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Conserved domains on  [gi|169773285|ref|XP_001821111|]
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unnamed protein product [Aspergillus oryzae RIB40]

Protein Classification

2-hydroxyacid dehydrogenase( domain architecture ID 10187446)

NAD(+)-dependent 2-hydroxyacid dehydrogenase specific to D-isomers, similar to D-lactate dehydrogenase, which converts D-lactate to pyruvate

EC:  1.1.1.28
Gene Ontology:  GO:0070404|GO:0008720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-330 0e+00

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: 570.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYG---HELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd12183   78 GFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGL 239
Cdd:cd12183  158 AFARILKGFGCRVLAYDPYPNPELAKLGvEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 240 VNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLED 319
Cdd:cd12183  238 IDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDD 317

                        330
                 ....*....|.
gi 169773285 320 FVLKRTCKNSL 330
Cdd:cd12183  318 FEAGKPLKNEV 328
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-330 0e+00

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: 570.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYG---HELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd12183   78 GFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGL 239
Cdd:cd12183  158 AFARILKGFGCRVLAYDPYPNPELAKLGvEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 240 VNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLED 319
Cdd:cd12183  238 IDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDD 317

                        330
                 ....*....|.
gi 169773285 320 FVLKRTCKNSL 330
Cdd:cd12183  318 FEAGKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-328 6.43e-118

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 343.22  E-value: 6.43e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDAtLRKHHpalCEITYHSFALS-SETVSLAQDSDAVCVFVNDQLDAPVLETLyaNGVRAILLRC 79
Cdd:COG1052    1 KPILVLDPRTLPDEVLER-LEAEH---FEVTVYEDETSpEELAERAAGADAVITNGKDPIDAEVLEAL--PGLKLIANRG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGRI 158
Cdd:COG1052   75 VGYDNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 159 GLAFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRG 237
Cdd:COG1052  155 GQAVARRAKGFGMKVLYYDRSPKPEVAELGaEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 238 GLVNTKAVINALKSGQLGGVALDVYEEEGALfyNDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNL 317
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPP--PDH-----------PLLSLPNVVLTPHIASATEEAREAMAELALDNL 301

                        330
                 ....*....|.
gi 169773285 318 EDFVLKRTCKN 328
Cdd:COG1052  302 LAFLAGEPPPN 312
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 29-328 1.32e-76

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: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 237.96  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   29 EITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLEtlYANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAV 108
Cdd:pfam00389  19 EVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLE--AAPKLKVIGRAGVGVDNVDLDAATERGILVTNAPGYNTESV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  109 AEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYG 188
Cdd:pfam00389  97 AELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFGMGVVAYDPYPNPERAEAG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  189 EFVELGDLLAQSDVVSLHcpltegtrHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAL 268
Cdd:pfam00389 177 GVEVLSLLLLLLDLPESD--------DVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAALDALLEEGIA 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  269 FYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFVLKRTCKN 328
Cdd:pfam00389 249 AAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPAN 308
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 1-306 1.79e-68

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 217.69  E-value: 1.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:PRK08605   2 TKIKIMSVRDEDAPYIKAWAEKHH---VEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIKQIAQRSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVAliQTLN--RKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGR 157
Cdd:PRK08605  79 GFDTYDLELATKYNLIISNVPSYSPESIAEFTVT--QAINlvRHFNQIQTKVREHDFRWEpPILSRSIKDLKVAVIGTGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 158 IGLAFAKIL-HGFGCKLVAYDPFGGEEFKKYGEFVE-LGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTS 235
Cdd:PRK08605 157 IGLAVAKIFaKGYGSDVVAYDPFPNAKAATYVDYKDtIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCA 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169773285 236 RGGLVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEAL 306
Cdd:PRK08605 237 RGSLVDTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTINDPLLESLINREDVILTPHIAFYTDAAV 307
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-330 0e+00

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: 570.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYG---HELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd12183   78 GFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGL 239
Cdd:cd12183  158 AFARILKGFGCRVLAYDPYPNPELAKLGvEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 240 VNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLED 319
Cdd:cd12183  238 IDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDD 317

                        330
                 ....*....|.
gi 169773285 320 FVLKRTCKNSL 330
Cdd:cd12183  318 FEAGKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-328 6.43e-118

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 343.22  E-value: 6.43e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDAtLRKHHpalCEITYHSFALS-SETVSLAQDSDAVCVFVNDQLDAPVLETLyaNGVRAILLRC 79
Cdd:COG1052    1 KPILVLDPRTLPDEVLER-LEAEH---FEVTVYEDETSpEELAERAAGADAVITNGKDPIDAEVLEAL--PGLKLIANRG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGRI 158
Cdd:COG1052   75 VGYDNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 159 GLAFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRG 237
Cdd:COG1052  155 GQAVARRAKGFGMKVLYYDRSPKPEVAELGaEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 238 GLVNTKAVINALKSGQLGGVALDVYEEEGALfyNDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNL 317
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPP--PDH-----------PLLSLPNVVLTPHIASATEEAREAMAELALDNL 301

                        330
                 ....*....|.
gi 169773285 318 EDFVLKRTCKN 328
Cdd:COG1052  302 LAFLAGEPPPN 312
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 1-328 5.78e-113

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: 331.42  E-value: 5.78e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12186    1 MKILMYNVRDDEKPYIEEWAKEHP---VEVDTTTELLTPETVDLAKGYDGVVVQQTLPYDEEVYEKLAEYGIKQIALRSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGRIG 159
Cdd:cd12186   78 GVDMIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGDFRWApGLIGREIRDLTVGIIGTGRIG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 160 LAFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGG 238
Cdd:cd12186  158 SAAAKIFKGFGAKVIAYDPYPNPELEKFLlYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 239 LVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLE 318
Cdd:cd12186  238 LVDTKALIDALDSGKIAGAALDTYENETGYFNKDWSGKEIEDEVLKELIAMPNVLITPHIAFYTDTAVKNMVEISLDDAL 317

                        330
                 ....*....|
gi 169773285 319 DFVLKRTCKN 328
Cdd:cd12186  318 EIIEGGTSEN 327
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
 1-326 7.26e-105

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: 310.29  E-value: 7.26e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12185    1 MKIFAYGVRPDELEYFEKFAKEYN---VEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAGVKYISTRSI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVpSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd12185   78 GYDHIDLDAAKELGIKVSNV-TYSPNSVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYDPFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLV 240
Cdd:cd12185  157 AVIKNLSGFGCKILAYDPYPNEEVKKYAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 241 NTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12185  237 DTEALIEGLESGKIGGAALDVIEGEDGIYYNDRKGDILSNRELAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLVAF 316


                 ....*.
gi 169773285 321 VLKRTC 326
Cdd:cd12185  317 EKGGEN 322
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-326 9.54e-105

