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Conserved domains on  [gi|767961783|ref|XP_011537657|]
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C-terminal-binding protein 2 isoform X2 [Homo sapiens]

Protein Classification

C-terminal binding protein (domain architecture ID 10143094)

C-terminal binding protein (CtBP) functions as a transcriptional regulator by tethering chromatin remodeling proteins, such as histone deacetylases, histone methyl transferases, and histone demethylases, to DNA-bound transcription factors; CtBP may also have NAD-dependent dehydrogenase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 4.37e-148

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: 423.46  E-value: 4.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  34 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 110 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 190 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 270 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961783 350 PES 352
Cdd:cd05299  310 PRN 312
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 4.37e-148

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: 423.46  E-value: 4.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  34 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 110 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 190 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 270 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961783 350 PES 352
Cdd:cd05299  310 PRN 312
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
38-358 1.28e-84

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: 261.84  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783   38 LLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNeaVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIKAA 116
Cdd:pfam00389   2 LITDPLSPEALELLKEAAEVEVHDELLTEELLEKAKG--ADALIVRSNTpVTAEVLEAAPKLKVIARAGVGVDNIDLDAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  117 GELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQAVA 196
Cdd:pfam00389  80 TERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLEL-------YGKTLGVIGGGGIGGGVA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  197 VRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAA 271
Cdd:pfam00389 153 AIAKALGMGVVAYDPYPNP--ERAEAGGVYVLSLDLLLLDlpesdDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  272 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPe 351
Cdd:pfam00389 231 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVNS--PLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGPP- 307

                  ....*..
gi 767961783  352 slRNCVN 358
Cdd:pfam00389 308 --PNAVN 312
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
50-360 2.46e-83

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


Pssm-ID: 223189  Cd Length: 324  Bit Score: 258.78  E-value: 2.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  50 ILKDLATVAFCDAQSTQEIHEKVLNEAVG---AMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNI 126
Cdd:COG0111   16 ALEELLAAYDVEVPDGPDLDEEELLEALAdadALIVSVTPVTEEVLAAAPNLKAIGRAGAGVDNIDLEAATKRGILVVNA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 127 PSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSV 206
Cdd:COG0111   96 PGGNAISVAELVLALLLALARRIPDADASQRRG-------EWDRKAFRGTELAGKTVGIIGLGRIGRAVAKRLKAFGMKV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 207 IFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALK 286
Cdd:COG0111  169 IGYDPYSPRERAGVDGVVGVDSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVDEDALLAALD 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961783 287 EGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKE 360
Cdd:COG0111  249 SGKIAGAALDVFEEEPLP-ADSPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAGGPVVNNAPEVDLE 321
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
86-358 7.27e-72

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 235.35  E-value: 7.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGT----R 161
Cdd:PRK13581  53 KVTAEVLEAAKNLKVIGRAGVGVDNVDVPAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKwerkK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 VQSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSL 241
Cdd:PRK13581 133 FMGVE-----------LYGKTLGIIGLGRIGSEVAKRAKAFGMKVIAYDPYISPERAAQLGVELV-SLDELLARADFITL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 242 HCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPH 321
Cdd:PRK13581 201 HTPLTPETRGLIGAEELAKMKPGVRIINCARGGIIDEAALAEALKSGKVAGAALDVFEKEP--PTDSPLFELPNVVVTPH 278
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767961783 322 TAwyseqAS-LEMREAAAT----EIRRAITGripESLRNCVN 358
Cdd:PRK13581 279 LG-----AStAEAQENVAIqvaeQVIDALRG---GPVPNAVN 312
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
86-358 1.71e-66

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: 221.43  E-value: 1.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783   86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsv 165
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  166 EQIREVASGAaRIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNL 245
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERAEQLGVELVDDLDELLARADFITVHTPL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  246 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWY 325
Cdd:TIGR01327 204 TPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPT--DNPLFDLDNVIATPHLGAS 281
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767961783  326 SEQASLEMREAAATEIRRAITGripESLRNCVN 358
Cdd:TIGR01327 282 TREAQENVATQVAEQVLDALKG---LPVPNAVN 311
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 4.37e-148

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: 423.46  E-value: 4.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  34 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 110 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 190 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 270 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961783 350 PES 352
Cdd:cd05299  310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
36-343 2.22e-103

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: 309.56  E-value: 2.22e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  36 VALLDGRDCTVEMPILKDL-ATVAFCDAQSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIK 114
Cdd:cd05198    2 VLVLEPLFPPEALEALEATgFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 115 AAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRvqsveqIREVASGAARIRGETLGLIGFGRTGQA 194
Cdd:cd05198   81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 195 VAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGG 274
Cdd:cd05198  155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961783 275 LVDEKALAQALKEGRIRGAALDVHESEPFSFAqGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRR 343
Cdd:cd05198  234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
64-344 3.94e-89

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: 273.21  E-value: 3.94e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  64 STQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHIL 143
Cdd:cd12172   37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 144 NLYRRNTWLYQALREG--TRVQSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSL 221
Cdd:cd12172  115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 222 GVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE 301
Cdd:cd12172  184 GVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767961783 302 PFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 344
Cdd:cd12172  263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
88-348 5.77e-86

