD 139
Cdd:cd12178   2 KVLVTGWIPKEALEELEENFEVTYYdglGLISKEELLERIADYDALITPLSTPVDKEIIDAAK-NLKIIANYGAGFDNID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 140 LSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAG---EWKRNKYVGVSLVGKTLAVLGFGKVGTEVA 216
Cdd:cd12178  81 VDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRGgflGWAPLFFLGHELAGKTLGIIGMGRIGQAVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 217 RRAKGLGMRVIAHDPY-APADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVI 295
Cdd:cd12178 161 RRAKAFGMKILYYNRHrLSEETEKELGATYVDLDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLV 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235282 296 DEDALVRALDAGIVAQAALDVFTKEPPAKDsKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVN 373
Cdd:cd12178 241 DEKALVDALKTGEIAGAALDVFEFEPEVSP-ELKKLDNVILTPHIGNATVEARDAMAKEAADNIISFLEGKRPKNIVN 317
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
90-347 6.56e-80

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648  Cd Length: 310  Bit Score: 254.38  E-value: 6.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  90 MTPEELNIKISLCDALIVRSGTkVGREVFESSHgRLKVVG--RAGVgiDNVDLSAATEFGCLVVNAPTANTIAAAEHGIA 167
Cdd:cd12171  35 EPEEELLEALKDADILITHFAP-VTKKVIEAAP-KLKLIGvcRGGP--ENVDVEAATERGIPVLNTPGRNAEAVAEFTVG 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 168 LMAAMARNVAQADASVKAGEWKRNKY----VGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGV 243
Cdd:cd12171 111 LMLAETRNIARAHAALKDGEWRKDYYnydgYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGV 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 244 DLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPA 323
Cdd:cd12171 191 KKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLP 270
                       250       260
                ....*....|....*....|....
gi 15235282 324 KDSKLVQHERVTVTPHLGASTMEA 347
Cdd:cd12171 271 ADHPLLKLDNVTLTPHIAGATRDV 294
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
115-373 1.25e-79

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654  Cd Length: 321  Bit Score: 254.17  E-value: 1.25e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 115 REVFESSHGrLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTA-NTIAAAEHGIALMAAMARNVAQADASVKAGEW-KRNK 192
Cdd:cd12177  61 KEFFEYNDG-LKLIARHGIGYDNVDLKAATEHGVIVTRVPGAvERDAVAEHAVALILTVLRKINQASEAVKEGKWtERAN 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 193 YVGVSLVGKTLAVLGFGKVGTEVARRAK-GLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKI 271
Cdd:cd12177 140 FVGHELSGKTVGIIGYGNIGSRVAEILKeGFNAKVLAYDPYVSEEVIKKKGAKPVSLEELLAESDIISLHAPLTEETYHM 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 272 LNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGV 351
Cdd:cd12177 220 INEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADHPLLHYENVVITPHIGAYTYESLYGM 299
                       250       260
                ....*....|....*....|..
gi 15235282 352 AIEIAEAVVGALNGELAATAVN 373
Cdd:cd12177 300 GEKVVDDIEDFLAGKEPKGILN 321
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
166-341 3.92e-78

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 335114 [Multi-domain]  Cd Length: 176  Bit Score: 244.70  E-value: 3.92e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   166 IALMAAMARNVAQADASVKAGEW-KRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADrAHAIGVD 244
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWaRRNALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPE-EEELGAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   245 LVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAK 324
Cdd:pfam02826  80 YVSLDELLAESDIVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEEEPLPA 159
                         170
                  ....*....|....*..
gi 15235282   325 DSKLVQHERVTVTPHLG 341
Cdd:pfam02826 160 DHPLLDLPNVILTPHIA 176
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
71-349 2.08e-75

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639  Cd Length: 307  Bit Score: 242.36  E-value: 2.08e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  71 GDAGIKLLEDVANVDCsYNMTPEELNIKIsLCDALIVRSG-TKVGREVFESSHgRLKVVGRAGVGIDNVDLSAATEFGCL 149
Cdd:cd12162  14 GDLSWDPLEFLGELTV-YDRTSPEEVVER-IKDADIVITNkVVLDAEVLAQLP-NLKLIGVLATGYNNVDLAAAKERGIT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 150 VVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRN------KYVGVSLVGKTLAVLGFGKVGTEVARRAKGLG 223
Cdd:cd12162  91 VTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSpdfcfwDYPIIELAGKTLGIIGYGNIGQAVARIARAFG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 224 MRVIAHDPYAPADRahaiGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRA 303
Cdd:cd12162 171 MKVLFAERKGAPPL----REGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADA 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15235282 304 LDAGIVAQAALDVFTKEPPAKDSKLVQ-HERVTVTPHLGASTMEAQE 349
Cdd:cd12162 247 LNSGKIAGAGLDVLSQEPPRADNPLLKaAPNLIITPHIAWASREARQ 293
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
125-360 5.02e-72

D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified as an enzyme that interconverts benzoylformate and D-mandelate, is a D-2-hydroxyacid dehydrogenase family member that catalyzes the conversion of c3-branched 2-ketoacids. D-ManDH exhibits broad substrate specificities for 2-ketoacids with large hydrophobic side chains, particularly those with C3-branched side chains. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Glycerate dehydrogenase catalyzes the reaction (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240645  Cd Length: 321  Bit Score: 233.98  E-value: 5.02e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNK--YVGVSLVGKT 202
Cdd:cd12168  77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLdlTLAHDPRGKT 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 203 LAVLGFGKVGTEVARRAKGLGMRVIAHDPY-APADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMK 281
Cdd:cd12168 157 LGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAKMK 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 282 KGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAkDSKLVQHERVTVTPHLGASTMEAQ---EGVAIEIAEA 358
Cdd:cd12168 237 DGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPEV-NPGLLKMPNVTLLPHMGTLTVETQekmEELVLENIEA 315

                ..
gi 15235282 359 VV 360
Cdd:cd12168 316 FL 317
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-377 1.34e-71

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 233.53  E-value: 1.34e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   60 SKPTILVAEKLGDAGIKLLEDVANVDC--SYNMTPEELNI-KISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGID 136
Cdd:PRK13243   1 MKPKVFITREIPENGIEMLEEHFEVEVweDEREIPREVLLeKVRDVDALVTMLSERIDCEVFEAAP-RLRIVANYAVGYD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  137 NVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNK-------YVGVSLVGKTLAVLGFG 209
Cdd:PRK13243  80 NIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  210 KVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNV 289
Cdd:PRK13243 160 RIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  290 ARGGVIDEDALVRALDAGIVAQAALDVFTKEpPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAA 369
Cdd:PRK13243 240 ARGKVVDTKALVKALKEGWIAGAGLDVFEEE-PYYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPP 318

                 ....*...
gi 15235282  370 TAVNAPMV 377
Cdd:PRK13243 319 TLVNREVV 326
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
76-367 6.53e-70

