NCBI Conserved Domain Search

Conserved domains on [gi|1046889495|ref|XP_017449110|]

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glyoxylate reductase/hydroxypyruvate reductase isoform X1 [Rattus norvegicus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

NADB_Rossmann super family

cl21454

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...

1-174

1.01e-102

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.

The actual alignment was detected with superfamily member cd05301:

Pssm-ID: 473865 [Multi-domain] Cd Length: 309 Bit Score: 297.77 E-value: 1.01e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:cd05301   137 LLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM-KILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:cd05301   216 INAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPNVVLLPHIGSATVETRTAM 295

                         170
                  ....*....|....
gi 1046889495 161 SLLAANNLLAGLRG 174
Cdd:cd05301   296 AELAADNLLAVLAG 309

Name

Accession

Description

Interval

E-value

GDH

cd05301

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...

1-174

1.01e-102

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: 297.77 E-value: 1.01e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:cd05301   137 LLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM-KILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:cd05301   216 INAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPNVVLLPHIGSATVETRTAM 295

                         170
                  ....*....|....
gi 1046889495 161 SLLAANNLLAGLRG 174
Cdd:cd05301   296 AELAADNLLAVLAG 309

LdhA

COG1052

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...

1-181

5.31e-85

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: 253.09 E-value: 5.31e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPqEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:COG1052   136 LLGRDLSGKTLGIIGLGRIGQAVARRAKGFGM-KVLYYDRSPKP-EVAELGAEYVSLDELLAESDIVSLHCPLTPETRHL 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:COG1052   214 INAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDHPLLSLPNVVLTPHIASATEEAREAM 293

                         170       180
                  ....*....|....*....|.
gi 1046889495 161 SLLAANNLLAGLRGEPMPSEL 181
Cdd:COG1052   294 AELALDNLLAFLAGEPPPNPV 314

2-Hacid_dh_C

pfam02826

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...

1-150

5.05e-71

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: 212.74 E-value: 5.05e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRP-QEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRG 79
Cdd:pfam02826  29 LLGRELSGKTVGIIGLGRIGRAVAKRLKAFGM-KVIAYDRYPKPeEEEEELGARYVSLDELLAESDVVSLHLPLTPETRH 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIG 150
Cdd:pfam02826 108 LINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPLPADHPLLDLPNVILTPHIA 178

PRK13243

glyoxylate reductase; Reviewed

1-179

1.19e-59

glyoxylate reductase; Reviewed

Pssm-ID: 183914 Cd Length: 333 Bit Score: 188.85 E-value: 1.19e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:PRK13243  143 FLGYDVYGKTIGIIGFGRIGQAVARRAKGFGM-RILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHM 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLpPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:PRK13243  222 INEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPY-YNEELFSLKNVVLAPHIGSATFEAREGM 300

                         170
                  ....*....|....*....
gi 1046889495 161 SLLAANNLLAGLRGEPMPS 179
Cdd:PRK13243  301 AELVAENLIAFKRGEVPPT 319

Name

Accession

Description

Interval

E-value

GDH

cd05301

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...

1-174

1.01e-102

Pssm-ID: 240626 [Multi-domain] Cd Length: 309 Bit Score: 297.77 E-value: 1.01e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:cd05301   137 LLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM-KILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:cd05301   216 INAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPNVVLLPHIGSATVETRTAM 295

                         170
                  ....*....|....
gi 1046889495 161 SLLAANNLLAGLRG 174
Cdd:cd05301   296 AELAADNLLAVLAG 309

LdhA

COG1052

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...

1-181

5.31e-85

Pssm-ID: 440672 [Multi-domain] Cd Length: 316 Bit Score: 253.09 E-value: 5.31e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPqEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:COG1052   136 LLGRDLSGKTLGIIGLGRIGQAVARRAKGFGM-KVLYYDRSPKP-EVAELGAEYVSLDELLAESDIVSLHCPLTPETRHL 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:COG1052   214 INAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDHPLLSLPNVVLTPHIASATEEAREAM 293

                         170       180
                  ....*....|....*....|.
gi 1046889495 161 SLLAANNLLAGLRGEPMPSEL 181
Cdd:COG1052   294 AELALDNLLAFLAGEPPPNPV 314

formate_dh_like

cd05198

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...

1-170

6.20e-75

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: 226.74 E-value: 6.20e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVQrFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:cd05198   133 FPGYELEGKTVGIVGLGRIGQRVAKRLQAFGMK-VLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRHL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:cd05198   212 INEEELALMKPGAVLVNTARGGLVDEDALLRALKSGKIAGAALDVFEPEPLPADHPLLELPNVILTPHIAGYTEEARERM 291

                         170
                  ....*....|
gi 1046889495 161 SLLAANNLLA 170
Cdd:cd05198   292 AEIAVENLER 301

SerA

COG0111

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...

3-181

2.80e-71

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: 217.75 E-value: 2.80e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFV-PIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:COG0111   135 GRELRGKTVGIVGLGRIGRAVARRLRAFGM-RVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLI 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:COG0111   214 GAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAALDVFEPEPLPADSPLWDLPNVILTPHIAGSTEEAQERAA 293

                         170       180
                  ....*....|....*....|
gi 1046889495 162 LLAANNLLAGLRGEPMPSEL 181
Cdd:COG0111   294 RQVAENIRRFLAGEPLRNLV 313

2-Hacid_dh_C

pfam02826

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...

1-150

5.05e-71

Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 212.74 E-value: 5.05e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRP-QEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRG 79
Cdd:pfam02826  29 LLGRELSGKTVGIIGLGRIGRAVAKRLKAFGM-KVIAYDRYPKPeEEEEELGARYVSLDELLAESDVVSLHLPLTPETRH 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIG 150
Cdd:pfam02826 108 LINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPLPADHPLLDLPNVILTPHIA 178

PGDH_like_2

cd12172

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...