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: 264.66  E-value: 5.77e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  88 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGT----RVQ 163
Cdd:cd12173   53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 164 SVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHC 243
Cdd:cd12173  133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGGVELV-SLDELLAEADFISLHT 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 244 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 323
Cdd:cd12173  201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                        250       260
                 ....*....|....*....|....*
gi 767961783 324 WYSEQASLEMREAAATEIRRAITGR 348
Cdd:cd12173  280 ASTEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
38-358 1.28e-84

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: 261.84  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783   38 LLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNeaVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIKAA 116
Cdd:pfam00389   2 LITDPLSPEALELLKEAAEVEVHDELLTEELLEKAKG--ADALIVRSNTpVTAEVLEAAPKLKVIARAGVGVDNIDLDAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  117 GELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQAVA 196
Cdd:pfam00389  80 TERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLEL-------YGKTLGVIGGGGIGGGVA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  197 VRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAA 271
Cdd:pfam00389 153 AIAKALGMGVVAYDPYPNP--ERAEAGGVYVLSLDLLLLDlpesdDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  272 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPe 351
Cdd:pfam00389 231 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVNS--PLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGPP- 307

                  ....*..
gi 767961783  352 slRNCVN 358
Cdd:pfam00389 308 --PNAVN 312
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
50-360 2.46e-83

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


Pssm-ID: 223189  Cd Length: 324  Bit Score: 258.78  E-value: 2.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  50 ILKDLATVAFCDAQSTQEIHEKVLNEAVG---AMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNI 126
Cdd:COG0111   16 ALEELLAAYDVEVPDGPDLDEEELLEALAdadALIVSVTPVTEEVLAAAPNLKAIGRAGAGVDNIDLEAATKRGILVVNA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 127 PSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSV 206
Cdd:COG0111   96 PGGNAISVAELVLALLLALARRIPDADASQRRG-------EWDRKAFRGTELAGKTVGIIGLGRIGRAVAKRLKAFGMKV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 207 IFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALK 286
Cdd:COG0111  169 IGYDPYSPRERAGVDGVVGVDSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVDEDALLAALD 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961783 287 EGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPESLRNCVNKE 360
Cdd:COG0111  249 SGKIAGAALDVFEEEPLP-ADSPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAGGPVVNNAPEVDLE 321
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
51-360 6.33e-82

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: 255.23  E-value: 6.33e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  51 LKDLATVAFCDAQSTQEIHE-KVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA 129
Cdd:COG1052   19 LKEKFEVERYEDDLTPDTELaERLKDADAVITFVNDRIDAEVLEKLPGLKLIATRSAGYDNVDLEAAKERGITVTNVPGY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 130 AVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVASgaaRIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFY 209
Cdd:COG1052   99 STEAVAEHAVALILALARRIHEGDRRVREGNWSLSGGPDPLLGF---DLRGKTLGIIGLGRIGQAVARRLKGFGMKVLYY 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 210 DPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGR 289
Cdd:COG1052  176 DRSPNPEAEKELGARYV-DLDELLAESDIISLHCPLTPETRHLINAEELAKMKPGAILVNTARGGLVDEQALIDALKSGK 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961783 290 IRGAALDVHESEPFSFAQgPLKDAPN---LICTPHTAWYSEQASLEMREAAATEIRRAITGRIPEslrNCVNKE 360
Cdd:COG1052  255 IAGAGLDVFENEPALFDH-PLLRLDNfpnVVLTPHIASATEEARKAMAELALENLEAFFDGGVPP---NEVNPE 324
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
84-350 1.07e-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: 240652  Cd Length: 311  Bit Score: 249.03  E-value: 1.07e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  84 TITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvq 163
Cdd:cd12175   52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 164 svEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLH 242
Cdd:cd12175  128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLH 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 243 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHT 322
Cdd:cd12175  205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLP-PDDPLLRLDNVILTPHI 283
                        250       260
                 ....*....|....*....|....*...
gi 767961783 323 AWYSEQASLEMREAAATEIRRAITGRIP 350
Cdd:cd12175  284 AGVTDESYQRMAAIVAENIARLLRGEPP 311
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
87-335 2.33e-76

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: 240.43  E-value: 2.33e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 166
Cdd:cd12162   55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 Q------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIerslGVQRVyTLQDLLYQSDCVS 240
Cdd:cd12162  135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYV-SLDELLAQSDVIS 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL-KDAPNLICT 319
Cdd:cd12162  203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPR-ADNPLlKAAPNLIIT 281
                        250
                 ....*....|....*.
gi 767961783 320 PHTAWyseqASLEMRE 335
Cdd:cd12162  282 PHIAW----ASREARQ 293
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
88-358 1.07e-73

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: 233.67  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  88 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlyqaLREGTRvqsveQ 167
Cdd:cd12178   56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR-------IAEGDR-----L 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 168 IRE-VASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDC 238
Cdd:cd12178  124 MRRgGFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDF 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 239 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGpLKDAPNLIC 318
Cdd:cd12178  203 VSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVIL 280
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767961783 319 TPHTAWYSEQASLEMREAAATEIRRAITGRIPeslRNCVN 358
Cdd:cd12178  281 TPHIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
86-358 7.27e-72