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240620  Cd Length: 323  Bit Score: 228.72  E-value: 6.53e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  76 KLLEDVANVDCSYNmtPEELNIKISLCDALIVRSGTKVGREVFESSHGrLKVVGRAGVGIDNVDLSAATEFGCLVVNAPT 155
Cdd:cd01619  22 AGGVDVEIVTYLLN--DDETAELAKGADAILTAFTDKIDAELLDKAPG-LKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 156 ANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPA 235
Cdd:cd01619  99 YSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNP 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 236 DrAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALD 315
Cdd:cd01619 179 E-LEDKGVKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLD 257
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235282 316 VFTKEPP-------------AKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGEL 367
Cdd:cd01619 258 VLEDETPdllkdlegeifkdALNALLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEGEE 322
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
61-365 2.10e-68

Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240646  Cd Length: 308  Bit Score: 224.31  E-value: 2.10e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  61 KPTIL-----VAEKLGDagIKLLEDVANVDcSYNMT---PEELNIKISLCDALIV-RSGTKVGREVFESSHgRLKVVGRA 131
Cdd:cd12169   1 RIAILddyqdVARTLAD--WSKLDDRAEVT-VFNDHlldEDALAERLAPFDAIVLmRERTPFPAALLERLP-NLKLLVTT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 132 GVGIDNVDLSAATEFGCLVVNAPTANTiAAAEHGIALMAAMARNVAQADASVKAGEWKRNkyVGVSLVGKTLAVLGFGKV 211
Cdd:cd12169  77 GMRNASIDLAAAKERGIVVCGTGGGPT-ATAELTWALILALARNLPEEDAALRAGGWQTT--LGTGLAGKTLGIVGLGRI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 212 GTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDL-VSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVA 290
Cdd:cd12169 154 GARVARIGQAFGMRVIAWSSNLTAERAAAAGVEAaVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTS 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235282 291 RGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNG 365
Cdd:cd12169 234 RGPLVDEGALLAALRAGRIAGAALDVFDVEPLPADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
90-360 1.77e-67

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240653  Cd Length: 304  Bit Score: 221.68  E-value: 1.77e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  90 MTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALM 169
Cdd:cd12176  31 LDEDELIEALKDVHLLGIRSKTQLTEEVLEAAP-KLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 170 AAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPyAPAdRAHAIGVDLVSFD 249
Cdd:cd12176 110 IMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYDI-AEK-LPLGNARQVSSLE 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 250 EALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKD---- 325
Cdd:cd12176 188 ELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGepfs 267
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15235282 326 SKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVV 360
Cdd:cd12176 268 SPLQGLPNVILTPHIGGSTEEAQENIGLEVAGKLV 302
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
61-365 3.41e-63

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634  Cd Length: 318  Bit Score: 210.61  E-value: 3.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  61 KPTILVAEKLGDAGIKLLEDVANVDCSYN---MTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDN 137
Cdd:cd12157   1 KPKVVITHKVHPEVLELLKPHCEVISNQTdepLSREELLRRCKDADGLMAFMPDRIDADFLDACP-RLKIIACALKGYDN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 138 VDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWK--RNKYVGVSLVGKTLAVLGFGKVGTEV 215
Cdd:cd12157  80 FDVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGgwRPKFYGTGLDGKTVGILGMGALGRAI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 216 ARRAKGLGMRVIAHDPYA-PADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGV 294
Cdd:cd12157 160 ARRLSGFGATLLYYDPHPlDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSV 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235282 295 IDEDALVRALDAGIVAQAALDVFTKEPPAKDSK--------LVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNG 365
Cdd:cd12157 240 VDEAAVAEALKSGHLGGYAADVFEMEDWARPDRprsipqelLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
111-347 9.93e-63

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240663  Cd Length: 329  Bit Score: 209.82  E-value: 9.93e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 111 TKVGREVFESsHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKR 190
Cdd:cd12187  51 SRLDAEVLEK-LPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQ 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 191 NKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSK 270
Cdd:cd12187 130 AGLRGFELAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYVSLEELLQESDIISLHVPYTPQTHH 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 271 ILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEP-------------PAKDSK-------LVQ 330
Cdd:cd12187 210 LINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelfredvSPEDLKklladhaLLR 289
                       250
                ....*....|....*..
gi 15235282 331 HERVTVTPHLGASTMEA 347
Cdd:cd12187 290 KPNVIITPHVAYNTKEA 306
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
62-352 4.94e-61

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625  Cd Length: 313  Bit Score: 204.68  E-value: 4.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  62 PTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIvrsGTKVGREVFESSHgRLKVVGRAGVGIDNVDLS 141
Cdd:cd05300   1 MKILVLSPLDDEHLERLRAAAPGAELRVVTAEELTEELADADVLL---GNPPLPELLPAAP-RLRWIQSTSAGVDALLFP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 142 AATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGvSLVGKTLAVLGFGKVGTEVARRAKG 221
Cdd:cd05300  77 ELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQRRGPVR-ELAGKTVLIVGLGDIGREIARRAKA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 222 LGMRVIA---HDPYAPADRAHAIGVDlvSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDED 298
Cdd:cd05300 156 FGMRVIGvrrSGRPAPPVVDEVYTPD--ELDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDED 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15235282 299 ALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVA 352
Cdd:cd05300 234 ALIEALESGRIAGAALDVFEEEPLPADSPLWDLPNVIITPHISGDSPSYPERVV 287
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
64-357 2.12e-60

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240656  Cd Length: 306  Bit Score: 202.91  E-value: 2.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  64 ILVAEKLGDAGIKLLEDVA-NVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSA 142
Cdd:cd12179   2 ILIIDKNHPSLTELLEALGfEVDYDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKAT-NLKFIARAGAGLENIDLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 143 ATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGL 222
Cdd:cd12179  81 AKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGIIGYGNMGKAFAKRLSGF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 223 GMRVIAHDPYAPADRAHAIGVDLvsfDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVR 302
Cdd:cd12179 161 GCKVIAYDKYKNFGDAYAEQVSL---ETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVK 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235282 303 ALDAGIVAQAALDV-----FTKEPPAKDSK----LVQHERVTVTPHLGASTMEAQEGVAIEIAE 357
Cdd:cd12179 238 ALKSGKILGACLDVleyekASFESIFNQPEafeyLIKSPKVILTPHIAGWTFESYEKIAEVLVD 301
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
91-344 1.06e-59

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644  Cd Length: 330  Bit Score: 202.02  E-value: 1.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  91 TPEELNIKISLCDALIVRSGT-KVGREVFESsHGRLKVVGRAGVGI-DNVDLsAATEFGCLVVNAPTANTIAAAEHGIAL 168
Cdd:cd12167  39 AAEELRALLAGVEVLVTGWGTpPLDAELLAR-APRLRAVVHAAGSVrGLVTD-AVWERGILVTSAADANAEPVAEFTLAA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 169 MAAMARNVAQADASVKAG--EWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLV 246
Cdd:cd12167 117 ILLALRRIPRFAAAYRAGrdWGWPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 247 SFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVaQAALDVFTKEPPAKDS 326
Cdd:cd12167 197 SLDELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRL-RAALDVTDPEPLPPDS 275
                       250
                ....*....|....*...
gi 15235282 327 KLVQHERVTVTPHLGAST 344
Cdd:cd12167 276 PLRTLPNVLLTPHIAGST 293
PRK11790 PRK11790
D-3-phosphoglycerate dehydrogenase; Provisional
58-378 1.03e-57