3-173

1.40e-69

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: 213.50 E-value: 1.40e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:cd12172   137 GTELYGKTLGIIGLGRIGKAVARRLSGFGM-KVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLIN 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSL 162
Cdd:cd12172   216 AAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEEPPPADSPLLELPNVILTPHIGASTKEAVLRMGT 295

                         170
                  ....*....|.
gi 1046889495 163 LAANNLLAGLR 173
Cdd:cd12172   296 MAAQNVIDVLA 306

2-Hacid_dh_11

cd12175

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...

1-176

2.53e-66

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: 205.11 E-value: 2.53e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEA-AEFQAEFVPIAQLAAESDFIVVSCSLTPATRG 79
Cdd:cd12175   135 RPSRELSGKTVGIVGLGNIGRAVARRLRGFGV-EVIYYDRFRDPEAEeKDLGVRYVELDELLAESDVVSLHVPLTPETRH 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNT 159
Cdd:cd12175   214 LIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDDPLLRLDNVILTPHIAGVTDESYQR 293

                         170
                  ....*....|....*..
gi 1046889495 160 MSLLAANNLLAGLRGEP 176
Cdd:cd12175   294 MAAIVAENIARLLRGEP 310

2-Hacid_dh_1

cd05300

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...

6-177

3.82e-63

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: 196.97 E-value: 3.82e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEaaEFQAEFVPIAQLA---AESDFIVVSCSLTPATRGLCN 82
Cdd:cd05300   132 LAGKTVLIVGLGDIGREIARRAKAFGM-RVIGVRRSGRPAP--PVVDEVYTPDELDellPEADYVVNALPLTPETRGLFN 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSL 162
Cdd:cd05300   209 AERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLPADSPLWDLPNVIITPHISGDSPSYPERVVE 288

                         170
                  ....*....|....*
gi 1046889495 163 LAANNLLAGLRGEPM 177
Cdd:cd05300   289 IFLENLRRYLAGEPL 303

PRK13243

glyoxylate reductase; Reviewed

1-179

1.19e-59

glyoxylate reductase; Reviewed

Pssm-ID: 183914 Cd Length: 333 Bit Score: 188.85 E-value: 1.19e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   1 MCGYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:PRK13243  143 FLGYDVYGKTIGIIGFGRIGQAVARRAKGFGM-RILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHM 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLpPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:PRK13243  222 INEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPY-YNEELFSLKNVVLAPHIGSATFEAREGM 300

                         170
                  ....*....|....*....
gi 1046889495 161 SLLAANNLLAGLRGEPMPS 179
Cdd:PRK13243  301 AELVAENLIAFKRGEVPPT 319

PGDH_4

cd12173

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...

3-175

4.69e-59

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: 186.47 E-value: 4.69e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgrqP--RPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:cd12173   133 GVELRGKTLGIVGLGRIGREVARRARAFGMKVLAYD---PyiSAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGL 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTM 160
Cdd:cd12173   210 INAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPPADSPLLGLPNVILTPHLGASTEEAQERV 289

                         170
                  ....*....|....*
gi 1046889495 161 SLLAANNLLAGLRGE 175
Cdd:cd12173   290 AVDAAEQVLAVLAGE 304

CtBP_dh

cd05299

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...

4-176

5.41e-59

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: 186.57 E-value: 5.41e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNK 83
Cdd:cd05299   138 RRLRGLTLGLVGFGRIGRAVAKRAKAFGF-RVIAYDPYVPDGVAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  84 DFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLL 163
Cdd:cd05299   217 EALALMKPGAFLVNTARGGLVDEAALARALKSGRIAGAALDVLEEEPPPADSPLLSAPNVILTPHAAWYSEESLAELRRK 296

                         170
                  ....*....|...
gi 1046889495 164 AANNLLAGLRGEP 176
Cdd:cd05299   297 AAEEVVRVLRGEP 309

2-Hacid_dh_2

cd12159

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

6-180

1.93e-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: 240636 Cd Length: 303 Bit Score: 182.08 E-value: 1.93e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDF 85
Cdd:cd12159   123 LRGSTVAIVGAGGIGRALIPLLAPFGA-KVIAVNRSGRPVEGADETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAA 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAA 165
Cdd:cd12159   202 LAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEPLPDGHPLWSLPNALITPHVANTPEVIRPLLAERVA 281

                         170
                  ....*....|....*
gi 1046889495 166 NNLLAGLRGEPMPSE 180
Cdd:cd12159   282 ENVRAFAAGEPLLGV 296

HPPR

cd12156

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...

3-170

3.27e-57

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: 181.51 E-value: 3.27e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEfvpIAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:cd12156   136 TRKVSGKRVGIVGLGRIGRAIARRLEAFGM-EIAYHGRRPKPDVPYRYYAS---LLELAAESDVLVVACPGGPATRHLVN 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPShPLLTLKNCVILPHIGSATYKTRNTMSL 162
Cdd:cd12156   212 AEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEPNVPA-ALLDLDNVVLTPHIASATVETRRAMGD 290


                  ....*...
gi 1046889495 163 LAANNLLA 170
Cdd:cd12156   291 LVLANLEA 298

2-Hacid_dh_4

cd12162

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

6-170

4.09e-56

Pssm-ID: 240639 [Multi-domain] Cd Length: 307 Bit Score: 178.80 E-value: 4.09e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgrqpRPQeAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDF 85
Cdd:cd12162   145 LAGKTLGIIGYGNIGQAVARIARAFGMKVLFAE----RKG-APPLREGYVSLDELLAQSDVISLHCPLTPETRNLINAEE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLT-LKNCVILPHIGSATYKTRNTMSLLA 164
Cdd:cd12162   220 LAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPRADNPLLKaAPNLIITPHIAWASREARQRLMDIL 299


                  ....*.
gi 1046889495 165 ANNLLA 170
Cdd:cd12162   300 VDNIKA 305

2-Hacid_dh_13

cd12178

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...