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 235.35  E-value: 7.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGT----R 161
Cdd:PRK13581  53 KVTAEVLEAAKNLKVIGRAGVGVDNVDVPAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKwerkK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 VQSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSL 241
Cdd:PRK13581 133 FMGVE-----------LYGKTLGIIGLGRIGSEVAKRAKAFGMKVIAYDPYISPERAAQLGVELV-SLDELLARADFITL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 242 HCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPH 321
Cdd:PRK13581 201 HTPLTPETRGLIGAEELAKMKPGVRIINCARGGIIDEAALAEALKSGKVAGAALDVFEKEP--PTDSPLFELPNVVVTPH 278
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767961783 322 TAwyseqAS-LEMREAAAT----EIRRAITGripESLRNCVN 358
Cdd:PRK13581 279 LG-----AStAEAQENVAIqvaeQVIDALRG---GPVPNAVN 312
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
48-347 1.01e-70

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: 225.74  E-value: 1.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  48 MPILKDLATVAFCD---AQSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVC 124
Cdd:cd05301   14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 125 NIPSAAVEETADSTICHILNLYRRntwlyqaLREGtrvqsveqIREVASGA-----------ARIRGETLGLIGFGRTGQ 193
Cdd:cd05301   93 NTPDVLTDATADLAFALLLAAARR-------VVEG--------DRFVRAGEwkgwsptlllgTDLHGKTLGIVGMGRIGQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 194 AVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 273
Cdd:cd05301  158 AVARRAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961783 274 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 347
Cdd:cd05301  237 GVVDEDALVEALKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
37-355 1.99e-70

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: 225.66  E-value: 1.99e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  37 ALLDGRDCTVEMPILKDLATVAFCDAQSTqeIHEKVLNEAVgaMMYHTI------TLTREDLEKFKALRVIVRIGSGYDN 110
Cdd:cd12177    7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKL--KGYDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 111 VDIKAAGELGIAVCNIPSA----AVEETAdstICHILNLYRRNTWLYQALREGtrvqsveQIREVASGAAR-IRGETLGL 185
Cdd:cd12177   83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 186 IGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQG 264
Cdd:cd12177  153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 265 AFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 344
Cdd:cd12177  232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIK-ADHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                        330
                 ....*....|.
gi 767961783 345 ITGRIPESLRN 355
Cdd:cd12177  311 LAGKEPKGILN 321
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
98-347 3.34e-70

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: 224.73  E-value: 3.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  98 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEqirevASGAAR 177
Cdd:cd12168   77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 178 IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDF 256
Cdd:cd12168  152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALATYYV-SLDELLAQSDVVSLNCPLTAATRHLINKK 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 257 TIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAWYSEQASLEMREA 336
Cdd:cd12168  231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEP--EVNPGLLKMPNVTLLPHMGTLTVETQEKMEEL 308
                        250
                 ....*....|.
gi 767961783 337 AATEIRRAITG 347
Cdd:cd12168  309 VLENIEAFLET 319
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
50-348 7.34e-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: 224.10  E-value: 7.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  50 ILKDL-ATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPS 128
Cdd:cd01619   19 ILKAGgVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 129 AAVEETADSTICHILNLYRRntwlyqalREGTRVQSVEQIREVAS-GAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVI 207
Cdd:cd01619   99 YSPNAVAEHTIALILALLRN--------RKYIDERDKNQDLQDAGvIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 208 FYDPYLQDGIERSlGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKE 287
Cdd:cd01619  171 AYDPFRNPELEDK-GVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDS 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961783 288 GRIRGAALDVHESE-----------PFSFAQGP-LKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 348
Cdd:cd01619  249 GKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEGE 321
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
139-323 2.04e-67

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: 212.72  E-value: 2.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  139 ICHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGI 217
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwARRNALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  218 ERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV 297
Cdd:pfam02826  74 EE-LGARYV-SLDELLAESDIVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 151
                         170       180
                  ....*....|....*....|....*.
gi 767961783  298 HESEPFSfAQGPLKDAPNLICTPHTA 323
Cdd:pfam02826 152 FEEEPLP-ADHPLLDLPNVILTPHIA 176
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
86-358 1.71e-66

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: 221.43  E-value: 1.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783   86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsv 165
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  166 EQIREVASGAaRIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNL 245
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERAEQLGVELVDDLDELLARADFITVHTPL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  246 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWY 325
Cdd:TIGR01327 204 TPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPT--DNPLFDLDNVIATPHLGAS 281
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767961783  326 SEQASLEMREAAATEIRRAITGripESLRNCVN 358
Cdd:TIGR01327 282 TREAQENVATQVAEQVLDALKG---LPVPNAVN 311
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
83-323 4.05e-65

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: 211.24  E-value: 4.05e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  83 HTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrv 162
Cdd:cd12171   53 HFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDG--- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 163 qsveQIREVASGAAR----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDC 238
Cdd:cd12171  130 ----EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGVKKV-SLEELLKRSDV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 239 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 318
Cdd:cd12171  205 VSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLP-ADHPLLKLDNVTL 283

                 ....*
gi 767961783 319 TPHTA 323
Cdd:cd12171  284 TPHIA 288
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
86-321 6.36e-65

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: 210.47  E-value: 6.36e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsv 165
Cdd:cd05303   52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 166 eQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNL 245
Cdd:cd05303  126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLHVPL 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961783 246 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgpLKDAPNLICTPH 321
Cdd:cd05303  204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
89-358 8.49e-61

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: 200.09  E-value: 8.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  89 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETAdstICHILNLYRRntwLYQALREGTRVQSV 165
Cdd:cd12174   42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGAnanAVAELV---IAMMLALSRN---IIQAIKWVTNGDGD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 166 EQIREVASGAAR-----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLG--VQRVYTLQDLLYQSDC 238
Cdd:cd12174  116 DISKGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSveVQRVTSLEELLATADY 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 239 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEpfsfaqgPLKDAPNLIC 318
Cdd:cd12174  196 ITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIA 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767961783 319 TPHTAWYSEQASLEMREAAATEIRRAI-TGRIPeslrNCVN 358
Cdd:cd12174  269 TPHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
64-352 6.89e-58