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 198.86  E-value: 1.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   58 DGSKPTILVAEKLGDAGIKLLED--VANVDC-SYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVG 134
Cdd:PRK11790   7 PKDKIKFLLLEGVHQSAVEVLRAagYTNIEYhKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAE-KLVAIGCFCIG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  135 IDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTE 214
Cdd:PRK11790  86 TNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNKSAAGSFEVRGKTLGIVGYGHIGTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  215 VARRAKGLGMRVIAHD-----PYAPADRAHaigvdlvSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNV 289
Cdd:PRK11790 166 LSVLAESLGMRVYFYDiedklPLGNARQVG-------SLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAILINA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  290 ARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKD----SKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNG 365
Cdd:PRK11790 239 SRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGdpfeSPLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYSDN 318
                        330
                 ....*....|...
gi 15235282  366 ELAATAVNAPMVS 378
Cdd:PRK11790 319 GSTLSAVNFPEVS 331
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
90-364 1.06e-57

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 196.60  E-value: 1.06e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  90 MTPEELNIK-ISL---CDALIVRSGTKVGREVFESSHGR-LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEH 164
Cdd:cd12186  29 TTTELLTPEtVDLakgYDGVVVQQTLPYDEEVYEKLAEYgIKQIALRSAGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 165 giALMAAM--ARNVAQADASVKAGEWKRNKyvgvSLVGK-----TLAVLGFGKVGTEVARRAKGLGMRVIAHDPYaPADR 237
Cdd:cd12186 109 --AVTQALnlLRNTPEIDRRVAKGDFRWAP----GLIGReirdlTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPY-PNPE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 238 AHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVF 317
Cdd:cd12186 182 LEKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALDTY 261
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 318 TKE-------------PPAKDSKLVQHERVTVTPHLGASTMEAqegvaieIAEAVVGALN 364
Cdd:cd12186 262 ENEtgyfnkdwsgkeiEDEVLKELIAMPNVLITPHIAFYTDTA-------VKNMVEISLD 314
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
102-357 1.92e-56

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 193.04  E-value: 1.92e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 102 CDALIVRSGTKVGREVFES-SHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQAD 180
Cdd:cd12183  45 FDAVCVFVNDDLDAPVLEKlAELGVKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 181 ASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYaPADRAHAIGVDLVSFDEALATADFISL 260
Cdd:cd12183 125 NRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPY-PNPELAKLGVEYVDLDELLAESDIISL 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 261 HMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPA--KD-----------SK 327
Cdd:cd12183 204 HCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLffEDhsdeiiqddvlAR 283
                       250       260       270
                ....*....|....*....|....*....|
gi 15235282 328 LVQHERVTVTPHLGASTMEAQEgvaiEIAE 357
Cdd:cd12183 284 LLSFPNVLITGHQAFFTKEALT----NIAE 309
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
92-366 3.16e-55

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, aka Hydroxypyruvate Reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240638  Cd Length: 315  Bit Score: 189.35  E-value: 3.16e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  92 PEELNIKISLCDALIVrSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAA 171
Cdd:cd12161  39 TAELIERSKDADIVMI-ANMPLPGEVIEACK-NLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAID 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 172 MARNVAQADASVKAGEWKrNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYaPADRAHAIGVDLVSFDEA 251
Cdd:cd12161 117 LLRNIVPCDAAVRAGGTK-AGLIGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRS-EKEEAKALGIEYVSLDEL 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 252 LATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPP-AKDSKLVQ 330
Cdd:cd12161 195 LAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPlPADYPLLH 274
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15235282 331 HERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGE 366
Cdd:cd12161 275 APNTILTPHVAFATEEAMEKRAEIVFDNIEAWLAGK 310
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
124-366 2.37e-52

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642  Cd Length: 314  Bit Score: 181.67  E-value: 2.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 124 RLKVVGRAGVGIDNVDLSAATEfGCLVVNAPtANTIAAAEHGIALMAAMARNVAQADASVKAGEWKR---NKYVGVSLVG 200
Cdd:cd12165  60 RLKLIQVPSAGVDHLPLERLPE-GVVVANNH-GNSPAVAEHALALILALAKRIVEYDNDLRRGIWHGragEEPESKELRG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 201 KTLAVLGFGKVGTEVARRAKGLGMRVIA----HDPYAPADRAHAIGvdlvSFDEALATADFISLHMPLTPTTSKILNDET 276
Cdd:cd12165 138 KTVGILGYGHIGREIARLLKAFGMRVIGvsrsPKEDEGADFVGTLS----DLDEALEQADVVVVALPLTKQTRGLIGAAE 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 277 FAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQH------ERVTVTPHLGASTMEAQEG 350
Cdd:cd12165 214 LAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVWWRYPSRGDPVAPSRypfhelPNVIMSPHNAGWTEETFRR 293
                       250
                ....*....|....*.
gi 15235282 351 VAIEIAEAVVGALNGE 366
Cdd:cd12165 294 RIDEAAENIRRYLRGE 309
PRK15409 PRK15409
bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional
61-373 5.72e-50

bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional


Pssm-ID: 185307  Cd Length: 323  Bit Score: 175.71  E-value: 5.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   61 KPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNikiSLCDAL-----IVRSGTKVGREVFESShGRLKVVGRAGVGI 135
Cdd:PRK15409   2 KPSVILYKALPDDLLQRLEEHFTVTQVANLSPETVE---QHAAAFaeaegLLGSGEKVDAALLEKM-PKLRAASTISVGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  136 DNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRN---KYVGVSLVGKTLAVLGFGKVG 212
Cdd:PRK15409  78 DNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTASigpDWFGTDVHHKTLGIVGMGRIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  213 TEVARRAK-GLGMRVI--AHDPYAPAD-RAHAIGVDLvsfDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVN 288
Cdd:PRK15409 158 MALAQRAHfGFNMPILynARRHHKEAEeRFNARYCDL---DTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFIN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  289 VARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELA 368
Cdd:PRK15409 235 AGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE 314

                 ....*
gi 15235282  369 ATAVN 373
Cdd:PRK15409 315 KNCVN 319
PRK06487 PRK06487
glycerate dehydrogenase; Provisional
125-366 5.73e-50

glycerate dehydrogenase; Provisional


Pssm-ID: 180588  Cd Length: 317  Bit Score: 175.66  E-value: 5.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVG------VSL 198
Cdd:PRK06487  67 LKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLALATRLPDYQQAVAAGRWQQSSQFClldfpiVEL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  199 VGKTLAVLGFGKVGTEVARRAKGLGMRV-IAHDPYAPAdRAhaigvDLVSFDEALATADFISLHMPLTPTTSKILNDETF 277
Cdd:PRK06487 147 EGKTLGLLGHGELGGAVARLAEAFGMRVlIGQLPGRPA-RP-----DRLPLDELLPQVDALTLHCPLTEHTRHLIGAREL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  278 AKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQ--HERVTVTPHLGASTMEAQEGVAIEI 355
Cdd:PRK06487 221 ALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVEPPVNGNPLLApdIPRLIVTPHSAWGSREARQRIVGQL 300
                        250
                 ....*....|.
gi 15235282  356 AEAVVGALNGE 366
Cdd:PRK06487 301 AENARAFFAGK 311
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
104-347 1.20e-47