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 [Multi-domain]  Cd Length: 323  Bit Score: 310.00  E-value: 9.54e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHPalcEITYHSFALSS-ETVSLAQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRC 79
Cdd:cd01619    1 MKVLIYDYRDDELEIEKEILKAGGV---DVEIVTYLLNDdETAELAKGADAILTAFTDKIDAELLDK--APGLKFISLRA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIG 159
Cdd:cd01619   76 TGYDNIDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRELEDQTVGVVGTGKIG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 160 LAFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGG 238
Cdd:cd01619  156 RAVAQRAKGFGMKVIAYDPFRNPELEDKGvKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGS 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 239 LVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLE 318
Cdd:cd01619  236 LVDTEALIEALDSGKIFGAGLDVLEDETPDLLKDLEGEIFKDALNALLGRRPNVIITPHTAFYTDDALKNMVEISCENIV 315


                 ....*...
gi 169773285 319 DFVLKRTC 326
Cdd:cd01619  316 DFLEGEEE 323
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 1-330 7.45e-93

(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: 279.95  E-value: 7.45e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:cd12184    1 MKIICYGVRPVEKPIFEKLNKKFG---YDLTLVEEYLNDENVHLAKGHDAVIVRGNCFADKENLEIYKEYGIKYVFTRTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFL-GRTLYGKTVGVVGVGRIG 159
Cdd:cd12184   78 GFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNFKVDPFMfSKEIRNSTVGIIGTGRIG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 160 LAFAKILHGFGCKLVAYDPFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTR-HVINDENLGRMKKGALLVNTSRGG 238
Cdd:cd12184  158 LTAAKLFKGLGAKVIGYDIYPSDAAKDVVTFVSLDELLKKSDIISLHVPYIKGKNdKLINKEFISKMKDGAILINTARGE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 239 LVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMT-FPNVLVCGHQAFFTEEALSEIAGVTLGNL 317
Cdd:cd12184  238 LQDEEAILEALESGKLAGFGTDVLNNEKEIFFKDFDGDKIEDPVVEKLLDlYPRVLLTPHIGSYTDEALSNMIETSYENL 317

                        330
                 ....*....|...
gi 169773285 318 EDFVLKRTCKNSL 330
Cdd:cd12184  318 KEYLETGDCKNKI 330
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 2-321 6.14e-92

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 [Multi-domain]  Cd Length: 329  Bit Score: 277.62  E-value: 6.14e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   2 KLAVFSAKSYDKHYFdATLRKHHPALCEityhSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLyaNGVRAILLRCAG 81
Cdd:cd12187    1 KIVFFETEEWEQEYF-QELLPGHKVVFT----SQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKL--PRLKLIATRSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  82 FNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLA 161
Cdd:cd12187   74 FDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 162 FAKILHGFGCKLVAYDPFGGEEF-KKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGL 239
Cdd:cd12187  154 VARIARGFGMKVLAYDVVPDEELaERLGfRYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 240 VNTKAVINALKSGQLGGVALDVYEEEGAL---FYNDHSGEIIHDDVLM----RLMTFPNVLVCGHQAFFTEEALSEIAGV 312
Cdd:cd12187  234 VDTEALVRALKEGKLAGAGLDVLEQEEVLreeAELFREDVSPEDLKKLladhALLRKPNVIITPHVAYNTKEALERILDT 313


                 ....*....
gi 169773285 313 TLGNLEDFV 321
Cdd:cd12187  314 TVENIKAFA 322
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 15-320 1.68e-85

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 [Multi-domain]  Cd Length: 302  Bit Score: 260.25  E-value: 1.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  15 YFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLEtlYANGVRAILLRCAGFNNINLQVAEDLG 94
Cdd:cd05198   12 EALEALEATG---FEVIVADDLLADELEALLADADALIVSSTTPVTAEVLA--KAPKLKFIQVAGAGVDNIDLDAAKKRG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  95 FFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNL-EGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKL 173
Cdd:cd05198   87 ITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWGWLwAGFPGYELEGKTVGIVGLGRIGQRVAKRLQAFGMKV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 174 VAYDPFG--GEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKS 251
Cdd:cd05198  167 LYYDRTRkpEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDALLRALKS 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169773285 252 GQLGGVALDVYEEEGALFynDHSgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd05198  247 GKIAGAALDVFEPEPLPA--DHP-----------LLELPNVILTPHIAGYTEEARERMAEIAVENLERF 302
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 29-328 1.32e-76

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: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 237.96  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   29 EITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLEtlYANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAV 108
Cdd:pfam00389  19 EVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLE--AAPKLKVIGRAGVGVDNVDLDAATERGILVTNAPGYNTESV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  109 AEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYG 188
Cdd:pfam00389  97 AELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFGMGVVAYDPYPNPERAEAG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  189 EFVELGDLLAQSDVVSLHcpltegtrHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAL 268
Cdd:pfam00389 177 GVEVLSLLLLLLDLPESD--------DVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAALDALLEEGIA 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  269 FYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFVLKRTCKN 328
Cdd:pfam00389 249 AAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPAN 308
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 28-330 1.48e-75

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 235.09  E-value: 1.48e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  28 CEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEA 107
Cdd:COG0111   23 IEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAA--APNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 108 VAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTvgvvgvgRIGLAFAKILHGFGCKLVAYDPFGGEEFKK- 186
Cdd:COG0111  101 VAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTvgivglgRIGRAVARRLRAFGMRVLAYDPSPKPEEAAd 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 187 --YGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEE 264
Cdd:COG0111  181 lgVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAALDVFEP 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169773285 265 EGALfyNDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFVLKRTCKNSL 330
Cdd:COG0111  261 EPLP--ADS-----------PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPLRNLV 313
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 40-309 6.69e-75

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 [Multi-domain]  Cd Length: 312  Bit Score: 233.56  E-value: 6.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  40 ETVSLAQDSDAVCVFVNdQLDAPVLETLyaNGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTL 119
Cdd:cd05299   37 ELIEAAADADALLVQYA-PVTAEVIEAL--PRLKVIVRYGVGVDNVDVAAATERGIPVCNVPDYCTEEVADHALALILAL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 120 NRKTHRAFNRVREGNFNLEGFLG-RTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYG--EFVELGDL 196
Cdd:cd05299  114 ARKLPFLDRAVRAGGWDWTVGGPiRRLRGLTLGLVGFGRIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGgvRVVSLDEL 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 197 LAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAlfynDHSGE 276
Cdd:cd05299  194 LARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGGLVDEAALARALKSGRIAGAALDVLEEEPP----PADSP 269

                        250       260       270
                 ....*....|....*....|....*....|...
gi 169773285 277 IIHddvlmrlmtFPNVLVCGHQAFFTEEALSEI 309
Cdd:cd05299  270 LLS---------APNVILTPHAAWYSEESLAEL 293
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 11-320 1.77e-72