3-175

1.13e-54

Pssm-ID: 240655 [Multi-domain] Cd Length: 317 Bit Score: 175.50 E-value: 1.13e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEA-AEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12178   139 GHELAGKTLGIIGMGRIGQAVARRAKAFGM-KILYYNRHRLSEETeKELGATYVDLDELLKESDFVSLHAPYTPETHHLI 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHpLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:cd12178   218 DAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEPEVSPE-LKKLDNVILTPHIGNATVEARDAMA 296

                         170
                  ....*....|....
gi 1046889495 162 LLAANNLLAGLRGE 175
Cdd:cd12178   297 KEAADNIISFLEGK 310

Mand_dh_like

cd12168

D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...

10-176

2.28e-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: 172.35 E-value: 2.28e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVqRFLYTGR-QPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQK 88
Cdd:cd12168   156 TLGILGLGGIGKAIARKAAAFGM-KIIYHNRsRLPEELEKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAK 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  89 MKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPpsHP-LLTLKNCVILPHIGSATYKTRNTMSLLAANN 167
Cdd:cd12168   235 MKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPEV--NPgLLKMPNVTLLPHMGTLTVETQEKMEELVLEN 312


                  ....*....
gi 1046889495 168 LLAGLRGEP 176
Cdd:cd12168   313 IEAFLETGK 321

2-Hacid_dh_10

cd12171

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

6-170

4.96e-53

Pssm-ID: 240648 [Multi-domain] Cd Length: 310 Bit Score: 171.18 E-value: 4.96e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQP--RPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNK 83
Cdd:cd12171   145 LRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVY---DPyvDPEKIEADGVKKVSLEELLKRSDVVSLHARLTPETRGMIGA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  84 DFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLL 163
Cdd:cd12171   222 EEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLPADHPLLKLDNVTLTPHIAGATRDVAERSPEI 301


                  ....*..
gi 1046889495 164 AANNLLA 170
Cdd:cd12171   302 IAEELKR 308

2-Hacid_dh_12

cd12177

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...

3-176

1.44e-50

Pssm-ID: 240654 [Multi-domain] Cd Length: 321 Bit Score: 165.19 E-value: 1.44e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKP-FGVQRFLYTgRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12177   142 GHELSGKTVGIIGYGNIGSRVAEILKEgFNAKVLAYD-PYVSEEVIKKKGAKPVSLEELLAESDIISLHAPLTEETYHMI 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:cd12177   221 NEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADHPLLHYENVVITPHIGAYTYESLYGMG 300

                         170
                  ....*....|....*
gi 1046889495 162 LLAANNLLAGLRGEP 176
Cdd:cd12177   301 EKVVDDIEDFLAGKE 315

2-Hacid_dh_8

cd12167

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

2-180

2.29e-50

Pssm-ID: 240644 [Multi-domain] Cd Length: 330 Bit Score: 165.04 E-value: 2.29e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   2 CGYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPrPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12167   144 GGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLP-AAEAAALGVELVSLDELLARSDVVSLHAPLTPETRGMI 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAgLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:cd12167   223 DARLLALMRDGATFINTARGALVDEAALLAELRSGRLRAA-LDVTDPEPLPPDSPLRTLPNVLLTPHIAGSTGDERRRLG 301

                         170
                  ....*....|....*....
gi 1046889495 162 LLAANNLLAGLRGEPMPSE 180
Cdd:cd12167   302 DYALDELERFLAGEPLLHE 320

PRK15409

glyoxylate/hydroxypyruvate reductase GhrB;

10-174

2.54e-50

glyoxylate/hydroxypyruvate reductase GhrB;

Pssm-ID: 185307 Cd Length: 323 Bit Score: 164.54 E-value: 2.54e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKpFGV-QRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQK 88
Cdd:PRK15409  147 TLGIVGMGRIGMALAQRAH-FGFnMPILYNARRHHKEAEERFNARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  89 MKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAANNL 168
Cdd:PRK15409  226 MKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPLSVDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNL 305


                  ....*.
gi 1046889495 169 LAGLRG 174
Cdd:PRK15409  306 IDALQG 311

2-Hacid_dh_6

cd12165

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

6-177

5.70e-49

Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 160.87 E-value: 5.70e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDF 85
Cdd:cd12165   135 LRGKTVGILGYGHIGREIARLLKAFGMRVIGVS-RSPKEDEGADFVGTLSDLDEALEQADVVVVALPLTKQTRGLIGAAE 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDV--TTPEP----LPPSHPLLTLKNCVILPHIGSATYKTRNT 159
Cdd:cd12165   214 LAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwRYPSRgdpvAPSRYPFHELPNVIMSPHNAGWTEETFRR 293

                         170
                  ....*....|....*...
gi 1046889495 160 MSLLAANNLLAGLRGEPM 177
Cdd:cd12165   294 RIDEAAENIRRYLRGEPL 311

2-Hacid_dh_7

cd12166

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

5-176

5.45e-47

Pssm-ID: 240643 [Multi-domain] Cd Length: 300 Bit Score: 155.44 E-value: 5.45e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   5 GLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAefqaefVPIAQLAA---ESDFIVVSCSLTPATRGLC 81
Cdd:cd12166   129 SLADRRVLIVGYGSIGRAIERRLAPFEV-RVTRVARTARPGEQV------HGIDELPAllpEADVVVLIVPLTDETRGLV 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAgLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:cd12166   202 DAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLRAA-LDVTDPEPLPPGHPLWSAPGVLITPHVGGATPAFLPRAY 280

                         170
                  ....*....|....*
gi 1046889495 162 LLAANNLLAGLRGEP 176
Cdd:cd12166   281 ALVRRQLRRYAAGEP 295

GDH_like_1

cd12161

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...