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240633  Cd Length: 301  Bit Score: 168.80  E-value: 1.20e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 104 ALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASV 183
Cdd:cd12156  45 AVVTNGETGLSAALIAALP-ALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFV 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 184 KAGEWKRNKY-VGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVsfdeALAT-ADFISLH 261
Cdd:cd12156 124 RAGRWPKGAFpLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPYRYYASLL----ELAAeSDVLVVA 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 262 MPLTPTTSKILNDETFAKM-KKGVrIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEpPAKDSKLVQHERVTVTPHL 340
Cdd:cd12156 200 CPGGPATRHLVNAEVLEALgPDGV-LVNVARGSVVDEAALIAALQEGRIAGAGLDVFENE-PNVPAALLDLDNVVLTPHI 277

                ....*..
gi 15235282 341 GASTMEA 347
Cdd:cd12156 278 ASATVET 284
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
116-339 1.43e-47

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240632  Cd Length: 314  Bit Score: 168.91  E-value: 1.43e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 116 EVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKyVG 195
Cdd:cd12155  52 ELDLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMDS-SL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIA-----HD-PYApaDRAHAIGvDLvsfDEALATADFISLHMPLTPTTS 269
Cdd:cd12155 131 LELYGKTILFLGTGSIGQEIAKRLKAFGMKVIGvntsgRDvEYF--DKCYPLE-EL---DEVLKEADIVVNVLPLTEETH 204
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 270 KILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPH 339
Cdd:cd12155 205 HLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLPKDSPLWDLDNVLITPH 274
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
103-339 1.63e-47

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635  Cd Length: 343  Bit Score: 169.63  E-value: 1.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 103 DALIVRSGTKVGREVFESShgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARnvaqadas 182
Cdd:cd12158  38 DVLLVRSVTKVNEALLEGS--KVKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQ-------- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 183 vkagewkrnkYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADrahAIGVDLVSFDEALATADFISLHM 262
Cdd:cd12158 108 ----------RQGFSLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRAEA---EGDPGFVSLEELLAEADIITLHV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 263 PLTPT----TSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAkDSKLVqhERVT-VT 337
Cdd:cd12158 175 PLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEI-DLELL--DKVDiAT 251

                ..
gi 15235282 338 PH 339
Cdd:cd12158 252 PH 253
PRK06932 PRK06932
glycerate dehydrogenase; Provisional
105-340 3.09e-46

glycerate dehydrogenase; Provisional


Pssm-ID: 235890  Cd Length: 314  Bit Score: 165.36  E-value: 3.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  105 LIVRSGTKVGREVFeSSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVK 184
Cdd:PRK06932  47 IVITSKVLFTRETL-AQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALKHSLMGWYRDQL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  185 AGEWKRNK------YVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIahdpYAPADRAHAIGVDLVSFDEALATADFI 258
Cdd:PRK06932 126 SDRWATCKqfcyfdYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVL----YAEHKGASVCREGYTPFEEVLKQADIV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  259 SLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHER----V 334
Cdd:PRK06932 202 TLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPEKDNPLIQAAKrlpnL 281

                 ....*.
gi 15235282  335 TVTPHL 340
Cdd:PRK06932 282 LITPHI 287
PRK08410 PRK08410
2-hydroxyacid dehydrogenase; Provisional
61-366 1.15e-43

2-hydroxyacid dehydrogenase; Provisional


Pssm-ID: 181414  Cd Length: 311  Bit Score: 158.22  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   61 KPTILVAEKLGDAGIKLLEDVANVDcSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHgRLKVVGRAGVGIDNVDL 140
Cdd:PRK08410   2 KIVILDAKTLGDKDLSVFEEFGDFQ-IYPTTSPEEVIERIKDANIIITNKVVIDKEVLSQLP-NLKLICITATGTNNVDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  141 SAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNK-YVGVS-----LVGKTLAVLGFGKVGTE 214
Cdd:PRK08410  80 EYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSESPiFTHISrplgeIKGKKWGIIGLGTIGKR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  215 VARRAKGLGMRVIAhdpYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGV 294
Cdd:PRK08410 160 VAKIAQAFGAKVVY---YSTSGKNKNEEYERVSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGI 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235282  295 IDEDALVRALDAGIVAqAALDVFTKEPPAKDSKLVQ---HERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGE 366
Cdd:PRK08410 237 VNEKDLAKALDEKDIY-AGLDVLEKEPMEKNHPLLSiknKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEGG 310
PRK07574 PRK07574
formate dehydrogenase; Provisional
124-348 4.27e-43

formate dehydrogenase; Provisional


Pssm-ID: 181041  Cd Length: 385  Bit Score: 158.68  E-value: 4.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  124 RLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVS--LVGK 201
Cdd:PRK07574 114 NLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGWNIADCVSRSydLEGM 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  202 TLAVLGFGKVGTEVARRAKGLGMRVIAHDPY-APADRAHAIGVDL-VSFDEALATADFISLHMPLTPTTSKILNDETFAK 279
Cdd:PRK07574 194 TVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYhVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSR 273
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235282  280 MKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQ 348
Cdd:PRK07574 274 MKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQPAPADHPWRTMPRNGMTPHISGTTLSAQ 342
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
125-352 6.06e-43

NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of a formate anion to carbon dioxide coupled with the reduction of NAD+ to NADH. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family have 2 highly similar subdomains of the alpha/beta form, with NAD binding occurring in the cleft between subdomains. NAD contacts are primarily to the Rossmann-fold NAD-binding domain which is inserted within the linear sequence of the more diverse flavodoxin-like catalytic subdomain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production from C1 compounds such as methanol, and in the stress responses of plants. NAD-dependent FDH is useful in cofactor regeneration in asymmetrical biocatalytic reduction processes, where FDH irreversibly oxidizes formate to carbon dioxide, while reducing the oxidized form of the cofactor to the reduced form.