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 [Multi-domain]  Cd Length: 306  Bit Score: 226.99  E-value: 1.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  11 YDKHYFDAtLRKHHpalCEITYHSF--ALSSET-VSLAQDSDAVCVFVnDQLDAPVLETlyANGVRAILLRCAGFNNINL 87
Cdd:cd12172   12 YSEEAKEL-LEAAG---FEVVLNPLgrPLTEEElIELLKDADGVIAGL-DPITEEVLAA--APRLKVISRYGVGYDNIDL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  88 QVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNleGFLGRTLYGKTVGVVGVGRIGLAFAKILH 167
Cdd:cd12172   85 EAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWD--RPVGTELYGKTLGIIGLGRIGKAVARRLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 168 GFGCKLVAYDPFGGEEFKK--YGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAV 245
Cdd:cd12172  163 GFGMKVLAYDPYPDEEFAKehGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEAL 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169773285 246 INALKSGQLGGVALDVYEEEgalfyndhsgEIIHDDvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12172  243 YEALKSGRIAGAALDVFEEE----------PPPADS---PLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 20-321 6.54e-71

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 [Multi-domain]  Cd Length: 311  Bit Score: 223.22  E-value: 6.54e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  20 LRKHHPAL--CEITYhsfaLSSETVSLAQDSDA-VCVF-VNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGF 95
Cdd:cd12175   16 LRALLPPApgVEVVT----AAELDEEAALLADAdVLVPgMRKVIDAELLAA--APRLRLIQQPGVGLDGVDLEAATARGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  96 FVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGN-FNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLV 174
Cdd:cd12175   90 PVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGRwGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 175 AYDPF---GGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKS 251
Cdd:cd12175  170 YYDRFrdpEAEEKDLGVRYVELDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRS 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 252 GQLGGVALDVYEEEGALfyNDHSgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12175  250 GHLAGAGLDVFWQEPLP--PDDP-----------LLRLDNVILTPHIAGVTDESYQRMAAIVAENIARLL 306
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 40-310 2.33e-70

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 [Multi-domain]  Cd Length: 304  Bit Score: 221.52  E-value: 2.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  40 ETVSLAQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTL 119
Cdd:cd12173   33 ELLAIIADADALIVRSATKVTAEVIEA--APRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLAL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 120 NRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPF-GGEEFKKYG-EFVELGDLL 197
Cdd:cd12173  111 ARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYiSAERAAAGGvELVSLDELL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 198 AQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAlfYNDHsgei 277
Cdd:cd12173  191 AEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPP--PADS---- 264

                        250       260       270
                 ....*....|....*....|....*....|...
gi 169773285 278 ihddvlmRLMTFPNVLVCGHQAFFTEEALSEIA 310
Cdd:cd12173  265 -------PLLGLPNVILTPHLGASTEEAQERVA 290
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 1-306 1.79e-68

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 217.69  E-value: 1.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDKHYFDATLRKHHpalCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCA 80
Cdd:PRK08605   2 TKIKIMSVRDEDAPYIKAWAEKHH---VEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIKQIAQRSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVAliQTLN--RKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGR 157
Cdd:PRK08605  79 GFDTYDLELATKYNLIISNVPSYSPESIAEFTVT--QAINlvRHFNQIQTKVREHDFRWEpPILSRSIKDLKVAVIGTGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 158 IGLAFAKIL-HGFGCKLVAYDPFGGEEFKKYGEFVE-LGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTS 235
Cdd:PRK08605 157 IGLAVAKIFaKGYGSDVVAYDPFPNAKAATYVDYKDtIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCA 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169773285 236 RGGLVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEAL 306
Cdd:PRK08605 237 RGSLVDTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTINDPLLESLINREDVILTPHIAFYTDAAV 307
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
 39-321 1.90e-64

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 [Multi-domain]  Cd Length: 309  Bit Score: 206.48  E-value: 1.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  39 SETVSLAQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQT 118
Cdd:cd05301   35 EELLEAAKGADGLLCTLTDKIDAELLDA--APPLKVIANYSVGYDHIDVDAAKARGIPVTNTPDVLTDATADLAFALLLA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 119 LNRKTHRAFNRVREGNFN---LEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYG--EFVEL 193
Cdd:cd05301  113 AARRVVEGDRFVRAGEWKgwsPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGMKILYHNRSRKPEAEEELgaRYVSL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 194 GDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEgalfyndh 273
Cdd:cd05301  193 DELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPE-------- 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 169773285 274 sgEIIHDDvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd05301  265 --PLPADH---PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVL 307
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 26-321 1.74e-62

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 [Multi-domain]  Cd Length: 307  Bit Score: 201.53  E-value: 1.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  26 ALCEITYHSFALSSETVSLAQDSDAVcvFVND-QLDAPVLETLYAngVRAILLRCAGFNNINLQVAEDLGFFVANVPSYS 104
Cdd:cd12162   23 FLGELTVYDRTSPEEVVERIKDADIV--ITNKvVLDAEVLAQLPN--LKLIGVLATGYNNVDLAAAKERGITVTNVPGYS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 105 PEAVAEFAVALIQTLNRKTHRAFNRVREG------NFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDP 178
Cdd:cd12162   99 TDSVAQHTFALLLALARLVAYHNDVVKAGewqkspDFCFWDYPIIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAER 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 179 FGGEEFKKygEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVA 258
Cdd:cd12162  179 KGAPPLRE--GYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAG 256

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169773285 259 LDVYEEEgalfyndhsgEIIHDDVLMRLMtfPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12162  257 LDVLSQE----------PPRADNPLLKAA--PNLIITPHIAWASREARQRLMDILVDNIKAFL 307
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 39-321 7.02e-60

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 195.23  E-value: 7.02e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  39 SETVSLAQDSDAVCVFVNDQLDAPVLEtlYANGVRAILLRCAGFNNINLQVAEDLGFFVANVP-SYSPEAVAEFAVALIQ 117
Cdd:cd12177   39 KALAEKLKGYDIIIASVTPNFDKEFFE--YNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPgAVERDAVAEHAVALIL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 118 TLNRKTHRAFNRVREGNFNLEG-FLGRTLYGKTVGVVGVGRIGLAFAKILH-GFGCKLVAYDPFGGEEF--KKYGEFVEL 193
Cdd:cd12177  117 TVLRKINQASEAVKEGKWTERAnFVGHELSGKTVGIIGYGNIGSRVAEILKeGFNAKVLAYDPYVSEEVikKKGAKPVSL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 194 GDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE--GAlfyn 271
Cdd:cd12177  197 EELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEpiKA---- 272

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 169773285 272 DHSgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12177  273 DHP-----------LLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDFL 311
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 47-320 9.50e-60

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 [Multi-domain]  Cd Length: 301  Bit Score: 194.29  E-value: 9.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  47 DSDAVCVFVNDQLDAPVLETlyANGVRAILlRCA-GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHR 125
Cdd:cd05303   41 DYDVLIVRSRTKVTKEVIDA--AKNLKIIA-RAGvGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 126 AFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKY--GEFVELGDLLAQSDVV 203
Cdd:cd05303  118 ANREMKLGKWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVElgVKTVSLEELLKNSDFI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 204 SLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGALFyndhsgeiihddvl 283
Cdd:cd05303  198 SLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPG-------------- 263

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 169773285 284 MRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd05303  264 SKLLELPNVSLTPHIGASTKEAQERIGEELANKIIEF 300
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
 2-306 5.25e-59