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: 193.14  E-value: 6.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  64 STQEIHEKVLNEAVGA---MMYHTITLTREDLEKFKA--LRVI-VRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADS 137
Cdd:cd12186   30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEygIKQIaLRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 138 TICHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 216
Cdd:cd12186  109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 217 IErSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 296
Cdd:cd12186  182 LE-KFLLYYD-SLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961783 297 VHESE----PFSFAQGPLKDA--------PNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPES 352
Cdd:cd12186  260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEGGTSEN 327
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
87-334 5.98e-56

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: 187.43  E-value: 5.98e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 166
Cdd:cd12161   59 LPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 QiREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIErSLGVQRVyTLQDLLYQSDCVSLHCNLN 246
Cdd:cd12161  139 G-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK-ALGIEYV-SLDELLAESDIVSLHLPLN 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 247 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYS 326
Cdd:cd12161  209 DETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFAT 288

                 ....*...
gi 767961783 327 EQAsLEMR 334
Cdd:cd12161  289 EEA-MEKR 295
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
49-347 7.86e-56

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: 186.95  E-value: 7.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  49 PILKDLATV-AFCD-AQSTQEIHEKVLN-EAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN 125
Cdd:cd12169   19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 126 IPSAaVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFS 205
Cdd:cd12169   98 TGGG-PTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 206 VIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQAL 285
Cdd:cd12169  168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961783 286 KEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 347
Cdd:cd12169  248 RAGRIAGAALDVFDVEPLP-ADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
PRK13243 PRK13243
glyoxylate reductase; Reviewed
89-360 5.11e-55

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 185.77  E-value: 5.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  89 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQI 168
Cdd:PRK13243  59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAW 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 169 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEH 248
Cdd:PRK13243 139 HPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESDFVSLHVPLTKE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 249 NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWYSEQ 328
Cdd:PRK13243 218 TYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVVLAPHIGSATFE 295
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767961783 329 ASLEMREAAATEIRRAITGRIPESLrncVNKE 360
Cdd:PRK13243 296 AREGMAELVAENLIAFKRGEVPPTL---VNRE 324
PRK08410 PRK08410
2-hydroxyacid dehydrogenase; Provisional
36-347 5.35e-55

2-hydroxyacid dehydrogenase; Provisional


Pssm-ID: 181414  Cd Length: 311  Bit Score: 185.19  E-value: 5.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  36 VALLDGR---DCTVEmpILKDLATVAFCDAQSTQEIHEKVLNEAVgaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVD 112
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 113 IKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSvEQIREVASGAARIRGETLGLIGFGRTG 192
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 193 QAVAVRAKAFGFSVIFYDPylqDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAAR 272
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961783 273 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfAQGPL---KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 347
Cdd:PRK08410 234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
PRK06487 PRK06487
glycerate dehydrogenase; Provisional
61-348 1.79e-54

glycerate dehydrogenase; Provisional


Pssm-ID: 180588  Cd Length: 317  Bit Score: 183.75  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  61 DAQSTQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTIC 140
Cdd:PRK06487  32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 141 HILNLYRRNTWLYQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpyL 213
Cdd:PRK06487 110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 214 QDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGA 293
Cdd:PRK06487 177 GQLPGRPARPDRL-PLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767961783 294 ALDVHESEPfSFAQGPL--KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 348
Cdd:PRK06487 256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
87-329 3.96e-54

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: 183.25  E-value: 3.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 166
Cdd:cd12187   53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 QIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLN 246
Cdd:cd12187  133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 247 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEP--------FSFAQGPLKDA----- 313
Cdd:cd12187  205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelFREDVSPEDLKkllad 284
                        250       260
                 ....*....|....*....|..
gi 767961783 314 ------PNLICTPHTAWYSEQA 329
Cdd:cd12187  285 hallrkPNVIITPHVAYNTKEA 306
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
86-342 4.33e-51

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: 175.33  E-value: 4.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREG---- 159
Cdd:cd12183   55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGnfsl 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 160 ---TRVQsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQS 236
Cdd:cd12183  135 dglLGFD--------------LHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAK-LGVEYV-DLDELLAES 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 237 DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG----PLKD 312
Cdd:cd12183  199 DIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDhsdeIIQD 278
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767961783 313 A--------PNLICTPHTAWYSEQAsleMREAAATEIR 342
Cdd:cd12183  279 DvlarllsfPNVLITGHQAFFTKEA---LTNIAETTLE 313
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
83-335 4.72e-51

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: 175.09  E-value: 4.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  83 HTITLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAvEETADSTICHILNLYRRntwlYQALREGT 160
Cdd:cd12185   52 GKSKISAELLEKLKEAgvKYISTRSIGYDHIDLDAAKELGIKVSNVTYSP-NSVADYTVMLMLMALRK----YKQIMKRA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 161 RVQ--SVEQIRevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslGVQRVyTLQDLLYQSDC 238
Cdd:cd12185  127 EVNdySLGGLQ-----GRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNEEVKK--YAEYV-DLDTLYKESDI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 239 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQ----------- 307
Cdd:cd12185  199 ITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEDGIYYNdrkgdilsnre 278
                        250       260
                 ....*....|....*....|....*....
gi 767961783 308 -GPLKDAPNLICTPHTAWYSEQASLEMRE 335
Cdd:cd12185  279 lAILRSFPNVILTPHMAFYTDQAVSDMVE 307
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
86-366 1.46e-48