Pssm-ID: 240627  Cd Length: 348  Bit Score: 157.10  E-value: 6.06e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWK-----RNKYvgvSLV 199
Cdd:cd05302  85 LKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNvadvvKRAY---DLE 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 200 GKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYA-PADRAHAIGVDLV-SFDEALATADFISLHMPLTPTTSKILNDETF 277
Cdd:cd05302 162 GKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRlPEEVEKELGLTRHaDLEDMVSKCDVVTINCPLHPETEGLFNKELL 241
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235282 278 AKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVA 352
Cdd:cd05302 242 SKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPAPKDHPWRTMPNNAMTPHISGTTLDAQARYA 316
PLN02928 PLN02928
oxidoreductase family protein
84-344 1.51e-42

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 155.99  E-value: 1.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   84 VDCSYNMTPEElnikISLCDALIVRSgTKVGREVFESShGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAP---TANTIA 160
Cdd:PLN02928  48 DAVAREDVPDV----IANYDICVPKM-MRLDADIIARA-SQMKLIMQFGVGLEGVDVDAATKHGIKVARIPsegTGNAAS 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  161 AAEHGIALMAAMARNVAQADASVKA---GEwkrnkYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADR 237
Cdd:PLN02928 122 CAEMAIYLMLGLLRKQNEMQISLKArrlGE-----PIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEP 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  238 AHAIGVDLVSFD-------------EALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRAL 304
Cdd:PLN02928 197 EDGLLIPNGDVDdlvdekgghediyEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAAL 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15235282  305 DAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGAST 344
Cdd:PLN02928 277 ESGHLGGLAIDVAWSEPFDPDDPILKHPNVIITPHVAGVT 316
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
85-347 2.42e-42

Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, NAD-binding and catalytic domains; This group contains various putative dehydrogenases related to D-lactate dehydrogenase (LDH), (R)-2-hydroxyglutarate dehydrogenase (HGDH), and related enzymes, members of the 2-hydroxyacid dehydrogenases family. LDH catalyzes the interconversion of pyruvate and lactate, and HGDH catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Despite often low sequence identity within this 2-hydroxyacid dehydrogenase family, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240661  Cd Length: 322  Bit Score: 154.67  E-value: 2.42e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  85 DCSYNMTPEELNIK-ISL---CDALIVRSGTKVGREVFESSH-GRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTi 159
Cdd:cd12185  24 NVEVTLTKEPLTLEnAHLaegYDGISILGKSKISAELLEKLKeAGVKYISTRSIGYDHIDLDAAKELGIKVSNVTYSPN- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 160 AAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYaPADRAh 239
Cdd:cd12185 103 SVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPY-PNEEV- 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 240 AIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTK 319
Cdd:cd12185 181 KKYAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEG 260
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15235282 320 EP------------PAKD-SKLVQHERVTVTPHLGASTMEA 347
Cdd:cd12185 261 EDgiyyndrkgdilSNRElAILRSFPNVILTPHMAFYTDQA 301
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
123-357 4.32e-41

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240657  Cd Length: 308  Bit Score: 150.96  E-value: 4.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 123 GRLKVVGRAGVGIDNV--DLSAatefGCLVVNAPTANTIAAAEHGIALMAAMARNVAqaDASVK-AGEWKRNKyvGVSLV 199
Cdd:cd12180  63 GRLRWVQLVSSGIDYYpdWLFE----GPVVTCARGVAAEAIAEFVLAAILAAAKRLP--EIWVKgAEQWRREP--LGSLA 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 200 GKTLAVLGFGKVGTEVARRAKGLGMRVIA-HDPYAPADrahAIGVDLVS-FDEALATADFISLHMPLTPTTSKILNDETF 277
Cdd:cd12180 135 GSTLGIVGFGAIGQALARRALALGMRVLAlRRSGRPSD---VPGVEAAAdLAELFARSDHLVLAAPLTPETRHLINADVL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 278 AKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAE 357
Cdd:cd12180 212 AQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLPEGHPLYTHPRVRLSPHTSAIAPDGRRNLADRFLE 291
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
124-366 5.12e-40

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641  Cd Length: 306  Bit Score: 148.03  E-value: 5.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 124 RLKVVGRAGVGIDNVdLSAATEFG---CLVVNAPTANTIAAAehgiALMAAMA--RNVAQADASVKAGEWKRNKYVGVSL 198
Cdd:cd12164  58 NLKAIFSLGAGVDHL-LADPDLPDvpiVRLVDPGLAQGMAEY----VLAAVLRlhRDMDRYAAQQRRGVWKPLPQRPAAE 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 199 VgkTLAVLGFGKVGTEVARRAKGLGMRVI-----AHD-----PYAPADRahaigvdlvsFDEALATADF-ISLhMPLTPT 267
Cdd:cd12164 133 R--RVGVLGLGELGAAVARRLAALGFPVSgwsrsPKDiegvtCFHGEEG----------LDAFLAQTDIlVCL-LPLTPE 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 268 TSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLgASTMEA 347
Cdd:cd12164 200 TRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLPADHPLWRHPRVTVTPHI-AAITDP 278
                       250
                ....*....|....*....
gi 15235282 348 QEGVAIeIAEAVVGALNGE 366
Cdd:cd12164 279 DSAAAQ-VAENIRRLEAGE 296
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
89-347 7.56e-38

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240660  Cd Length: 330  Bit Score: 142.82  E-value: 7.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  89 NMTPEELN----IKISLCDALIVRSGTKVGREVFE--SSHGrLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAA 162
Cdd:cd12184  28 TLVEEYLNdenvHLAKGHDAVIVRGNCFADKENLEiyKEYG-IKYVFTRTVGFNHIDLEAAKELGFKMARVPSYSPNAIA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 163 EHGIALMAAMARNVAQADASVKAGEWKRNKYV-GVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYaPADRAHAI 241
Cdd:cd12184 107 ELAFTLAMTLSRHTAYTASRTANKNFKVDPFMfSKEIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIY-PSDAAKDV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 242 gVDLVSFDEALATADFISLHMPLTP-TTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKE 320
Cdd:cd12184 186 -VTFVSLDELLKKSDIISLHVPYIKgKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNE 264
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15235282 321 -------------PPAKDSKLVQ-HERVTVTPHLGASTMEA 347
Cdd:cd12184 265 keiffkdfdgdkiEDPVVEKLLDlYPRVLLTPHIGSYTDEA 305
PLN02306 PLN02306
hydroxypyruvate reductase
102-365 9.35e-34

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 132.67  E-value: 9.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  102 CDALIVRSGTKVGREVFES-SHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQAD 180
Cdd:PLN02306  63 CDGVIGQLTEDWGETLFSAlSKAGGKAFSNMAVGYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEAD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  181 ASVKAGE---WKRNKYVGVSLVGKTLAVLGFGKVGTEVAR-RAKGLGMRVIAHDPYaPADRAH----AIGVDL------- 245
Cdd:PLN02306 143 EFMRAGLyegWLPHLFVGNLLKGQTVGVIGAGRIGSAYARmMVEGFKMNLIYYDLY-QSTRLEkfvtAYGQFLkangeqp 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  246 ------VSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTK 319
Cdd:PLN02306 222 vtwkraSSMEEVLREADVISLHPVLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFED 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15235282  320 EPPAKDSkLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNG 365
Cdd:PLN02306 302 EPYMKPG-LADMKNAVVVPHIASASKWTREGMATLAALNVLGKLKG 346
PRK00257 PRK00257
erythronate-4-phosphate dehydrogenase; Validated
103-340 1.62e-33

erythronate-4-phosphate dehydrogenase; Validated


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 131.70  E-value: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  103 DALIVRSGTKVGREVFESShgRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANtiaaaehgialmaamARNVAQadas 182
Cdd:PRK00257  39 DVLLVRSVTRVDRALLEGS--RVRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCN---------------ARGVVD---- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  183 vkagewkrnkYV-----------GVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPyaPADRAHAIGvDLVSFDEA 251
Cdd:PRK00257  98 ----------YVlgslltlaereGVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDP--PRQEAEGDG-DFVSLERI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  252 LATADFISLHMPLTPT----TSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAkDSK 327
Cdd:PRK00257 165 LEECDVISLHTPLTKEgehpTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQI-DLE 243
                        250
                 ....*....|...
gi 15235282  328 LVQHERVTvTPHL 340
Cdd:PRK00257 244 LADLCTIA-TPHI 255
PLN03139 PLN03139
formate dehydrogenase; Provisional
125-348 1.24e-32