3-176

1.14e-46

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: 155.07 E-value: 1.14e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRpQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:cd12161   139 GRELAGKTVGIVGTGAIGLRVARLFKAFGC-KVLAYSRSEK-EEAKALGIEYVSLDELLAESDIVSLHLPLNDETKGLIG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPE-PLPPSHPLLTLKNCVILPHIGSATYKTRNTMS 161
Cdd:cd12161   217 KEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEpPLPADYPLLHAPNTILTPHVAFATEEAMEKRA 296

                         170
                  ....*....|....*
gi 1046889495 162 LLAANNLLAGLRGEP 176
Cdd:cd12161   297 EIVFDNIEAWLAGKP 311

PGDH_1

cd12155

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...

6-166

3.12e-46

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: 153.89 E-value: 3.12e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQrfLY----TGRqprpqEAAEFQaEFVPIAQL---AAESDFIVVSCSLTPATR 78
Cdd:cd12155   133 LYGKTILFLGTGSIGQEIAKRLKAFGMK--VIgvntSGR-----DVEYFD-KCYPLEELdevLKEADIVVNVLPLTEETH 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  79 GLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHI-GSATYKTR 157
Cdd:cd12155   205 HLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLPKDSPLWDLDNVLITPHIsGVSEHFNE 284


                  ....*....
gi 1046889495 158 NTMSLLAAN 166
Cdd:cd12155   285 RLFDIFYEN 293

PGDH_2

cd05303

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...

6-170

6.97e-46

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: 152.69 E-value: 6.97e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDF 85
Cdd:cd05303   137 LRGKTLGIIGFGRIGREVAKIARALGM-NVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKE 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPlPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAA 165
Cdd:cd05303   216 LELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEP-PPGSKLLELPNVSLTPHIGASTKEAQERIGEELA 294


                  ....*
gi 1046889495 166 NNLLA 170
Cdd:cd05303   295 NKIIE 299

2-Hacid_dh_15

cd12180

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...

6-177

3.06e-44

Pssm-ID: 240657 Cd Length: 308 Bit Score: 148.64 E-value: 3.06e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAeFVPIAQLAAESDFIVVSCSLTPATRGLCNKDF 85
Cdd:cd12180   133 LAGSTLGIVGFGAIGQALARRALALGM-RVLALRRSGRPSDVPGVEA-AADLAELFARSDHLVLAAPLTPETRHLINADV 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAA 165
Cdd:cd12180   211 LAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLPEGHPLYTHPRVRLSPHTSAIAPDGRRNLADRFL 290

                         170
                  ....*....|..
gi 1046889495 166 NNLLAGLRGEPM 177
Cdd:cd12180   291 ENLARYRAGQPL 302

PTDH

cd12157

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...

3-174

5.46e-44

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: 148.20 E-value: 5.46e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQP-RPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12157   139 GTGLDGKTVGILGMGALGRAIARRLSGFGA-TLLYYDPHPlDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLI 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPE-------PLPPSHPLLTLKNCVIL-PHIGSAT 153
Cdd:cd12157   218 NAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEMEdwarpdrPRSIPQELLDQHDRTVFtPHIGSAV 297

                         170       180
                  ....*....|....*....|.
gi 1046889495 154 YKTRNTMSLLAANNLLAGLRG 174
Cdd:cd12157   298 DEVRLEIELEAALNILQALQG 318

GDH_like_2

cd12164

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...

7-178

1.52e-43

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: 146.49 E-value: 1.52e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   7 SESTVGIVGLGRIGQAIARRLKPFGvqrFLYTG--RQPRPQEAAEfqaEFVPIAQLA---AESDfIVVSC-SLTPATRGL 80
Cdd:cd12164   131 AERRVGVLGLGELGAAVARRLAALG---FPVSGwsRSPKDIEGVT---CFHGEEGLDaflAQTD-ILVCLlPLTPETRGI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYktRNTM 160
Cdd:cd12164   204 LNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLPADHPLWRHPRVTVTPHIAAITD--PDSA 281

                         170
                  ....*....|....*...
gi 1046889495 161 SLLAANNLLAGLRGEPMP 178
Cdd:cd12164   282 AAQVAENIRRLEAGEPLP 299

2-Hacid_dh

pfam00389

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...

3-182

8.45e-42

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: 142.43 E-value: 8.45e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFG---VQRFLYTGRQPRPQEAAEFQAEFVpIAQLAAESDFIVVSCSLTPATRG 79
Cdd:pfam00389 130 GLELYGKTLGVIGGGGIGGGVAAIAKAFGmgvVAYDPYPNPERAEAGGVEVLSLLL-LLLDLPESDDVLTVNPLTTMKTG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNT 159
Cdd:pfam00389 209 VIIINEARGMLKDAVAIINAAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQER 288

                         170       180
                  ....*....|....*....|...
gi 1046889495 160 MSLLAANNLLAGLRGEPMPSELK 182
Cdd:pfam00389 289 IAEEAAENILAFLDGGPPANAVN 311

PGDH_like_1

cd12169

Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...

3-174

4.04e-41

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: 140.34 E-value: 4.04e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQPRPQEAAEFQAEF-VPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12169   137 GTGLAGKTLGIVGLGRIGARVARIGQAFGM-RVIAWSSNLTAERAAAAGVEAaVSKEELFATSDVVSLHLVLSDRTRGLV 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGsatYKTRNTMS 161
Cdd:cd12169   216 GAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEPLPADHPLRGLPNVLLTPHIG---YVTEEAYE 292

                         170
                  ....*....|....*.
gi 1046889495 162 LL---AANNLLAGLRG 174
Cdd:cd12169   293 GFygqAVENIAAWLAG 308

FDH

cd05302

NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...