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: 168.51  E-value: 1.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALRVIVRI-GSGYDNVDiKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQs 164
Cdd:cd12167   61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 165 veqiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCN 244
Cdd:cd12167  139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSLHAP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 245 LNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLICTPHTAW 324
Cdd:cd12167  214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLP-PDSPLRTLPNVLLTPHIAG 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767961783 325 YSEQASLEMREAAATEIRRAITGRIPeslRNCVNKEFFVTSA 366
Cdd:cd12167  292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
86-321 1.80e-48

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: 167.76  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwLYQALREGTRvqsv 165
Cdd:cd12176   53 QLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARR---LPDRNAAAHR---- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 166 EQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIE--RSLGVQR-VYTLQDLLYQSDCVSLH 242
Cdd:cd12176  126 GIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD------IAekLPLGNARqVSSLEELLAEADFVTLH 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 243 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLICT 319
Cdd:cd12176  200 VPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGEPfssPLQGLPNVILT 279

                 ..
gi 767961783 320 PH 321
Cdd:cd12176  280 PH 281
PRK06932 PRK06932
glycerate dehydrogenase; Provisional
87-329 1.55e-46

glycerate dehydrogenase; Provisional


Pssm-ID: 235890  Cd Length: 314  Bit Score: 163.05  E-value: 1.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIP---SAAVEETADSTIC---HILNLYRRNtwlyqalREGT 160
Cdd:PRK06932  55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTgysSTTVPEHVLGMIFalkHSLMGWYRD-------QLSD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 161 RVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgiERSLGVQRV-YT-LQDLLYQSDC 238
Cdd:PRK06932 128 RWATCKQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREgYTpFEEVLKQADI 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 239 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL----KDAP 314
Cdd:PRK06932 201 VTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLP 279
                        250
                 ....*....|....*
gi 767961783 315 NLICTPHTAWYSEQA 329
Cdd:PRK06932 280 NLLITPHIAWASDSA 294
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
82-339 1.12e-45

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: 161.34  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  82 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTR 161
Cdd:cd05302   69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVS 240
Cdd:cd05302  149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTP 320
Cdd:cd05302  224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302
                        250
                 ....*....|....*....
gi 767961783 321 HTAWYSEQAslEMREAAAT 339
Cdd:cd05302  303 HISGTTLDA--QARYAAGT 319
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
87-338 7.49e-44

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: 155.32  E-value: 7.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsvE 166
Cdd:cd12156   54 LSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------R 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgvQRVYTLQDLLYQSDCVSLHCNLN 246
Cdd:cd12156  128 WPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPY----RYYASLLELAAESDVLVVACPGG 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 247 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGP--LKDAPNLICTPHTAw 324
Cdd:cd12156  204 PATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIA- 278
                        250
                 ....*....|....
gi 767961783 325 yseQASLEMREAAA 338
Cdd:cd12156  279 ---SATVETRRAMG 289
PRK11790 PRK11790
D-3-phosphoglycerate dehydrogenase; Provisional
87-321 8.54e-44

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 158.03  E-value: 8.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALrviVRIGS---GYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQ 163
Cdd:PRK11790  65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNK 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 164 SveqirevASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIER--SLG-VQRVYTLQDLLYQSDCVS 240
Cdd:PRK11790 142 S-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDklPLGnARQVGSLEELLAQSDVVS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLI 317
Cdd:PRK11790 209 LHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDNVI 288

                 ....
gi 767961783 318 CTPH 321
Cdd:PRK11790 289 LTPH 292
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
64-347 1.24e-43

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: 155.14  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  64 STQEIHEKVLNeAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHIL 143
Cdd:cd12157   34 SREELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 144 NLYRRntwlyqaLREGTRVqsveqIREVASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 216
Cdd:cd12157  113 GLGRH-------ILAGDRF-----VRSGKFGGWRpkfygtgLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 217 I-ERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAAL 295
Cdd:cd12157  181 AeEQALNLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAA 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767961783 296 DVHESE-------PFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 347
Cdd:cd12157  260 DVFEMEdwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
63-327 4.37e-43

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: 153.60  E-value: 4.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  63 QSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETADSTI 139
Cdd:cd12179   29 ISREEI-LAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGnrdAVGEHALGML 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 140 CHILNLYRRNTWLYQA---LREGTRvqSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 216
Cdd:cd12179  108 LALFNKLNRADQEVRNgiwDREGNR--GVE-----------LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 217 IERslgVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 296
Cdd:cd12179  175 DAY---AEQV-SLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLD 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767961783 297 VHESEPFSF---AQGP-----LKDAPNLICTPHTA-WYSE 327
Cdd:cd12179  251 VLEYEKASFesiFNQPeafeyLIKSPKVILTPHIAgWTFE 290
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
89-350 3.51e-42