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 193.21  E-value: 5.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   2 KLAVFSAKSYDKhyfDATLRKHHPALCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCAG 81
Cdd:PRK12480   3 KIMFFGTRDYEK---EMALNWGKKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKLESYGIKQIAQRTAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  82 FNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEG-FLGRTLYGKTVGVVGVGRIGL 160
Cdd:PRK12480  80 FDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTWQAeIMSKPVKNMTVAIIGTGRIGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYD--PFGGEEFKKYGEFVElgDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGG 238
Cdd:PRK12480 160 ATAKIYAGFGATITAYDayPNKDLDFLTYKDSVK--EAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGA 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169773285 239 LVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEAL 306
Cdd:PRK12480 238 VINTPDLIAAVNDGTLLGAAIDTYENEAAYFTNDWTNKDIDDKTLLELIEHERILVTPHIAFFSDEAV 305
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 113-299 7.70e-58

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: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 185.01  E-value: 7.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  113 VALIQTLNRKTHRAFNRVREGNFNLE-GFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFG--GEEFKKYG- 188
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWASPdALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPkpEEEEEELGa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  189 EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAL 268
Cdd:pfam02826  81 RYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPLP 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 169773285  269 fyNDHsgeiihddvlmRLMTFPNVLVCGHQA 299
Cdd:pfam02826 161 --ADH-----------PLLDLPNVILTPHIA 178
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 34-321 3.38e-57

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 [Multi-domain]  Cd Length: 310  Bit Score: 187.75  E-value: 3.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  34 SFALSSETVSLAQDSDAVCVFVNDQL-----DAPVLETLYANGVRAILLRC----------AGFNNINLQVAEDLGFFVA 98
Cdd:cd12171   15 PFEDLQEVILVVEKSGPEAVEPEEELlealkDADILITHFAPVTKKVIEAApklkligvcrGGPENVDVEAATERGIPVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  99 NVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEG----FLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLV 174
Cdd:cd12171   95 NTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDGEWRKDYynydGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 175 AYDPF-GGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSG 252
Cdd:cd12171  175 VYDPYvDPEKIEADGvKKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEG 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169773285 253 QLGGVALDVYEEEGalfyndhsgeiIHDDvlMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12171  255 KIGGAALDVFPEEP-----------LPAD--HPLLKLDNVTLTPHIAGATRDVAERSPEIIAEELKRYL 310
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 81-321 7.67e-57

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 [Multi-domain]  Cd Length: 315  Bit Score: 187.04  E-value: 7.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNlEGFLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd12161   79 GVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTK-AGLIGRELAGKTVGIVGTGAIGL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAYDPFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGL 239
Cdd:cd12161  158 RVARLFKAFGCKVLAYSRSEKEEAKALGiEYVSLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 240 VNTKAVINALKSGQLGGVALDVYEEEGALfYNDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLED 319
Cdd:cd12161  238 VDNEALADALNEGKIAGAGIDVFDMEPPL-PADY-----------PLLHAPNTILTPHVAFATEEAMEKRAEIVFDNIEA 305


                 ..
gi 169773285 320 FV 321
Cdd:cd12161  306 WL 307
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 28-320 1.16e-54

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 [Multi-domain]  Cd Length: 317  Bit Score: 181.67  E-value: 1.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  28 CEITYHSFA--LSSETV--SLAqDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSY 103
Cdd:cd12178   21 FEVTYYDGLglISKEELleRIA-DYDALITPLSTPVDKEIIDA--AKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 104 SPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEG---FLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDP-- 178
Cdd:cd12178   98 STEPTAELTFGLILALARRIAEGDRLMRRGGFLGWAplfFLGHELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRhr 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 179 FGGEEFKKYG-EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGV 257
Cdd:cd12178  178 LSEETEKELGaTYVDLDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGA 257

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169773285 258 ALDVYEEEgalfyndhsgeiihDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12178  258 ALDVFEFE--------------PEVSPELKKLDNVILTPHIGNATVEARDAMAKEAADNIISF 306
PRK13243 PRK13243
glyoxylate reductase; Reviewed
 45-320 1.18e-54

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 181.92  E-value: 1.18e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  45 AQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTH 124
Cdd:PRK13243  43 VRDVDALVTMLSERIDCEVFEA--APRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 125 RAFNRVREGNFNLEG-------FLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKY--GEFVELGD 195
Cdd:PRK13243 121 EADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKElgAEYRPLEE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 196 LLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGalfYNDHSg 275
Cdd:PRK13243 201 LLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEP---YYNEE- 276

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 169773285 276 eiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:PRK13243 277 ----------LFSLKNVVLAPHIGSATFEAREGMAELVAENLIAF 311
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 39-289 2.37e-54

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 [Multi-domain]  Cd Length: 318  Bit Score: 180.95  E-value: 2.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  39 SETVSLAQDSDAVCVFVNDQLDAPVLetlyANGVRAILLRCA--GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALI 116
Cdd:cd12157   36 EELLRRCKDADGLMAFMPDRIDADFL----DACPRLKIIACAlkGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 117 QTLNRKTHRAFNRVREGNFN--LEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFG--GEEFKKYG-EFV 191
Cdd:cd12157  112 IGLGRHILAGDRFVRSGKFGgwRPKFYGTGLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPldQAEEQALNlRRV 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 192 ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYE-EEGALfy 270
Cdd:cd12157  192 ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEmEDWAR-- 269

                        250
                 ....*....|....*....
gi 169773285 271 NDHSGEIIHDDVLMRLMTF 289
Cdd:cd12157  270 PDRPRSIPQELLDQHDRTV 288
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
 71-323 2.13e-53

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 [Multi-domain]  Cd Length: 321  Bit Score: 178.51  E-value: 2.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  71 GVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALI-QTLnRKTHRAFNRVREGNFN--LEGFLGRTLYG 147
Cdd:cd12168   76 SLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLIlGAL-RNFSRAERSARAGKWRgfLDLTLAHDPRG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 148 KTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFG---GEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGR 224
Cdd:cd12168  155 KTLGILGLGGIGKAIARKAAAFGMKIIYHNRSRlpeELEKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAK 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 225 MKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEgalfyndhsgEIIHDdvlmRLMTFPNVLVCGHQAFFTEE 304
Cdd:cd12168  235 MKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENE----------PEVNP----GLLKMPNVTLLPHMGTLTVE 300

                        250
                 ....*....|....*....
gi 169773285 305 ALSEIAGVTLGNLEDFVLK 323
Cdd:cd12168  301 TQEKMEELVLENIEAFLET 319
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
 15-321 4.59e-50