4-153

1.81e-39

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: 137.07 E-value: 1.81e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVQRfLYTGRQPRPQEA-AEFQAEFVP-IAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd05302   158 YDLEGKTVGTVGAGRIGLRVLRRLKPFDVHL-LYYDRHRLPEEVeKELGLTRHAdLEDMVSKCDVVTINCPLHPETEGLF 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSAT 153
Cdd:cd05302   237 NKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPAPKDHPWRTMPNNAMTPHISGTT 308

LDH_like

cd01619

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...

6-176

1.20e-38

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: 134.35 E-value: 1.20e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQP-RPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKD 84
Cdd:cd01619   141 LEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAY---DPfRNPELEDKGVKYVSLEELFKNSDIISLHVPLTPENHHMINEE 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  85 FFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDV-----------TTPEPLPPS--HPLLTLKNCVILPHIGS 151
Cdd:cd01619   218 AFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDVledetpdllkdLEGEIFKDAlnALLGRRPNVIITPHTAF 297

                         170       180
                  ....*....|....*....|....*
gi 1046889495 152 ATYKTRNTMSLLAANNLLAGLRGEP 176
Cdd:cd01619   298 YTDDALKNMVEISCENIVDFLEGEE 322

2-Hacid_dh_5

cd12163

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

10-177

1.84e-37

Pssm-ID: 240640 Cd Length: 334 Bit Score: 131.63 E-value: 1.84e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPQEAAEFQAEFV-----------PIAQ------------LAAESDF 66
Cdd:cd12163   135 RVGILGYGSIGRQTARLAQALGMEVYAYT-RSPRPTPESRKDDGYIvpgtgdpdgsiPSAWfsgtdkaslhefLRQDLDL 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  67 IVVSCSLTPATRGLCNKDFFQKM-KNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVI 145
Cdd:cd12163   214 LVVSLPLTPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLPADHPLWSAPNVII 293

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1046889495 146 LPHIGSAT--YKTRnTMSLLAANnlLAGLR-GEPM 177
Cdd:cd12163   294 TPHVSWQTqeYFDR-ALDVLEEN--LERLRkGEPL 325

PRK07574

NAD-dependent formate dehydrogenase;

4-180

7.53e-36

NAD-dependent formate dehydrogenase;

Pssm-ID: 181041 Cd Length: 385 Bit Score: 128.64 E-value: 7.53e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQpRPQEAAEFQAE---FVPIAQLAAESDFIVVSCSLTPATRGL 80
Cdd:PRK07574  188 YDLEGMTVGIVGAGRIGLAVLRRLKPFDV-KLHYTDRH-RLPEEVEQELGltyHVSFDSLVSVCDVVTIHCPLHPETEHL 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  81 CNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSatyktrntM 160
Cdd:PRK07574  266 FDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQPAPADHPWRTMPRNGMTPHISG--------T 337

                         170       180
                  ....*....|....*....|....*...
gi 1046889495 161 SLLAANNLLAGLR--------GEPMPSE 180
Cdd:PRK07574  338 TLSAQARYAAGTReilecffeGRPIRDE 365

LDH_like_2

cd12183

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...

3-125

1.77e-32

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: 118.32 E-value: 1.77e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQPRP-QEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12183   139 GFDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAY---DPYPnPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLI 215

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDV 125
Cdd:cd12183   216 NAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDV 259

PRK08410

D-2-hydroxyacid dehydrogenase;

6-175

4.95e-32

D-2-hydroxyacid dehydrogenase;

Pssm-ID: 181414 [Multi-domain] Cd Length: 311 Bit Score: 117.01 E-value: 4.95e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgrqprpQEAAEFQAEF--VPIAQLAAESDFIVVSCSLTPATRGLCNK 83
Cdd:PRK08410  143 IKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYYS------TSGKNKNEEYerVSLEELLKTSDIISIHAPLNEKTKNLIAY 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  84 DFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIaAAGLDVTTPEPLPPSHPLLTLKN---CVILPHIGSATYKTRNTM 160
Cdd:PRK08410  217 KELKLLKDGAILINVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKEPMEKNHPLLSIKNkekLLITPHIAWASKEARKTL 295

                         170
                  ....*....|....*
gi 1046889495 161 SLLAANNLLAGLRGE 175
Cdd:PRK08410  296 IEKVKENIKDFLEGG 310

LDH_like_1

cd12187

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...

3-150

8.23e-32

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: 116.61 E-value: 8.23e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:cd12187   134 GFELAGKTLGVVGTGRIGRRVARIARGFGMKVLAYD-VVPDEELAERLGFRYVSLEELLQESDIISLHVPYTPQTHHLIN 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPL------------PP--------SHPLLTLKN 142
Cdd:cd12187   213 RENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVlreeaelfredvSPedlkkllaDHALLRKPN 292


                  ....*...
gi 1046889495 143 CVILPHIG 150
Cdd:cd12187   293 VIITPHVA 300

LDH

cd12186

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...

10-150

8.69e-32

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: 116.48 E-value: 8.69e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPqEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQKM 89
Cdd:cd12186   147 TVGIIGTGRIGSAAAKIFKGFGAKVIAYD-PYPNP-ELEKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKM 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046889495  90 KNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVT-----------TPEPLPPS--HPLLTLKNCVILPHIG 150
Cdd:cd12186   225 KDGAILVNAARGGLVDTKALIDALDSGKIAGAALDTYenetgyfnkdwSGKEIEDEvlKELIAMPNVLITPHIA 298

PLN02928

oxidoreductase family protein

3-176

3.56e-31

oxidoreductase family protein

Pssm-ID: 215501 Cd Length: 347 Bit Score: 115.55 E-value: 3.56e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGV-----QRFLYTGRQPRPQEAAEFQAEFV-------PIAQLAAESDFIVVS 70
Cdd:PLN02928  154 GDTLFGKTVFILGYGAIGIELAKRLRPFGVkllatRRSWTSEPEDGLLIPNGDVDDLVdekggheDIYEFAGEADIVVLC 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  71 CSLTPATRGLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIG 150
Cdd:PLN02928  234 CTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDDPILKHPNVIITPHVA 313

                         170       180
                  ....*....|....*....|....*.
gi 1046889495 151 SATYKTRNTMSLLAANNLLAGLRGEP 176
Cdd:PLN02928  314 GVTEYSYRSMGKIVGDAALQLHAGRP 339

PGDH_like_3

cd12174

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...