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: 151.24  E-value: 3.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  89 REDLEKFKALRVIVRIGSGYDNVDIKAAGElGIAVCNIP--SAAVEETAdstICHILNLYRRNTWLYQALREGTRVQSVE 166
Cdd:cd12165   52 EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHgnSPAVAEHA---LALILALAKRIVEYDNDLRRGIWHGRAG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 QIREVASgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCV 239
Cdd:cd12165  128 EEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVI--------GVSRSpkedEGADFVGTLSDLdeaLEQADVV 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 240 SLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--------HESEPFSFaqgPLK 311
Cdd:cd12165  196 VVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDPVAPSRY---PFH 272
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 767961783 312 DAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 350
Cdd:cd12165  273 ELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPL 311
PRK07574 PRK07574
formate dehydrogenase; Provisional
87-340 6.99e-41

formate dehydrogenase; Provisional


Pssm-ID: 181041  Cd Length: 385  Bit Score: 149.82  E-value: 6.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  87 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRvqsve 166
Cdd:PRK07574 104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 167 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNL 245
Cdd:PRK07574 179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 246 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTPHTAWY 325
Cdd:PRK07574 259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQP-APADHPWRTMPRNGMTPHISGT 337
                        250
                 ....*....|....*
gi 767961783 326 SEQAslEMREAAATE 340
Cdd:PRK07574 338 TLSA--QARYAAGTR 350
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
89-360 6.98e-40

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: 144.97  E-value: 6.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  89 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN---IPSAAVeetADSTICHILNLYRRnTWLYQALREGTRVQSV 165
Cdd:cd05300   51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNargIFGPPI---AEYVLGYMLAFARK-LPRYARNQAERRWQRR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 166 EQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL-----GVQRVYT---LQDLLYQSD 237
Cdd:cd05300  127 GPVRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEAD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 238 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLI 317
Cdd:cd05300  192 YVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVI 270
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767961783 318 CTPHTAWYSEQaslEMREAA---ATEIRRAITGripESLRNCVNKE 360
Cdd:cd05300  271 ITPHISGDSPS---YPERVVeifLENLRRYLAG---EPLLNVVDKD 310
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
86-335 1.97e-39

(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: 144.36  E-value: 1.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKAL---RVIVRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRR-NTWLYQALREGTR 161
Cdd:cd12184   55 FADKENLEIYKEYgikYVFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHtAYTASRTANKNFK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 VQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSL 241
Cdd:cd12184  134 VDPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKD---VVTFVSLDELLKKSDIISL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 242 HC-NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--HESEPF--SFAQGPLKDA--- 313
Cdd:cd12184  204 HVpYIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvve 283
                        250       260
                 ....*....|....*....|....*...
gi 767961783 314 ------PNLICTPHTAWYSEQASLEMRE 335
Cdd:cd12184  284 klldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK15409 PRK15409
bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional
65-358 1.01e-38

bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional


Pssm-ID: 185307  Cd Length: 323  Bit Score: 142.20  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  65 TQEIHEKVLNEAVGaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILN 144
Cdd:PRK15409  35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 145 LYRRntwlyqALREGTRVQSVEQIREVASG--AARIRGETLGLIGFGRTGQAVAVRAKaFGFSV-IFYDPYLQ-DGIERS 220
Cdd:PRK15409 114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 221 LGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHES 300
Cdd:PRK15409 187 FNARYC-DLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767961783 301 EPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPEslrNCVN 358
Cdd:PRK15409 266 EPLS-VDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEK---NCVN 319
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
86-345 1.45e-36

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: 136.89  E-value: 1.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  86 TLTREDLEKFKALrvIVR-----------------IGS---GYDNVDIKAAGELGIAVCNIP---SAAVeetADSTICHI 142
Cdd:cd12158   28 EITAEDLKDADVL--LVRsvtkvneallegskvkfVGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSAL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 143 LNLYRRNTWLyqalregtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQdgiERSLG 222
Cdd:cd12158  103 LVLAQRQGFS-------------------------LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAEGD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 223 VQRVyTLQDLLYQSDCVSLHCNLNEH----NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVH 298
Cdd:cd12158  155 PGFV-SLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767961783 299 ESEPfsfaqgplkdAPNL-------ICTPHTAWYseqaSLEMREAAATEIRRAI 345
Cdd:cd12158  234 ENEP----------EIDLelldkvdIATPHIAGY----SLEGKARGTEMIYEAL 273
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
98-329 6.83e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 134.87  E-value: 6.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  98 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlYQALREGTRVQSveqIREVASGAAR 177
Cdd:PRK08605  70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRH----FNQIQTKVREHD---FRWEPPILSR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 178 -IRGETLGLIGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSlgVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLIND 255
Cdd:PRK08605 143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATY--VDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 256 FTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFAQGPLKDA--------PNLICTPHTA 323
Cdd:PRK08605 221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                 ....*.
gi 767961783 324 WYSEQA 329
Cdd:PRK08605 301 FYTDAA 306
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
176-358 2.86e-35

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: 132.47  E-value: 2.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 176 ARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS------LGVQRVYTLQDLLYQSDCVSLHCNLNEHN 249
Cdd:cd12180  131 GSLAGSTLGIVGFGAIGQALARRALALGMRVL--------ALRRSgrpsdvPGVEAAADLAELFARSDHLVLAAPLTPET 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 250 HHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQA 329
Cdd:cd12180  203 RHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDG 281
                        170       180
                 ....*....|....*....|....*....
gi 767961783 330 SLEMREAAATEIRRAITGRipeSLRNCVN 358
Cdd:cd12180  282 RRNLADRFLENLARYRAGQ---PLHDLVD 307
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
91-328 1.49e-34