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 [Multi-domain]  Cd Length: 308  Bit Score: 169.23  E-value: 4.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  15 YFDATLR----KHHPALCEIT-YHSFALSSETVSLA-QDSDAVCVFVN-DQLDAPVLETLYAngVRAILLRCAGFNNINL 87
Cdd:cd12169    8 YQDVARTladwSKLDDRAEVTvFNDHLLDEDALAERlAPFDAIVLMRErTPFPAALLERLPN--LKLLVTTGMRNASIDL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  88 QVAEDLGFFVANVPSySPEAVAEFAVALIQTLNRKTHRAFNRVREGNFnlEGFLGRTLYGKTVGVVGVGRIGLAFAKILH 167
Cdd:cd12169   86 AAAKERGIVVCGTGG-GPTATAELTWALILALARNLPEEDAALRAGGW--QTTLGTGLAGKTLGIVGLGRIGARVARIGQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 168 GFGCKLVAYDP-FGGEEFKKYG--EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKA 244
Cdd:cd12169  163 AFGMRVIAWSSnLTAERAAAAGveAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGA 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169773285 245 VINALKSGQLGGVALDVYEEEgalfyndhsgEIIHDDVLMRLmtfPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12169  243 LLAALRAGRIAGAALDVFDVE----------PLPADHPLRGL---PNVLLTPHIGYVTEEAYEGFYGQAVENIAAWL 306
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 69-329 9.29e-45

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 [Multi-domain]  Cd Length: 305  Bit Score: 155.41  E-value: 9.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  69 ANGVRAILlRC-AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNL---------E 138
Cdd:cd12174   48 APSLKAIA-RAgAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKWVTNGDGDDiskgvekgkK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 139 GFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEE----FKKYGEFVE-LGDLLAQSDVVSLHCPLTEGT 213
Cdd:cd12174  127 QFVGTELRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEaawkLSVEVQRVTsLEELLATADYITLHVPLTDET 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 214 RHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGvALDVYEEEGALFYNdhsgeiihddvlmrlmtfPNVL 293
Cdd:cd12174  207 RGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGG-YVTDFPEPALLGHL------------------PNVI 267

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 169773285 294 VCGHQAFFTEEALSEIAGVTLGNLEDFVLKRTCKNS 329
Cdd:cd12174  268 ATPHLGASTEEAEENCAVMAARQIMDFLETGNITNS 303
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 14-321 8.53e-44

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 [Multi-domain]  Cd Length: 330  Bit Score: 153.49  E-value: 8.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  14 HYFDATLRKHHPALCEITYHSF--ALSSETVSLAQDSDAVCVFVND--QLDAPVLEtlYANGVRAILlRCAGfnNINLQV 89
Cdd:cd12167   13 LFFGPAALARLAALAEVLPPTPdaDFAAEELRALLAGVEVLVTGWGtpPLDAELLA--RAPRLRAVV-HAAG--SVRGLV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  90 AEDL---GFFVANVPSYSPEAVAEFAVALIQTLNRKTHR--AFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAK 164
Cdd:cd12167   88 TDAVwerGILVTSAADANAEPVAEFTLAAILLALRRIPRfaAAYRAGRDWGWPTRRGGRGLYGRTVGIVGFGRIGRAVVE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 165 ILHGFGCKLVAYDPFGGEEFKKYG--EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNT 242
Cdd:cd12167  168 LLRPFGLRVLVYDPYLPAAEAAALgvELVSLDELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGALVDE 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169773285 243 KAVINALKSGQLgGVALDVYEEEGALFynDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12167  248 AALLAELRSGRL-RAALDVTDPEPLPP--DS-----------PLRTLPNVLLTPHIAGSTGDERRRLGDYALDELERFL 312
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 80-312 1.64e-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 [Multi-domain]  Cd Length: 306  Bit Score: 152.06  E-value: 1.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIG 159
Cdd:cd12179   71 AGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGIIGYGNMG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 160 LAFAKILHGFGCKLVAYD---PFGGEefkkYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSR 236
Cdd:cd12179  151 KAFAKRLSGFGCKVIAYDkykNFGDA----YAEQVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTAR 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169773285 237 GGLVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEiihdDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGV 312
Cdd:cd12179  227 GKVVVTKDLVKALKSGKILGACLDVLEYEKASFESIFNQP----EAFEYLIKSPKVILTPHIAGWTFESYEKIAEV 298
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
 81-273 3.71e-42

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: 149.78  E-value: 3.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRT--LYGKTVGVVGVGRI 158
Cdd:cd05302   94 GSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNVADVVKRAydLEGKTVGTVGAGRI 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 159 GLAFAKILHGFGCKLVAYDP--FGGEEFKKYG--EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNT 234
Cdd:cd05302  174 GLRVLRRLKPFDVHLLYYDRhrLPEEVEKELGltRHADLEDMVSKCDVVTINCPLHPETEGLFNKELLSKMKKGAYLVNT 253

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 169773285 235 SRGGLVNTKAVINALKSGQLGGVALDVYEEEGALfyNDH 273
Cdd:cd05302  254 ARGKICDREAVAEALESGHLAGYAGDVWFPQPAP--KDH 290
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 80-328 1.27e-40

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 [Multi-domain]  Cd Length: 314  Bit Score: 144.69  E-value: 1.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDlGFFVANVPSYSPeAVAEFAVALIQTLNRKTHRAFNRVREGNFNL---EGFLGRTLYGKTVGVVGVG 156
Cdd:cd12165   69 AGVDHLPLERLPE-GVVVANNHGNSP-AVAEHALALILALAKRIVEYDNDLRRGIWHGragEEPESKELRGKTVGILGYG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 157 RIGLAFAKILHGFGCKLVAYD--PFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNT 234
Cdd:cd12165  147 HIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGTLSDLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNV 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 235 SRGGLVNTKAVINALKSGQLGGVALDVyeeegalFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTL 314
Cdd:cd12165  227 GRGPVVDEEALYEALKERPIAGAAIDV-------WWRYPSRGDPVAPSRYPFHELPNVIMSPHNAGWTEETFRRRIDEAA 299

                        250
                 ....*....|....
gi 169773285 315 GNLEDFVLKRTCKN 328
Cdd:cd12165  300 ENIRRYLRGEPLLN 313
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
17-320 3.86e-40

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 143.69  E-value: 3.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  17 DATLRKHHPALCEITYHSFALSSETVSLAQDsdAVCVFVND-QLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGF 95
Cdd:PRK06487  15 DLDLSPLEQAFDELQLHDATTPEQVAERLRG--AQVAISNKvALDAAALAA--APQLKLILVAATGTNNVDLAAARERGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  96 FVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREG------NFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGF 169
Cdd:PRK06487  91 TVCNCQGYGTPSVAQHTLALLLALATRLPDYQQAVAAGrwqqssQFCLLDFPIVELEGKTLGLLGHGELGGAVARLAEAF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 170 GCK-LVAYDPFGGEEFKKygefVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINA 248
Cdd:PRK06487 171 GMRvLIGQLPGRPARPDR----LPLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADA 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169773285 249 LKSGQLGGVALDVYEEE-----GALFYNDHsgeiihddvlmrlmtfPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:PRK06487 247 LRSGHLGGAATDVLSVEppvngNPLLAPDI----------------PRLIVTPHSAWGSREARQRIVGQLAENARAF 307
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
29-321 2.30e-37