3-153

5.60e-31

Pssm-ID: 240651 [Multi-domain] Cd Length: 305 Bit Score: 113.81 E-value: 5.60e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPQEAAEFQAEFVP---IAQLAAESDFIVVSCSLTPATRG 79
Cdd:cd12174   130 GTELRGKTLGVIGLGNIGRLVANAALALGMKVIGYD-PYLSVEAAWKLSVEVQRvtsLEELLATADYITLHVPLTDETRG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLpPSHPlltlkNCVILPHIGSAT 153
Cdd:cd12174   209 LINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPALL-GHLP-----NVIATPHLGAST 276

HGDH_LDH_like

cd12185

Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...

2-149

2.07e-30

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: 112.69 E-value: 2.07e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   2 CGYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12185   137 QGRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAY---DPYPNEEVKKYAEYVDLDTLYKESDIITLHTPLTEETYHLI 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPE-----------PLpPSHPLLTLK---NCVILP 147
Cdd:cd12185   214 NKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEdgiyyndrkgdIL-SNRELAILRsfpNVILTP 292


                  ..
gi 1046889495 148 HI 149
Cdd:cd12185   293 HM 294

PRK06487

2-hydroxyacid dehydrogenase;

6-176

1.16e-28

2-hydroxyacid dehydrogenase;

Pssm-ID: 180588 [Multi-domain] Cd Length: 317 Bit Score: 108.25 E-value: 1.16e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFL--YTGRQPRPQEaaefqaefVPIAQLAAESDFIVVSCSLTPATRGLCNK 83
Cdd:PRK06487  146 LEGKTLGLLGHGELGGAVARLAEAFGMRVLIgqLPGRPARPDR--------LPLDELLPQVDALTLHCPLTEHTRHLIGA 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  84 DFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLT--LKNCVILPHIGSATYKTRNTMS 161
Cdd:PRK06487  218 RELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVEPPVNGNPLLApdIPRLIVTPHSAWGSREARQRIV 297

                         170
                  ....*....|....*
gi 1046889495 162 LLAANNLLAGLRGEP 176
Cdd:PRK06487  298 GQLAENARAFFAGKP 312

2-Hacid_dh_14

cd12179

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...

3-153

1.08e-27

Pssm-ID: 240656 [Multi-domain] Cd Length: 306 Bit Score: 105.45 E-value: 1.08e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEaaefQAEFVPIAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:cd12179   133 GVELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDA----YAEQVSLETLFKEADILSLHIPLTPETRGMVN 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDV--------TTPEPLPPSHPLLTLKNCVIL-PHIGSAT 153
Cdd:cd12179   209 KEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVleyekasfESIFNQPEAFEYLIKSPKVILtPHIAGWT 288

ErythrP_dh

cd12158

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...

6-159

1.29e-27

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: 105.69 E-value: 1.29e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQPrPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTP----ATRGLC 81
Cdd:cd12158   113 LKGKTVGIVGVGNVGSRLARRLEALGMNVLLC---DP-PRAEAEGDPGFVSLEELLAEADIITLHVPLTRdgehPTYHLL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  82 NKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPlppsHPLLTLKNCVIL--PHIgsATY----K 155
Cdd:cd12158   189 DEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP----EIDLELLDKVDIatPHI--AGYslegK 262


                  ....
gi 1046889495 156 TRNT 159
Cdd:cd12158   263 ARGT 266

PLN03139

formate dehydrogenase; Provisional

4-153

1.36e-27

formate dehydrogenase; Provisional

Pssm-ID: 178684 Cd Length: 386 Bit Score: 106.47 E-value: 1.36e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVP-IAQLAAESDFIVVSCSLTPATRGLCN 82
Cdd:PLN03139  195 YDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPELEKETGAKFEEdLDAMLPKCDVVVINTPLTEKTRGMFN 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046889495  83 KDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSAT 153
Cdd:PLN03139  275 KERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAPKDHPWRYMPNHAMTPHISGTT 345

HGDH_like

cd12184

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...

9-153

1.39e-26

(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: 102.76 E-value: 1.39e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   9 STVGIVGLGRIGQAIARRLKPFGVQRFLYtgrQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRG-LCNKDFFQ 87
Cdd:cd12184   146 STVGIIGTGRIGLTAAKLFKGLGAKVIGY---DIYPSDAAKDVVTFVSLDELLKKSDIISLHVPYIKGKNDkLINKEFIS 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  88 KMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPE-------------PLPPSHPLLTLKNCVIL-PHIGSAT 153
Cdd:cd12184   223 KMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNEkeiffkdfdgdkiEDPVVEKLLDLYPRVLLtPHIGSYT 302

PGDH_3

cd12176

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...