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: 130.78  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  91 DLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTrVQSVEQIRE 170
Cdd:cd12155   54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKK-WKMDSSLLE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 171 VAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVSLHC 243
Cdd:cd12155  133 LY-------GKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 244 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 323
Cdd:cd12155  198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                 ....*
gi 767961783 324 WYSEQ 328
Cdd:cd12155  277 GVSEH 281
PLN02928 PLN02928
oxidoreductase family protein
76-350 2.93e-34

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 130.57  E-value: 2.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  76 AVGAMMyhtiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAV---EETADSTICHILNLYRRNTWL 152
Cdd:PLN02928  65 CVPKMM----RLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTgnaASCAEMAIYLMLGLLRKQNEM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 153 YQALRegtrvqsveqirevasgaARIRGETLG---------LIGFGRTGQAVAVRAKAFGFSVIFY------DPYLQDGI 217
Cdd:PLN02928 141 QISLK------------------ARRLGEPIGdtlfgktvfILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 218 ERSLGVQRVY------TLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIR 291
Cdd:PLN02928 203 PNGDVDDLVDekggheDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLG 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767961783 292 GAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 350
Cdd:PLN02928 283 GLAIDVAWSEPFD-PDDPILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPL 340
PLN02306 PLN02306
hydroxypyruvate reductase
107-349 2.06e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.51  E-value: 2.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 107 GYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREvasgAARIRGETLGLI 186
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 187 GFGRTGQAVA-VRAKAFGFSVIFYDPY---------------LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNH 250
Cdd:PLN02306 172 GAGRIGSAYArMMVEGFKMNLIYYDLYqstrlekfvtaygqfLKANGEQPVTWKRASSMEEVLREADVISLHPVLDKTTY 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 251 HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAwyseQAS 330
Cdd:PLN02306 252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SAS 325
                        250
                 ....*....|....*....
gi 767961783 331 LEMREAAATEIRRAITGRI 349
Cdd:PLN02306 326 KWTREGMATLAALNVLGKL 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
82-340 4.94e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 114.18  E-value: 4.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  82 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTR 161
Cdd:PLN03139 106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVS 240
Cdd:PLN03139 186 -----NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVVV 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTP 320
Cdd:PLN03139 261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMTP 339
                        250       260
                 ....*....|....*....|
gi 767961783 321 HTAWYSEQASLemREAAATE 340
Cdd:PLN03139 340 HISGTTIDAQL--RYAAGVK 357
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
92-329 3.61e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 110.77  E-value: 3.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  92 LEKFkALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlYQALREgtRVQSVEQIREV 171
Cdd:PRK12480  65 LESY-GIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRR----FPDIER--RVQAHDFTWQA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 172 ASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSLHCNLNEHNHH 251
Cdd:PRK12480 138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 252 LINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFA---QGPLKDAP---------NLICT 319
Cdd:PRK12480 215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAYFTndwTNKDIDDKtllelieheRILVT 294
                        250
                 ....*....|
gi 767961783 320 PHTAWYSEQA 329
Cdd:PRK12480 295 PHIAFFSDEA 304
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
88-353 2.67e-23

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: 99.20  E-value: 2.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  88 TREDLEKFKALRVIVRIGSGYDNVdIKAAGElGIAVCNipSAAVEE--TADSTICHILNLYRRNTWLYQALREG----TR 161
Cdd:cd12166   51 VLEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGLPRFVRAQARGrwepRR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 162 VQSVEqirevasgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDLLYQSD 237
Cdd:cd12166  127 TPSLA-------------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEAD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 238 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLI 317
Cdd:cd12166  186 VVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEPLP-PGHPLWSAPGVL 263
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767961783 318 CTPHTAWYSEQASLEMREAAATEIRRAITGRIPESL 353
Cdd:cd12166  264 ITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
90-358 3.04e-23

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: 99.11  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  90 EDLEKFKALRVIVRIGSGYDNVDiKAAGELGIAVCNIPSAAVEET-ADSTICHILNLYRRntwlYQALREGTRVQSVEQI 168
Cdd:cd12164   51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRD----MDRYAAQQRRGVWKPL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 169 REVASGAARIrgetlGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL----GVQRVY---TLQDLLYQSDCVsl 241
Cdd:cd12164  126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkdieGVTCFHgeeGLDAFLAQTDIL-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 242 hCNL---NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 318
Cdd:cd12164  191 -VCLlplTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTV 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767961783 319 TPHTawyseqASLEMREAAATEIRRAIT-GRIPESLRNCVN 358
Cdd:cd12164  269 TPHI------AAITDPDSAAAQVAENIRrLEAGEPLPNLVD 303
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
168-323 5.02e-21

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: 92.71  E-value: 5.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 168 IREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVS 240
Cdd:cd12159  113 PAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQG-PLKDAPNLICT 319
Cdd:cd12159  185 LAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALIT 262

                 ....
gi 767961783 320 PHTA 323
Cdd:cd12159  263 PHVA 266
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
187-355 1.60e-20

