NCBI Conserved Domain Search

formate dehydrogenase; Provisional

Pssm-ID: 178684 Cd Length: 386 Bit Score: 115.72 E-value: 1.92e-31

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929328    85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAPMVIPSRIIP 147
Cdd:PLN03139 271 GMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAPKDHPWRYMP 333

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: 98.17 E-value: 4.17e-25

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAPMVIPSRIIP 147
Cdd:cd05302 234 GLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPAPKDHPWRTMP 296

NAD-dependent formate dehydrogenase;

Pssm-ID: 181041 Cd Length: 385 Bit Score: 83.18 E-value: 2.21e-19

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929328    85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAPMVIPSRIIP 147
Cdd:PRK07574 264 HLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQPAPADHPWRTMP 326

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: 65.98 E-value: 3.72e-14

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 3929328     85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:pfam02826 107 HLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPLP 160

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: 65.99 E-value: 1.68e-13

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW--YPLPA 137
Cdd:COG0111 211 GLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAALDVFepEPLPA 265

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: 65.51 E-value: 2.36e-13

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:cd12173 208 GLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP 261

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: 65.73 E-value: 2.40e-13

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:cd05198 210 HLINEEELALMKPGAVLVNTARGGLVDEDALLRALKSGKIAGAALDVFEPEPLP 263

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: 64.15 E-value: 8.75e-13

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12185 212 LINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDV 257

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: 64.11 E-value: 9.54e-13

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12168 225 HLINKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDV 271

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: 62.94 E-value: 2.53e-12

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12186 214 HLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALDT 260

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: 62.41 E-value: 3.77e-12

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:COG1052 212 HLINAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPPP 265

(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: 62.31 E-value: 4.03e-12

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW 132
Cdd:cd12184 215 LINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVL 261

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: 59.62 E-value: 4.34e-11

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd01619 213 MINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDV 258

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: 59.18 E-value: 5.76e-11

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW--YPLPAPMVIPSRI 145
Cdd:cd12165 207 GLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVWwrYPSRGDPVAPSRY 269

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: 57.84 E-value: 1.45e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12183 214 LINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDV 259

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: 57.52 E-value: 1.71e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd05299 212 HLIDAEALALMKPGAFLVNTARGGLVDEAALARALKSGRIAGAALDV 258

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: 57.46 E-value: 2.17e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12162 213 NLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDV 259

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: 56.05 E-value: 5.55e-10

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVwYP 134
Cdd:cd12176 208 NMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDV-FP 256

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: 56.13 E-value: 6.32e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12187 210 LINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDV 255

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: 55.73 E-value: 8.81e-10

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:cd12159 195 HLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEPLP 248

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: 55.79 E-value: 9.03e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12177 218 HMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDV 264

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: 55.76 E-value: 9.72e-10

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV-----WYPLPAPMVIPSRII 146
Cdd:cd12157 216 LINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVfemedWARPDRPRSIPQELL 281

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: 55.66 E-value: 9.82e-10

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:cd12175 213 HLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLP 266

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: 55.28 E-value: 1.10e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLPA 137
Cdd:cd12155 205 HLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEeePLPK 259

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: 55.22 E-value: 1.42e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLPA 137
Cdd:cd05300 205 GLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEeePLPA 259

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: 54.85 E-value: 1.57e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLPA 137
Cdd:cd12171 217 GMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPeePLPA 271

D-lactate dehydrogenase; Provisional

Pssm-ID: 183550 Cd Length: 330 Bit Score: 54.53 E-value: 2.13e-09

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW 132
Cdd:PRK12480 215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTY 261

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: 54.08 E-value: 2.63e-09

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd05303 210 MINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDV 255

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: 54.03 E-value: 3.17e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLPA 137
Cdd:cd12172 213 LINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEeePPPA 266

oxidoreductase family protein

Pssm-ID: 215501 Cd Length: 347 Bit Score: 53.92 E-value: 3.75e-09

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 3929328    85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:PLN02928 242 GIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDV 288

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: 53.00 E-value: 8.22e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVV-DACSSGHVTGEARDVWYPLPAP 138
Cdd:cd12154 234 LVPEELVEQMKPGSVIVNVAVGAVGCVQALHtQLLEEGHGVVHYGDVNMPGPGC 287

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: 52.95 E-value: 8.28e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGeARDVWY--PLPAP 138
Cdd:cd12167 220 GMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLRA-ALDVTDpePLPPD 274

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: 52.61 E-value: 1.10e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY---PLPA 137
Cdd:cd12161 213 GLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDmepPLPA 268

D-lactate dehydrogenase; Validated

Pssm-ID: 181499 Cd Length: 332 Bit Score: 51.67 E-value: 2.45e-08

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW 132
Cdd:PRK08605 217 LFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTY 263

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: 50.99 E-value: 4.43e-08

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW 132
Cdd:cd12158 187 LLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233

phosphoglycerate dehydrogenase;

Pssm-ID: 236985 [Multi-domain] Cd Length: 409 Bit Score: 50.95 E-value: 4.50e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 3929328    85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVwYP 134
Cdd:PRK11790 219 NMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDV-FP 267

2-hydroxyacid dehydrogenase;

Pssm-ID: 180588 [Multi-domain] Cd Length: 317 Bit Score: 50.47 E-value: 6.63e-08

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 3929328    85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:PRK06487 213 HLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDV 259

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: 50.19 E-value: 6.82e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLPA 137
Cdd:cd12164 202 GILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEqePLPA 256

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: 50.25 E-value: 6.83e-08

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDvwYPLPAPMVIPSRIIPKP 149
Cdd:cd12174 208 GLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTD--FPEPALLGHLPNVIATP 270

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: 49.51 E-value: 1.07e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGeARDVWYPLPAP 138
Cdd:cd12166 199 GLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLRA-ALDVTDPEPLP 251

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: 48.66 E-value: 2.30e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW--YPLPAP 138
Cdd:cd12169 213 GLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFdvEPLPAD 268

4-phosphoerythronate dehydrogenase PdxB;

Pssm-ID: 166874 [Multi-domain] Cd Length: 381 Bit Score: 46.95 E-value: 9.69e-07

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW 132
Cdd:PRK00257 188 LLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVW 234

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: 45.03 E-value: 4.63e-06

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:cd12180 204 HLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP 257

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: 44.21 E-value: 8.30e-06

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDV 131
Cdd:cd12179 205 GMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDV 251

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: 43.90 E-value: 1.09e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3929328   85 GLFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVW--YPLPAP 138
Cdd:cd12160 212 HALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTatEPLPAS 267

glyoxylate reductase; Reviewed

Pssm-ID: 183914 Cd Length: 333 Bit Score: 43.24 E-value: 1.97e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPAP 138
Cdd:PRK13243 221 MINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY 273

erythronate-4-phosphate dehydrogenase PdxB; Provisional

Pssm-ID: 185335 [Multi-domain] Cd Length: 378 Bit Score: 38.73 E-value: 7.70e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWYPLPA 137
Cdd:PRK15438 188 LADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPE 239

glyoxylate/hydroxypyruvate reductase GhrB;

Pssm-ID: 185307 Cd Length: 323 Bit Score: 38.20 E-value: 8.89e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3929328    86 LFDKERISKLKKGVLIVNNARGAIMDTQAVVDACSSGHVTGEARDVWY--PLP 136
Cdd:PRK15409 217 LFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEqePLS 269