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 129.20  E-value: 1.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNK--YVGVSLVGKT 202
Cdd:PLN03139 122 LELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNVAGiaYRAYDLEGKT 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  203 LAVLGFGKVGTEVARRAKGLGMRVIAHDPYA-PADRAHAIGVDLVS-FDEALATADFISLHMPLTPTTSKILNDETFAKM 280
Cdd:PLN03139 202 VGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKmDPELEKETGAKFEEdLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKM 281
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235282  281 KKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQ 348
Cdd:PLN03139 282 KKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAPKDHPWRYMPNHAMTPHISGTTIDAQ 349
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
124-344 3.97e-31

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240643  Cd Length: 300  Bit Score: 123.08  E-value: 3.97e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 124 RLKVVGRAGVGIDNVdLSAATEfGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNkyVGVSLVGKTL 203
Cdd:cd12166  60 RLRVVQTLSAGYDGV-LPLLPE-GVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPR--RTPSLADRRV 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 204 AVLGFGKVGTEVARRAKGLGMRV--IAHDPyAPADRAHAIGvdlvSFDEALATADFISLHMPLTPTTSKILNDETFAKMK 281
Cdd:cd12166 136 LIVGYGSIGRAIERRLAPFEVRVtrVARTA-RPGEQVHGID----ELPALLPEADVVVLIVPLTDETRGLVDAEFLARMP 210
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235282 282 KGVRIVNVARGGVIDEDALVRALDAGIVaQAALDVFTKEPPAKDSKLVQHERVTVTPHLGAST 344
Cdd:cd12166 211 DGALLVNVARGPVVDTDALVAELASGRL-RAALDVTDPEPLPPGHPLWSAPGVLITPHVGGAT 272
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
125-373 9.27e-31

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 122.55  E-value: 9.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYV-GVSLVGKTL 203
Cdd:PRK08605  70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFRWEPPIlSRSIKDLKV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  204 AVLGFGKVGTEVAR-RAKGLGMRVIAHDPYaPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKK 282
Cdd:PRK08605 150 AVIGTGRIGLAVAKiFAKGYGSDVVAYDPF-PNAKAATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKK 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  283 GVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPP--AKDSK-----------LVQHERVTVTPHLGASTMEAQE 349
Cdd:PRK08605 229 GAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFERPlfPSDQRgqtindpllesLINREDVILTPHIAFYTDAAVK 308
                        250       260
                 ....*....|....*....|....
gi 15235282  350 GVAIEIAEAVVGALNGELAATAVN 373
Cdd:PRK08605 309 NLIVDALDATLEVLQTGTTRLRVN 332
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
162-344 5.18e-30

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240636  Cd Length: 303  Bit Score: 119.68  E-value: 5.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 162 AEHGIALMAAMARnvaQADASVKAGEWkrNKYVGVSLV----GKTLAVLGFGKVGTEVARRAKGLGMRVIA----HDPYA 233
Cdd:cd12159  88 AEHALALLLAGLR---QLPARARATTW--DPAEEDDLVtllrGSTVAIVGAGGIGRALIPLLAPFGAKVIAvnrsGRPVE 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 234 PADRAhaigVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAA 313
Cdd:cd12159 163 GADET----VPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAA 238
                       170       180       190
                ....*....|....*....|....*....|.
gi 15235282 314 LDVFTKEPPAKDSKLVQHERVTVTPHLGAST 344
Cdd:cd12159 239 LDVTDPEPLPDGHPLWSLPNALITPHVANTP 269
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
184-352 8.42e-29

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240640  Cd Length: 334  Bit Score: 116.99  E-value: 8.42e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 184 KAGEWKRNKYV--GVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH------DPYAPADRAHAI-------------- 241
Cdd:cd12163 115 KEQTWGRRQEAysVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprpTPESRKDDGYIVpgtgdpdgsipsaw 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 242 --GVDLVSFDEALATA-DFISLHMPLTPTTSKILNDETFAKM-KKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVF 317
Cdd:cd12163 195 fsGTDKASLHEFLRQDlDLLVVSLPLTPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVT 274
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15235282 318 TKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVA 352
Cdd:cd12163 275 DPEPLPADHPLWSAPNVIITPHVSWQTQEYFDRAL 309
PRK06436 PRK06436
glycerate dehydrogenase; Provisional
124-356 1.51e-27

glycerate dehydrogenase; Provisional


Pssm-ID: 235800  Cd Length: 303  Bit Score: 112.67  E-value: 1.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  124 RLKVVGRAGVGIDNVDLSAATEFGCLVVNApTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVgvSLVGKTL 203
Cdd:PRK06436  49 KTKMIQSLSAGVDHIDVSGIPENVVLCSNA-GAYSISVAEHAFALLLAWAKNICENNYNMKNGNFKQSPTK--LLYNKSL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  204 AVLGFGKVGTEVARRAKGLGMRVIAhdpYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKG 283
Cdd:PRK06436 126 GILGYGGIGRRVALLAKAFGMNIYA---YTRSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKG 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235282  284 VRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLvqhERVTVTPHLGASTMEAQEGVAIEIA 356
Cdd:PRK06436 203 LAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP---DNVILSPHVAGGMSGEIMQPAVALA 272
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
125-368 3.01e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 112.70  E-value: 3.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  125 LKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWK-RNKYVGVSLVGKTL 203
Cdd:PRK12480  70 IKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTwQAEIMSKPVKNMTV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  204 AVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDlvSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKG 283
Cdd:PRK12480 150 AIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDFLTYKD--SVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKG 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  284 VRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPP-------AKD------SKLVQHERVTVTPHLGASTMEAqeg 350
Cdd:PRK12480 228 AILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAyftndwtNKDiddktlLELIEHERILVTPHIAFFSDEA--- 304
                        250
                 ....*....|....*...
gi 15235282  351 vaieIAEAVVGALNGELA 368
Cdd:PRK12480 305 ----VQNLVEGGLNAALS 318
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
162-339 2.56e-24