10-153

1.80e-26

Pssm-ID: 240653 Cd Length: 304 Bit Score: 101.89 E-value: 1.80e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEfqaEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQKM 89
Cdd:cd12176   142 TLGIIGYGHIGSQLSVLAEALGMRVIFYDIAEKLPLGNAR---QVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQM 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046889495  90 KNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPL----PPSHPLLTLKNCVILPHIGSAT 153
Cdd:cd12176   219 KKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPAsngePFSSPLQGLPNVILTPHIGGST 286

2-Hacid_dh_3

cd12160

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

11-177

8.65e-23

Pssm-ID: 240637 Cd Length: 310 Bit Score: 92.44 E-value: 8.65e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  11 VGIVGLGRIGQAIARRLKPFGVQrflYTGRQPRPQEAAEFqaEFVPIAQLAA---ESDFIVVSCSLTPATRGLCNKDFFQ 87
Cdd:cd12160   146 VLIWGFGSIGQRLAPLLTALGAR---VTGVARSAGERAGF--PVVAEDELPEllpETDVLVMILPATPSTAHALDAEVLA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  88 KMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHigSATYKTRNTMSLLAAnN 167
Cdd:cd12160   221 ALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLPASSPLWDAPNLILTPH--AAGGRPQGAEELIAE-N 297

                         170
                  ....*....|
gi 1046889495 168 LLAGLRGEPM 177
Cdd:cd12160   298 LRAFLAGGPL 307

PLN02306

hydroxypyruvate reductase

6-177

2.48e-22

hydroxypyruvate reductase

Pssm-ID: 177941 Cd Length: 386 Bit Score: 92.23 E-value: 2.48e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIAR-------------------RLKPF--GVQRFLYT-GRQPRPQEAAEFQAEFVpiaqlaAE 63
Cdd:PLN02306  163 LKGQTVGVIGAGRIGSAYARmmvegfkmnliyydlyqstRLEKFvtAYGQFLKAnGEQPVTWKRASSMEEVL------RE 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  64 SDFIVVSCSLTPATRGLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEP-LPPShpLLTLKN 142
Cdd:PLN02306  237 ADVISLHPVLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPyMKPG--LADMKN 314

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1046889495 143 CVILPHIGSATYKTRNTMSLLAANNLLAGLRGEPM 177
Cdd:PLN02306  315 AVVVPHIASASKWTREGMATLAALNVLGKLKGYPV 349

PRK00257

4-phosphoerythronate dehydrogenase PdxB;

3-181

1.62e-20

4-phosphoerythronate dehydrogenase PdxB;

Pssm-ID: 166874 [Multi-domain] Cd Length: 381 Bit Score: 87.01 E-value: 1.62e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLytgRQPrPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTP----ATR 78
Cdd:PRK00257  111 GVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLV---CDP-PRQEAEGDGDFVSLERILEECDVISLHTPLTKegehPTR 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  79 GLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLppSHPLLtLKNCVI-LPHIG--SATYK 155
Cdd:PRK00257  187 HLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQ--IDLEL-ADLCTIaTPHIAgySLDGK 263

                         170       180
                  ....*....|....*....|....*.
gi 1046889495 156 TRNTMSLLAAnnlLAGLRGEPMPSEL 181
Cdd:PRK00257  264 ARGTAQIYQA---LCRFFGIPARVSL 286

PRK11790

phosphoglycerate dehydrogenase;

59-153

2.53e-16

phosphoglycerate dehydrogenase;

Pssm-ID: 236985 [Multi-domain] Cd Length: 409 Bit Score: 75.60 E-value: 2.53e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  59 QLAAESDFIvvscSL----TPATRGLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPL--- 131
Cdd:PRK11790  199 ELLAQSDVV----SLhvpeTPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKsng 274

                          90       100
                  ....*....|....*....|....
gi 1046889495 132 -PPSHPLLTLKNcVIL-PHIGSAT 153
Cdd:PRK11790  275 dPFESPLRGLDN-VILtPHIGGST 297

ghrA

PRK15469

glyoxylate/hydroxypyruvate reductase GhrA;

4-153

4.79e-15

glyoxylate/hydroxypyruvate reductase GhrA;

Pssm-ID: 185366 Cd Length: 312 Bit Score: 71.37 E-value: 4.79e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVQ-RFLYTGRQPRPQEAAefqaeFVPIAQLAAESDFIVVSCSL---TPATRG 79
Cdd:PRK15469  132 YHREDFTIGILGAGVLGSKVAQSLQTWGFPlRCWSRSRKSWPGVQS-----FAGREELSAFLSQTRVLINLlpnTPETVG 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046889495  80 LCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSAT 153
Cdd:PRK15469  207 IINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLPPESPLWQHPRVAITPHVAAVT 280

FDH_GDH_like

cd12154

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...

4-137

1.72e-14

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: 69.95 E-value: 1.72e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   4 YGLSESTVGIVGLGRIGQAIARRLKPFGVqRFLYTGRQP--RPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLC 81
Cdd:cd12154   156 PDVAGKTVVVVGAGVVGKEAAQMLRGLGA-QVLITDINVeaLEQLEELGGKNVEELEEALAEADVIVTTTLLPGKRAGIL 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046889495  82 N-KDFFQKMKNTAVFINISRGDVVNQEDLY-QALASGQIAAAGLDVTTPEPLPPS-HPL 137
Cdd:cd12154   235 VpEELVEQMKPGSVIVNVAVGAVGCVQALHtQLLEEGHGVVHYGDVNMPGPGCAMgVPW 293

PRK06436

2-hydroxyacid dehydrogenase;

6-176

8.77e-14

2-hydroxyacid dehydrogenase;

Pssm-ID: 235800 [Multi-domain] Cd Length: 303 Bit Score: 67.60 E-value: 8.77e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRPQEAAEFQAEFVPIAQlaaESDFIVVSCSLTPATRGLCNKDF 85
Cdd:PRK06436  120 LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYT-RSYVNDGISSIYMEPEDIMK---KSDFVLISLPLTDETRGMINSKM 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  86 FQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHpllTLKNCVILPHIGSATykTRNTMSL--- 162
Cdd:PRK06436  196 LSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITET---NPDNVILSPHVAGGM--SGEIMQPava 270