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 136.08  E-value: 2.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  29 EITYHSFALSSETVSLAQDSDAVcVFVNDQLDAPVLETLYAngVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAV 108
Cdd:PRK06932  26 EWIEYDHTSAEQTIERAKDADIV-ITSKVLFTRETLAQLPK--LKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 109 AEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLY------GKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGE 182
Cdd:PRK06932 103 PEHVLGMIFALKHSLMGWYRDQLSDRWATCKQFCYFDYpitdvrGSTLGVFGKGCLGTEVGRLAQALGMKVLYAEHKGAS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 183 EFKK-YGEFvelGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDV 261
Cdd:PRK06932 183 VCREgYTPF---EEVLKQADIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDV 259

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169773285 262 YEEEGALfyndhsgeiiHDDVLMRLM-TFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:PRK06932 260 LVKEPPE----------KDNPLIQAAkRLPNLLITPHIAWASDSAVTTLVNKVAQNIEEFV 310
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
1-320 1.43e-36

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 133.96  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAKSYDkhyfDATLRKHHpALCEITYHSFALSSETVSLAQDSDAVcvFVND-QLDAPVLEtlYANGVRAILLRC 79
Cdd:PRK08410   1 MKIVILDAKTLG----DKDLSVFE-EFGDFQIYPTTSPEEVIERIKDANII--ITNKvVIDKEVLS--QLPNLKLICITA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNF-------NLEGFLGrTLYGKTVGV 152
Cdd:PRK08410  72 TGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYsespiftHISRPLG-EIKGKKWGI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 153 VGVGRIGLAFAKILHGFGCKLVAYDPFG---GEEFKKygefVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGA 229
Cdd:PRK08410 151 IGLGTIGKRVAKIAQAFGAKVVYYSTSGknkNEEYER----VSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 230 LLVNTSRGGLVNTKAVINALKSGQLgGVALDVYEEEgalfyndhsgEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEI 309
Cdd:PRK08410 227 ILINVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKE----------PMEKNHPLLSIKNKEKLLITPHIAWASKEARKTL 295

                        330
                 ....*....|.
gi 169773285 310 AGVTLGNLEDF 320
Cdd:PRK08410 296 IEKVKENIKDF 306
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
 56-320 4.91e-34

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 [Multi-domain]  Cd Length: 301  Bit Score: 126.81  E-value: 4.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  56 NDQLDA-PVLETLYANGVraillrcaGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGN 134
Cdd:cd12156   56 AALIAAlPALELIASFGV--------GYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAGR 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 135 FNLEGF-LGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKlVAY---DPFGGEEFKKYGEFVELGdllAQSDVVSLHCPLT 210
Cdd:cd12156  128 WPKGAFpLTRKVSGKRVGIVGLGRIGRAIARRLEAFGME-IAYhgrRPKPDVPYRYYASLLELA---AESDVLVVACPGG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 211 EGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAlfyndhsgeiihddVLMRLMTFP 290
Cdd:cd12156  204 PATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEPN--------------VPAALLDLD 269

                        250       260       270
                 ....*....|....*....|....*....|
gi 169773285 291 NVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12156  270 NVVLTPHIASATVETRRAMGDLVLANLEAF 299
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
81-262 2.71e-32

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 124.02  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRT--LYGKTVGVVGVGRI 158
Cdd:PRK07574 124 GSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGWNIADCVSRSydLEGMTVGIVGAGRI 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 159 GLAFAKILHGFGCKLVAYDPF----GGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNT 234
Cdd:PRK07574 204 GLAVLRRLKPFDVKLHYTDRHrlpeEVEQELGLTYHVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYLVNT 283

                        170       180
                 ....*....|....*....|....*...
gi 169773285 235 SRGGLVNTKAVINALKSGQLGGVALDVY 262
Cdd:PRK07574 284 ARGKIVDRDAVVRALESGHLAGYAGDVW 311
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 28-310 3.27e-32

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: 122.30  E-value: 3.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  28 CEITYHSFALSSETVSLA-QDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPE 106
Cdd:cd12176   22 IEVERLKGALDEDELIEAlKDVHLLGIRSKTQLTEEVLEA--APKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 107 AVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYD-----PFGG 181
Cdd:cd12176  100 SVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYDiaeklPLGN 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 182 EEfkkygEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDV 261
Cdd:cd12176  180 AR-----QVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDV 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169773285 262 YEEE----GALFYNDhsgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIA 310
Cdd:cd12176  255 FPEEpasnGEPFSSP-------------LQGLPNVILTPHIGGSTEEAQENIG 294
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 1-328 1.15e-31

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 [Multi-domain]  Cd Length: 313  Bit Score: 121.09  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285   1 MKLAVFSAksyDKHYFDATLRKHHPALCEItyhsFALSSETVSLAQDSDAVCVFVndqLDAPVLETlyANGVRAILLRCA 80
Cdd:cd05300    1 MKILVLSP---LDDEHLERLRAAAPGAELR----VVTAEELTEELADADVLLGNP---PLPELLPA--APRLRWIQSTSA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGfLGRTLYGKTVGVVGVGRIGL 160
Cdd:cd05300   69 GVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQRRG-PVRELAGKTVLIVGLGDIGR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 161 AFAKILHGFGCKLVAY------DPFGGEEfkkygefV----ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGAL 230
Cdd:cd05300  148 EIARRAKAFGMRVIGVrrsgrpAPPVVDE-------VytpdELDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAV 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 231 LVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE--GAlfynDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSE 308
Cdd:cd05300  221 LINVGRGSVVDEDALIEALESGRIAGAALDVFEEEplPA----DS-----------PLWDLPNVIITPHISGDSPSYPER 285

                        330       340
                 ....*....|....*....|
gi 169773285 309 IAGVTLGNLEDFVLKRTCKN 328
Cdd:cd05300  286 VVEIFLENLRRYLAGEPLLN 305
PLN02928 PLN02928
oxidoreductase family protein
 51-312 2.09e-31

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 120.94  E-value: 2.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  51 VCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSY---SPEAVAEFAVALIQTLNRKTHRAF 127
Cdd:PLN02928  64 ICVPKMMRLDADIIAR--ASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRKQNEMQ 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 128 NRVRegNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAY--------DPFGGEEFKKYGEFVE------- 192
Cdd:PLN02928 142 ISLK--ARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsepEDGLLIPNGDVDDLVDekgghed 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 193 LGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEgalfynd 272
Cdd:PLN02928 220 IYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSE------- 292

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 169773285 273 hsgEIIHDDVLMRlmtFPNVLVCGHQAFFTEEALSEIAGV 312
Cdd:PLN02928 293 ---PFDPDDPILK---HPNVIITPHVAGVTEYSYRSMGKI 326
PLN02306 PLN02306
hydroxypyruvate reductase
 81-265 1.29e-30

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 119.58  E-value: 1.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFnlEG-----FLGRTLYGKTVGVVGV 155
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLY--EGwlphlFVGNLLKGQTVGVIGA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 156 GRIGLAFAKIL-HGFGCKLVAYDPFGGEEFKK----YGEFVE--------------LGDLLAQSDVVSLHCPLTEGTRHV 216
Cdd:PLN02306 174 GRIGSAYARMMvEGFKMNLIYYDLYQSTRLEKfvtaYGQFLKangeqpvtwkrassMEEVLREADVISLHPVLDKTTYHL 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169773285 217 INDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE 265
Cdd:PLN02306 254 INKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDE 302
PLN03139 PLN03139
formate dehydrogenase; Provisional
 12-262 2.56e-29