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: 91.28  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 187 GFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSLGVQ---RVYT---LQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQ 260
Cdd:cd12160  150 GFGSIGQRLAPLLTALGARVT--------GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAA 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 261 MRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMreaAATE 340
Cdd:cd12160  222 LPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLP-ASSPLWDAPNLILTPHAAGGRPQGAEEL---IAEN 297
                        170
                 ....*....|....*
gi 767961783 341 IRRAITGRipeSLRN 355
Cdd:cd12160  298 LRAFLAGG---PLRN 309
PRK00257 PRK00257
erythronate-4-phosphate dehydrogenase; Validated
84-326 6.58e-20

erythronate-4-phosphate dehydrogenase; Validated


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 90.87  E-value: 6.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  84 TIT-LTREDLEKFKaLRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLyrrntwlyqALREGtrv 162
Cdd:PRK00257  45 SVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTL---------AEREG--- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 163 qsveqirevasgaARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqrvyTLQDLLYQSDCVSLH 242
Cdd:PRK00257 112 -------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFV----SLERILEECDVISLH 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 243 CNLN-EHNH---HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGPLKDAPN-LI 317
Cdd:PRK00257 175 TPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTI 250

                 ....*....
gi 767961783 318 CTPHTAWYS 326
Cdd:PRK00257 251 ATPHIAGYS 259
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
150-327 1.35e-19

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: 89.25  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 150 TWL-----YQALREGTRVQSVEQiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFY--------------- 209
Cdd:cd12163   99 TWLvlshhFLQYIELQKEQTWGR-RQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkddg 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 210 -------DPylqDGI--------ERSLGVQRVYTLQ-DLLyqsdCVSLhcNLNEHNHHLIN--DFTIKQMRqGAFLVNAA 271
Cdd:cd12163  178 yivpgtgDP---DGSipsawfsgTDKASLHEFLRQDlDLL----VVSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIA 247
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767961783 272 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSE 327
Cdd:cd12163  248 RGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAPNVIITPHVSWQTQ 302
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
63-329 1.01e-15

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: 76.96  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  63 QSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYD----NVDIKAAGELGIAVCNIPSAAVEETADST 138
Cdd:cd12170   35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 139 ICH---ILNLYRRNTWLYQALRegtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD 215
Cdd:cd12170  114 ISElirLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 216 GIERSlGVqRVYTLQDLLYQSDCVSLHCNlneHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGrirGAAL 295
Cdd:cd12170  174 DAEAK-GI-RYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767961783 296 DVHESEPfSFAQGPLKDAPNLICTPHTAWYSEQA 329
Cdd:cd12170  246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
79-349 1.12e-13

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 71.86  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  79 AMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWlyqALRE 158
Cdd:PRK15438  40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 159 gtrvqsveqirevasgaarirgETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD-GIERSLgvqrvYTLQDLLYQSD 237
Cdd:PRK15438 117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 238 CVSLHCNLNEHNH----HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDA 313
Cdd:PRK15438 170 ILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKV 248
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767961783 314 PnlICTPHTAWYseqaSLEMREAAATEIRRAITGRI 349
Cdd:PRK15438 249 D--IGTPHIAGY----TLEGKARGTTQVFEAYSKFI 278
PRK06436 PRK06436
glycerate dehydrogenase; Provisional
180-360 5.11e-13

glycerate dehydrogenase; Provisional


Pssm-ID: 235800  Cd Length: 303  Bit Score: 69.14  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 180 GETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGierslGVQRVY-TLQDLLYQSDCVSLHCNLNEHNHHLINDFTI 258
Cdd:PRK06436 122 NKSLGILGYGGIGRRVALLAKAFGMNIYAYTRSYVND-----GISSIYmEPEDIMKKSDFVLISLPLTDETRGMINSKML 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 259 KQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPlkdaPNLICTPHTAwysEQASLEMREAAA 338
Cdd:PRK06436 197 SLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHVA---GGMSGEIMQPAV 269
                        170       180
                 ....*....|....*....|..
gi 767961783 339 TEIRRAITGRIPESLRNCVNKE 360
Cdd:PRK06436 270 ALAFENIKNFFEGKPKNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
91-316 9.31e-12

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: 65.33  E-value: 9.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  91 DLEKFKALRVIVRIGSGYDNVDIK-AAGELGIAVCNIP-SAAVEETADSTIChilnlyrrntwLYQALREGTRVQSVeQI 168
Cdd:cd12154   81 ALIQKLGDRLLFTYTIGADHRDLTeALARAGLTAIAVEgVELPLLTSNSIGA-----------GELSVQFIARFLEV-QQ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 169 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVSLHCNLNE 247
Cdd:cd12154  149 PGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALeQLEELGGKNVEELEEALAEADVIVTTTLLPG 228
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961783 248 HNHHLINDFT-IKQMRQGAFLVNAARG-GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNL 316
Cdd:cd12154  229 KRAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional
96-346 1.52e-10

bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional


Pssm-ID: 185366  Cd Length: 312  Bit Score: 61.74  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783  96 KALRVIVRIGSGYDNV--DIKAAGELGIAvcNIPSAAVEETA------DSTICHILNLYRRNTwLYQALREGTRVQSVEQ 167
Cdd:PRK15469  55 RDLKAVFALGAGVDSIlsKLQAHPEMLDP--SVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 168 IRevasgaariRGE-TLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD--GIERSLGVQRvytLQDLLYQSDC-VSLHC 243
Cdd:PRK15469 132 YH---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGREE---LSAFLSQTRVlINLLP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961783 244 NLNEhNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 323
Cdd:PRK15469 200 NTPE-TVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVA 277
                        250       260
                 ....*....|....*....|...
gi 767961783 324 WYSEQASlemreaAATEIRRAIT 346
Cdd:PRK15469 278 AVTRPAE------AVEYISRTIA 294
 
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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