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240637  Cd Length: 310  Bit Score: 103.61  E-value: 2.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 162 AEHGIALMAAMARNVAQADASVKAGEWK---------RNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPY 232
Cdd:cd12160  96 AEHTLALILAAVRRLDEMREAQREHRWAgelgglqplRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVTGVARS 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 233 ApADRAhaiGVDLVS---FDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIV 309
Cdd:cd12160 176 A-GERA---GFPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRL 251
                       170       180       190
                ....*....|....*....|....*....|
gi 15235282 310 AQAALDVFTKEPPAKDSKLVQHERVTVTPH 339
Cdd:cd12160 252 GGAALDVTATEPLPASSPLWDAPNLILTPH 281
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
103-358 1.03e-22

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 99.98  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  103 DALIVRSGTKVGREVFesSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMArnvaqadas 182
Cdd:PRK15438  39 DALMVRSVTKVNESLL--AGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA--------- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  183 vkagewKRNkyvGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPyAPADRAHAigVDLVSFDEALATADFISLHM 262
Cdd:PRK15438 108 ------ERD---GFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDP-PRADRGDE--GDFRSLDELVQEADILTFHT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  263 PL---TPTTSKILNDETF-AKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPpakDSKLVQHERVTV-T 337
Cdd:PRK15438 176 PLfkdGPYKTLHLADEKLiRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP---ELNVELLKKVDIgT 252
                        250       260
                 ....*....|....*....|.
gi 15235282  338 PHLGASTMEAQEGVAIEIAEA 358
Cdd:PRK15438 253 PHIAGYTLEGKARGTTQVFEA 273
ACT_3PGDH-xct cd04902
C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The ...
532-603 2.58e-21

C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153174 [Multi-domain]  Cd Length: 73  Bit Score: 87.53  E-value: 2.58e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235282 532 ILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL 603
Cdd:cd04902   2 LVVRNTDRPGVIGKVGTILGEAGINIAGMQVGRDEPGGEALMVLSVDEPVPDEVLEELRALPGILSAKVVEL 73
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
94-304 8.97e-19

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 87.29  E-value: 8.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  94 ELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLS-AATEFGCLVVNAPTA-------NTIAAAEHG 165
Cdd:cd12154  57 TLAKALWSLDVVLKVKEPLTNAEYALIQKLGDRLLFTYTIGADHRDLTeALARAGLTAIAVEGVelplltsNSIGAGELS 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 166 IALMAAMARNVAQADASVKAGewkrnkyvgvsLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHD--PYAPADRAHAIGV 243
Cdd:cd12154 137 VQFIARFLEVQQPGRLGGAPD-----------VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDinVEALEQLEELGGK 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235282 244 DLVSFDEALATADFISLHMPLTPTTSKILNDET-FAKMKKGVRIVNVARGGVIDEDALVRAL 304
Cdd:cd12154 206 NVEELEEALAEADVIVTTTLLPGKRAGILVPEElVEQMKPGSVIVNVAVGAVGCVQALHTQL 267
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
532-601 8.80e-18

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151 [Multi-domain]  Cd Length: 71  Bit Score: 77.51  E-value: 8.80e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 532 ILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFL 601
Cdd:cd04879   2 LLIVHKDVPGVIGKVGTILGEHGINIAAMQVGRKEKGGIAYMVLDVDSPVPEEVLEELKALPGIIRVRLI 71
ghrA PRK15469
bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional
202-364 4.61e-17

bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional


Pssm-ID: 185366  Cd Length: 312  Bit Score: 82.15  E-value: 4.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  202 TLAVLGFGKVGTEVARRAKGLG--MRVIAHDpyapadRAHAIGVDlvSF---DEALA----TADFISLhMPLTPTTSKIL 272
Cdd:PRK15469 138 TIGILGAGVLGSKVAQSLQTWGfpLRCWSRS------RKSWPGVQ--SFagrEELSAflsqTRVLINL-LPNTPETVGII 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  273 NDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGAST--MEAQEG 350
Cdd:PRK15469 209 NQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLPPESPLWQHPRVAITPHVAAVTrpAEAVEY 288
                        170
                 ....*....|....*....
gi 15235282  351 VA-----IEIAEAVVGALN 364
Cdd:PRK15469 289 ISrtiaqLEKGERVCGQVD 307
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
538-596 1.06e-12

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175 [Multi-domain]  Cd Length: 71  Bit Score: 63.32  E-value: 1.06e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15235282 538 DQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVE 596
Cdd:cd04903   8 DKPGAIAKVTSVLADHEINIAFMRVSRKEKGDQALMVIEVDQPIDEEVIEEIKKIPNIH 66
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
195-289 8.64e-11

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 60.54  E-value: 8.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    195 GVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-I 271
Cdd:smart00997  18 NVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTeiDPIR-ALEAAMDGFEVMKMEEAAKRADIF-----VTATGNKdV 91
                           90
                   ....*....|....*...
gi 15235282    272 LNDETFAKMKKGVRIVNV 289
Cdd:smart00997  92 ITREHFRAMKDGAILANA 109
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
196-288 3.34e-08

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 223573  Cd Length: 420  Bit Score: 55.72  E-value: 3.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPyAPADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-IL 272
Cdd:COG0499 205 VLLAGKNVVVAGYGWVGRGIAMRLRGMGARVIVTevDP-IRALEAAMDGFRVMTMEEAAKTGDIF-----VTATGNKdVI 278
                        90
                ....*....|....*.
gi 15235282 273 NDETFAKMKKGVRIVN 288
Cdd:COG0499 279 RKEHFEKMKDGAILAN 294
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
196-300 8.72e-08

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619  Cd Length: 402  Bit Score: 54.38  E-value: 8.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATAD-FIslhmplTPTTSK-I 271
Cdd:cd00401 191 VLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTevDPIC-ALQAAMDGFEVMPMEEAAKIGDiFV------TATGNKdV 263
                        90       100       110
                ....*....|....*....|....*....|
gi 15235282 272 LNDETFAKMKKGVRIVNVARGGV-IDEDAL 300
Cdd:cd00401 264 IRGEHFEKMKDGAILCNAGHFDVeIDVAAL 293
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
196-287 1.02e-07

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488  Cd Length: 425  Bit Score: 54.36  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-IL 272
Cdd:PRK05476 208 VLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTevDPIC-ALQAAMDGFRVMTMEEAAELGDIF-----VTATGNKdVI 281
                         90
                 ....*....|....*
gi 15235282  273 NDETFAKMKKGVrIV 287
Cdd:PRK05476 282 TAEHMEAMKDGA-IL 295
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
198-300 2.66e-06

adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]


Pssm-ID: 213572  Cd Length: 407  Bit Score: 49.71  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   198 LVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPyAPADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-ILND 274
Cdd:TIGR00936 194 IAGKTVVVAGYGWCGKGIAMRARGMGARVIVTevDP-IRALEAAMDGFRVMTMEEAAKIGDIF-----ITATGNKdVIRG 267
                          90       100
                  ....*....|....*....|....*..
gi 15235282   275 ETFAKMKKGVRIVNVARGGV-IDEDAL 300
Cdd:TIGR00936 268 EHFENMKDGAIVANIGHFDVeIDVKAL 294
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
530-594 3.47e-05

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5.