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 116.10  E-value: 2.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  12 DKHYFDATLRKHHP---ALCEITYHSFALSSETVSLAQDsdavcvfvndqldapvLETLYANGVraillrcaGFNNINLQ 88
Cdd:PLN03139  83 DKEGPDCELEKHIPdlhVLITTPFHPAYVTAERIKKAKN----------------LELLLTAGI--------GSDHIDLP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  89 VAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRT--LYGKTVGVVGVGRIGLAFAKIL 166
Cdd:PLN03139 139 AAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNVAGIAYRAydLEGKTVGTVGAGRIGRLLLQRL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 167 HGFGCKLVAYD--PFGGEEFKKYG-EFVE-LGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNT 242
Cdd:PLN03139 219 KPFNCNLLYHDrlKMDPELEKETGaKFEEdLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDT 298

                        250       260
                 ....*....|....*....|
gi 169773285 243 KAVINALKSGQLGGVALDVY 262
Cdd:PLN03139 299 QAVADACSSGHIGGYGGDVW 318
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 80-321 4.47e-28

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 [Multi-domain]  Cd Length: 314  Bit Score: 111.13  E-value: 4.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPS-YSpEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEgFLGRTLYGKTVGVVGVGRI 158
Cdd:cd12155   69 AGVDYLPLEYIKKKGILLTNNSGiHS-IPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMD-SSLLELYGKTILFLGTGSI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 159 GLAFAKILHGFGCKL---------VAYdpfggeeFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGA 229
Cdd:cd12155  147 GQEIAKRLKAFGMKVigvntsgrdVEY-------FDKCYPLEELDEVLKEADIVVNVLPLTEETHHLFDEAFFEQMKKGA 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 230 LLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGalFYNDHSgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEI 309
Cdd:cd12155  220 LFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEP--LPKDSP-----------LWDLDNVLITPHISGVSEHFNERL 286

                        250
                 ....*....|..
gi 169773285 310 AGVTLGNLEDFV 321
Cdd:cd12155  287 FDIFYENLKSFL 298
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 80-265 6.45e-28

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 [Multi-domain]  Cd Length: 343  Bit Score: 111.47  E-value: 6.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  80 AGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIqtlnrkthraFNRVREGNFNLEGflgRTL----YGktvgvvgv 155
Cdd:cd12158   66 IGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSAL----------LVLAQRQGFSLKG---KTVgivgVG-------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 156 gRIGLAFAKILHGFGCKLVAYDPFGGEEFKKyGEFVELGDLLAQSDVVSLHCPLTEG----TRHVINDENLGRMKKGALL 231
Cdd:cd12158  125 -NVGSRLARRLEALGMNVLLCDPPRAEAEGD-PGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQIL 202

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169773285 232 VNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE 265
Cdd:cd12158  203 INASRGAVIDNQALLALLQRGKDLRVVLDVWENE 236
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 102-321 8.80e-27

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: 107.35  E-value: 8.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 102 SYSpEAVAEFAVALIQTLNRKtHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGG 181
Cdd:cd12159   82 AYA-ETVAEHALALLLAGLRQ-LPARARATTWDPAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNRSGR 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 182 --EEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVAL 259
Cdd:cd12159  160 pvEGADETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAAL 239

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169773285 260 DVYEEEGAlfYNDHSgeiihddvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:cd12159  240 DVTDPEPL--PDGHP-----------LWSLPNALITPHVANTPEVIRPLLAERVAENVRAFA 288
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
29-321 1.82e-25

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 105.64  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  29 EITYHSFALSSETVSLA-QDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPsYS-PE 106
Cdd:PRK11790  34 NIEYHKGALDEEELIEAiKDAHFIGIRSRTQLTEEVLAA--AEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAP-FSnTR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 107 AVAEFAVALIQTL-------NRKTHRA-FNRVREGNFNLEGflgRTL----YGKtvgvvgvgrIG-----LAFAkilhgF 169
Cdd:PRK11790 111 SVAELVIGEIILLlrgipekNAKAHRGgWNKSAAGSFEVRG---KTLgivgYGH---------IGtqlsvLAES-----L 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 170 GCKLVAYD-----PFGGEEfkkygEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKA 244
Cdd:PRK11790 174 GMRVYFYDiedklPLGNAR-----QVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDA 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169773285 245 VINALKSGQLGGVALDVYEEEGAlfYNDhsgeiihDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDFV 321
Cdd:PRK11790 249 LADALKSGHLAGAAIDVFPVEPK--SNG-------DPFESPLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYS 316
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 104-320 3.09e-23

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: 97.80  E-value: 3.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 104 SPEAVAEFAVALIqtLNRKTHRAFNRVREGNFNLEGFLGrTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEE 183
Cdd:cd12180   95 AAEAIAEFVLAAI--LAAAKRLPEIWVKGAEQWRREPLG-SLAGSTLGIVGFGAIGQALARRALALGMRVLALRRSGRPS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 184 FKKYGEFV-ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVY 262
Cdd:cd12180  172 DVPGVEAAaDLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVT 251

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169773285 263 EEE----GALFYNDhsgeiihddvlmrlmtfPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12180  252 DPEplpeGHPLYTH-----------------PRVRLSPHTSAIAPDGRRNLADRFLENLARY 296
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
81-317 4.38e-23

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 97.90  E-value: 4.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  81 GFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNL---EGFLGRTLYGKTVGVVGVGR 157
Cdd:PRK15409  76 GYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTAsigPDWFGTDVHHKTLGIVGMGR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 158 IGLAFAKILH-GFGCKLV--AYDPFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNT 234
Cdd:PRK15409 156 IGMALAQRAHfGFNMPILynARRHHKEAEERFNARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINA 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 235 SRGGLVNTKAVINALKSGQLGGVALDVYEEEGAlfyndhsgeiihdDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTL 314
Cdd:PRK15409 236 GRGPVVDENALIAALQKGEIHAAGLDVFEQEPL-------------SVDSPLLSLPNVVAVPHIGSATHETRYNMAACAV 302


                 ...
gi 169773285 315 GNL 317
Cdd:PRK15409 303 DNL 305
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
29-265 2.52e-21

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 93.56  E-value: 2.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  29 EITY-HSFALSSETVslaQDSDAVCVFVNDQLDAPVLEtlyANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEA 107
Cdd:PRK00257  21 EIRRlPGRAFDRAAV---RDADVLLVRSVTRVDRALLE---GSRVRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 108 VAEFAVALIQTLNRkthrafnrvregnfnLEGFlgrTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPfGGEEFKKY 187
Cdd:PRK00257  95 VVDYVLGSLLTLAE---------------REGV---DLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDP-PRQEAEGD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 188 GEFVELGDLLAQSDVVSLHCPLTEG----TRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYE 263
Cdd:PRK00257 156 GDFVSLERILEECDVISLHTPLTKEgehpTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWE 235


                 ..
gi 169773285 264 EE 265
Cdd:PRK00257 236 GE 237
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 107-261 5.34e-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: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 91.50  E-value: 5.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 107 AVAEFAVALIQTLNRKTHRAFNRVREGNFnlEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKL--VAYDPfggeef 184
Cdd:cd12166   94 STAELAVALILASLRGLPRFVRAQARGRW--EPRRTPSLADRRVLIVGYGSIGRAIERRLAPFEVRVtrVARTA------ 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 185 kKYGEFV----ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLgGVALD 260
Cdd:cd12166  166 -RPGEQVhgidELPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRL-RAALD 243


                 .
gi 169773285 261 V 261
Cdd:cd12166  244 V 244
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 158-265 2.88e-20

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 [Multi-domain]  Cd Length: 306  Bit Score: 89.48  E-value: 2.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 158 IGLAFAKILHGFGCK----------LVAYDPFGGEEfkkygefvELGDLLAQSDV-VSLhCPLTEGTRHVINDENLGRMK 226
Cdd:cd12164  143 LGAAVARRLAALGFPvsgwsrspkdIEGVTCFHGEE--------GLDAFLAQTDIlVCL-LPLTPETRGILNAELLARLP 213

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 169773285 227 KGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE 265
Cdd:cd12164  214 RGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQE 252
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 107-318 1.76e-16

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: 79.24  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 107 AVAEFAVALIQTLNRKTHRAFNRVREGNFN--LEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAY-------- 176
Cdd:cd12163   91 QIAEWVIGTWLVLSHHFLQYIELQKEQTWGrrQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 177 --------------DP--------FGGEEFKKYGEFVELG-DLLaqsdVVSLhcPLTEGTRHVINDENLGRM-KKGALLV 232
Cdd:cd12163  171 esrkddgyivpgtgDPdgsipsawFSGTDKASLHEFLRQDlDLL----VVSL--PLTPATKHLLGAEEFEILaKRKTFVS 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 233 NTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGalFYNDHsgeiihddvlmRLMTFPNVLVCGHQAFFTEEALSEIAGV 312
Cdd:cd12163  245 NIARGSLVDTDALVAALESGQIRGAALDVTDPEP--LPADH-----------PLWSAPNVIITPHVSWQTQEYFDRALDV 311


                 ....*.
gi 169773285 313 TLGNLE 318
Cdd:cd12163  312 LEENLE 317
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 108-265 1.20e-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: 240637  Cd Length: 310  Bit Score: 76.26  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 108 VAEFAVALIQTLNRKTHRAFNRVREGNFNLEgfLG-----------RTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAY 176
Cdd:cd12160   95 VAEHTLALILAAVRRLDEMREAQREHRWAGE--LGglqplrpagrlTTLLGARVLIWGFGSIGQRLAPLLTALGARVTGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 177 DPFGGEefkKYGEFV----ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSG 252
Cdd:cd12160  173 ARSAGE---RAGFPVvaedELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESG 249

                        170
                 ....*....|...
gi 169773285 253 QLGGVALDVYEEE 265
Cdd:cd12160  250 RLGGAALDVTATE 262
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
31-251 1.97e-15

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 75.69  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  31 TYHSFALSSETVSLAQ---DSDAVCVFvNDQLDAP--VLETLYANGVRAILLRC--AGFNNINLQVAEDLGFFVANVPSY 103
Cdd:PRK06436   3 VYVNFPMSKKLLEICRdilDLDDVHWY-PDYYDAEaiLIKGRYVPGKKTKMIQSlsAGVDHIDVSGIPENVVLCSNAGAY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 104 SPeAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFlgRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDpfggEE 183
Cdd:PRK06436  82 SI-SVAEHAFALLLAWAKNICENNYNMKNGNFKQSPT--KLLYNKSLGILGYGGIGRRVALLAKAFGMNIYAYT----RS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169773285 184 FKKYG---EFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKS 251
Cdd:PRK06436 155 YVNDGissIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRN 225
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 144-263 1.04e-13

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: 70.72  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 144 TLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDP------FGGEEFKKygEFVELGDLLAQSDVVSLHCPLTEGTRHVI 217
Cdd:cd12154  157 DVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDInvealeQLEELGGK--NVEELEEALAEADVIVTTTLLPGKRAGIL 234

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169773285 218 NDENL-GRMKKGALLVNTSRGGLVNTKAVIN-ALKSGQLGGVALDVYE 263
Cdd:cd12154  235 VPEELvEQMKPGSVIVNVAVGAVGCVQALHTqLLEEGHGVVHYGDVNM 282
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
 142-268 8.70e-12

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 65.70  E-value: 8.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 142 GRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDP---FGGEEfkkyGEFVELGDLLAQSDVVSLHCPL-TEG---TR 214
Cdd:PRK15438 111 GFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPpraDRGDE----GDFRSLDELVQEADILTFHTPLfKDGpykTL 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169773285 215 HVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGAL 268
Cdd:PRK15438 187 HLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 30-320 4.40e-09

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 [Multi-domain]  Cd Length: 294  Bit Score: 56.93  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285  30 ITYHSFALSS-ETVSLAQDSDAVCVFVNDQLDAPVLETlyANGVRAILLRCAGFN----NINLQVAEDLGFFVANVPSYS 104
Cdd:cd12170   28 VFYDDIPESDeEIIERIGDADCVLVSYTTQIDEEVLEA--CPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 105 PEAVAEFAVA-LIQTLNrkthrAFNRVREGNFNLE------GFLGrtlygktvgvvgVGRIGLAFAKILHGFGCKLVAYD 177
Cdd:cd12170  106 DEGVVEYVISeLIRLLH-----GFGGKQWKEEPREltglkvGIIG------------LGTTGQMIADALSFFGADVYYYS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 178 PFGGEEFKKYG-EFVELGDLLAQSDVVSLHCPltegtRHVI--NDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQL 254
Cdd:cd12170  169 RTRKPDAEAKGiRYLPLNELLKTVDVICTCLP-----KNVIllGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKASGY 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169773285 255 ggvaldvyeeegALFYNDHSGEIIHDDvlmrLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF 320
Cdd:cd12170  244 ------------NIFDCDTAGALGDEE----LLRYPNVICTNKSAGWTRQAFERLSQKVLANLEEY 293
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
192-265 5.29e-06

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 47.48  E-value: 5.29e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169773285 192 ELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEE 265
Cdd:PRK15469 183 ELSAFLSQTRVLINLLPNTPETVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSRE 256
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 156-242 5.53e-04

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


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 41.24  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169773285 156 GRIGLAFAKILHGFGCKLVAYD---------PFGGEEFKKYGEFVELGDLLAQSDVVsLHCPLTEGTR--HVINDENLGR 224
Cdd:cd01620  171 GVVGLGAAKIAKKLGANVLVYDikeeklkgvETLGGSRLRYSQKEELEKELKQTDIL-INAILVDGPRapILIMEELVGP 249

                         90       100
                 ....*....|....*....|
gi 169773285 225 MKKGALLVNTS--RGGLVNT 242
Cdd:cd01620  250 MKRGAVIVDLAadQGGNDET 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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