Pssm-ID: 334705 [Multi-domain]  Cd Length: 66  Bit Score: 41.91  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235282   530 SIILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRI-APRKQAIMAIGVDDIPSKETLKKIGEIPA 594
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALAERGINITSIEQRPSgDKGGIVFVVIVVDEEDLEEVLEALKKLEG 66
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
196-349 4.64e-05

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240647  Cd Length: 294  Bit Score: 45.37  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIahdpYAPADR---AHAIGVDLVSFDEALATADFISLHMpltPTTSKIL 272
Cdd:cd12170 134 RELTGLKVGIIGLGTTGQMIADALSFFGADVY----YYSRTRkpdAEAKGIRYLPLNELLKTVDVICTCL---PKNVILL 206
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235282 273 NDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDvftKEPPAKDSKLVQHERVTVTPHLGASTMEAQE 349
Cdd:cd12170 207 GEEEFELLGDGKILFNTSLGPSFEVEALKKWLKASGYNIFDCD---TAGALGDEELLRYPNVICTNKSAGWTRQAFE 280
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
196-292 8.40e-05

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 45.03  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-IL 272
Cdd:PTZ00075 250 VMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTeiDPIC-ALQAAMEGYQVVTLEDVVETADIF-----VTATGNKdII 323
                         90       100
                 ....*....|....*....|
gi 15235282  273 NDETFAKMKKGVRIVNVARG 292
Cdd:PTZ00075 324 TLEHMRRMKNNAIVGNIGHF 343
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
196-289 2.17e-04

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 279062 [Multi-domain]  Cd Length: 162  Bit Score: 41.95  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-IL 272
Cdd:pfam00670  19 VMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTeiDPIC-ALQAAMEGFQVVTLEEVVDKADIF-----VTTTGNKdII 92
                          90
                  ....*....|....*..
gi 15235282   273 NDETFAKMKKGVRIVNV 289
Cdd:pfam00670  93 TGEHMAKMKNDAIVCNI 109
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
204-295 3.80e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.95  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    204 AVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRA-----HAIGVDLVS----FDEALATAD-FISLHMPLTPTTSKILN 273
Cdd:smart01002  24 VVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQlesllGARFTTLYSqaelLEEAVKEADlVIGAVLIPGAKAPKLVT 103
                           90       100
                   ....*....|....*....|....
gi 15235282    274 DETFAKMKKGVRIVNVA--RGGVI 295
Cdd:smart01002 104 REMVKSMKPGSVIVDVAadQGGCI 127
SdaA COG1760
L-serine deaminase [Amino acid transport and metabolism];
515-595 6.09e-04

L-serine deaminase [Amino acid transport and metabolism];


Pssm-ID: 224674  Cd Length: 262  Bit Score: 41.82  E-value: 6.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 515 LTKVGSFEVDVTLEGSIILCrqVDQPGMI-GTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIP 593
Cdd:COG1760 167 LTELNGGSPEQSGNAPEIAM--EHNLGLTcDPVAGLVQVPCINRNAMGAVRAINGAKAAMAIEVDQRPLDEVIETMYETG 244

                ..
gi 15235282 594 AV 595
Cdd:COG1760 245 KD 246
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
538-588 6.94e-04

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 38.04  E-value: 6.94e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15235282 538 DQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKK 588
Cdd:cd02116   7 DRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLE 57
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
168-288 7.51e-04

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 41.83  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   168 LMAAMARNVAQADASVKagewkRNKYVGVSLVGKTLAVLGFG-KVGT---------EVARRAKGLGMRVIAHDPYAPADR 237
Cdd:TIGR03026 284 IEAAREINDSQPDYVVE-----KIKDLLGPLKGKTVLILGLAfKPNTddvrespalDIIELLKEKGAKVKAYDPLVPEEE 358
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15235282   238 AHAIGvDLVSFDEALATADFISLhmpLTPTTS-KILNDETFAKMKKGVRIVN 288
Cdd:TIGR03026 359 VKGLP-SIDDLEEALKGADALVI---LTDHSEfKDLDLEKIKDLMKGKVVVD 406
PRK08306 PRK08306
dipicolinate synthase subunit A; Reviewed
200-294 9.68e-04

dipicolinate synthase subunit A; Reviewed


Pssm-ID: 181371  Cd Length: 296  Bit Score: 41.36  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282  200 GKTLAVLGFGKVGTEVARRAKGLGMR--VIAHDPYAPAdRAHAIGVDLVSFD---EALATADFISLHMPltpttSKILND 274
Cdd:PRK08306 152 GSNVLVLGFGRTGMTLARTLKALGANvtVGARKSAHLA-RITEMGLSPFHLSelaEEVGKIDIIFNTIP-----ALVLTK 225
                         90       100
                 ....*....|....*....|..
gi 15235282  275 ETFAKMKKGVRIVNVAR--GGV 294
Cdd:PRK08306 226 EVLSKMPPEALIIDLASkpGGT 247
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
192-228 1.53e-03

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 40.21  E-value: 1.53e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15235282 192 KYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIA 228
Cdd:cd01076  23 KKLGIGLAGARVAIQGFGNVGSHAARFLHEAGAKVVA 59
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
202-297 3.82e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.70  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282 202 TLAVLGFGKVGTEVARRAKGLGMRVIAHDpyAPADRAHAIGVDLVSFD---------EALATAD-FISLHMPLTPTTSKI 271
Cdd:cd01620 164 KVLIIGAGVVGLGAAKIAKKLGANVLVYD--IKEEKLKGVETLGGSRLrysqkeeleKELKQTDiLINAILVDGPRAPIL 241
                        90       100
                ....*....|....*....|....*...
gi 15235282 272 LNDETFAKMKKGVRIVNVA--RGGVIDE 297
Cdd:cd01620 242 IMEELVGPMKRGAVIVDLAadQGGNDET 269
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
196-289 7.63e-03

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963  Cd Length: 426  Bit Score: 38.68  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282    196 VSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAH--DPYApADRAHAIGVDLVSFDEALATADFIslhmpLTPTTSK-IL 272
Cdd:smart00996 203 VMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTeiDPIC-ALQAAMDGFEVVTMEEVAPQADIF-----VTTTGNKdVI 276
                           90
                   ....*....|....*..
gi 15235282    273 NDETFAKMKKGVRIVNV 289
Cdd:smart00996 277 TREHMRAMKDGAIVCNI 293
purT TIGR01142
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ...
206-291 8.27e-03

phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 130212 [Multi-domain]  Cd Length: 380  Bit Score: 38.57  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235282   206 LGFGKVGTEVARRAKGLGMRVIAHDPY--AP----ADRAHAIgvDLVSFDEALATadfISLHMP--LTPTTSKILNDETF 277
Cdd:TIGR01142   5 LGSGELGKEVAIEAQRLGVEVIAVDRYanAPamqvAHRSYVI--NMLDGDALRAV---IEREKPdyIVPEIEAIATDALF 79
                          90
                  ....*....|....
gi 15235282   278 AKMKKGVRIVNVAR 291
Cdd:TIGR01142  80 ELEKEGYFVVPNAR 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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