                         170
                  ....*....|....
gi 1046889495 163 LAANNLLAGLRGEP 176
Cdd:PRK06436  271 LAFENIKNFFEGKP 284

PRK08605

D-lactate dehydrogenase; Validated

6-124

7.46e-13

D-lactate dehydrogenase; Validated

Pssm-ID: 181499 Cd Length: 332 Bit Score: 65.15 E-value: 7.46e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRL-KPFGvqrFLYTGRQPRPQEAAEFQAEFV-PIAQLAAESDFIVVSCSLTPATRGLCNK 83
Cdd:PRK08605  144 IKDLKVAVIGTGRIGLAVAKIFaKGYG---SDVVAYDPFPNAKAATYVDYKdTIEEAVEGADIVTLHMPATKYNHYLFNA 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046889495  84 DFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLD 124
Cdd:PRK08605  221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALD 261

PRK15438

erythronate-4-phosphate dehydrogenase PdxB; Provisional

3-130

1.88e-12

erythronate-4-phosphate dehydrogenase PdxB; Provisional

Pssm-ID: 185335 [Multi-domain] Cd Length: 378 Bit Score: 64.54 E-value: 1.88e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   3 GYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgrQPRPQEAAEfqAEFVPIAQLAAESDFIVVSCSLTP----ATR 78
Cdd:PRK15438  111 GFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCD--PPRADRGDE--GDFRSLDELVQEADILTFHTPLFKdgpyKTL 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046889495  79 GLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEP 130
Cdd:PRK15438  187 HLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP 238

PRK12480

D-lactate dehydrogenase; Provisional

10-124

3.54e-11

D-lactate dehydrogenase; Provisional

Pssm-ID: 183550 Cd Length: 330 Bit Score: 60.70 E-value: 3.54e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQrflYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQKM 89
Cdd:PRK12480  148 TVAIIGTGRIGAATAKIYAGFGAT---ITAYDAYPNKDLDFLTYKDSVKEAIKDADIISLHVPANKESYHLFDKAMFDHV 224

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1046889495  90 KNTAVFINISRGDVVNQEDLYQALASGQIAAAGLD 124
Cdd:PRK12480  225 KKGAILVNAARGAVINTPDLIAAVNDGTLLGAAID 259

2-Hacid_dh_9

cd12170

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...

6-168

1.02e-10

Pssm-ID: 240647 [Multi-domain] Cd Length: 294 Bit Score: 58.85 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTgRQPRP-QEAAEFqaEFVPIAQLAAESDFIvvsCSLTPATRGLCNKD 84
Cdd:cd12170   136 LTGLKVGIIGLGTTGQMIADALSFFGADVYYYS-RTRKPdAEAKGI--RYLPLNELLKTVDVI---CTCLPKNVILLGEE 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  85 FFQKMKNTAVFINISRGDVVNQEDLYQALASGQIA------AAGLdvttpeplpPSHPLLTLKNCVILPHIGSATYKTRN 158
Cdd:cd12170   210 EFELLGDGKILFNTSLGPSFEVEALKKWLKASGYNifdcdtAGAL---------GDEELLRYPNVICTNKSAGWTRQAFE 280

                         170
                  ....*....|
gi 1046889495 159 TMSLLAANNL 168
Cdd:cd12170   281 RLSQKVLANL 290

PRK13302

aspartate dehydrogenase;

5-127

8.19e-06

aspartate dehydrogenase;

Pssm-ID: 237341 [Multi-domain] Cd Length: 271 Bit Score: 44.85 E-value: 8.19e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495   5 GLSESTVGIVGLGRIGQAIARRL---------------KPFGVQRFLYTGRQPRPqeaaefqaeFVPIAQLAAESDfIVV 69
Cdd:PRK13302    3 SRPELRVAIAGLGAIGKAIAQALdrglpgltlsavavrDPQRHADFIWGLRRPPP---------VVPLDQLATHAD-IVV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046889495  70 SCSLTPATRGLCnKDFFQKMKNTAVfinISRGDVVNQEDLYQ--ALASGQI-----AAAGLDVTT 127
Cdd:PRK13302   73 EAAPASVLRAIV-EPVLAAGKKAIV---LSVGALLRNEDLIDlaRQNGGQIivptgALLGLDAVT 133

F420_oxidored

pfam03807

NADP oxidoreductase coenzyme F420-dependent;

12-71

9.31e-05

NADP oxidoreductase coenzyme F420-dependent;

Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 39.52 E-value: 9.31e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046889495  12 GIVGLGRIGQAIARRLKPFGVQRFLYTGRqPRPQEAAEFQAEF------VPIAQLAAESDFIVVSC 71
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEVVVANS-RNPEKAEELAEEYgvgataVDNEEAAEEADVVFLAV 65

hemA

PRK00045

glutamyl-tRNA reductase; Reviewed

6-72

2.24e-04

glutamyl-tRNA reductase; Reviewed

Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 40.94 E-value: 2.24e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046889495   6 LSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTGR-QPRPQE-AAEFQAEFVPIAQLA---AESDfIVVSCS 72
Cdd:PRK00045  180 LSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRtLERAEElAEEFGGEAIPLDELPealAEAD-IVISST 250

MurD

COG0771

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...

10-70

6.14e-04

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis

Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 39.29 E-value: 6.14e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVPI------AQLAAESDFIVVS 70
Cdd:COG0771     6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVvlgehpEELLDGADLVVKS 72

MmsB

COG2084

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...

10-114

6.21e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];

Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 39.33 E-value: 6.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVP-IAQLAAESDFIVVSCSLTPATRGLCNKD--FF 86
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAAsPAEAAAAADVVITMLPDDAAVEEVLLGEdgLL 82

                          90       100
                  ....*....|....*....|....*...
gi 1046889495  87 QKMKNTAVFINISRGDVVNQEDLYQALA 114
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAA 110

COG2085

Predicted dinucleotide-binding enzyme [General function prediction only];

11-70

5.44e-03

Predicted dinucleotide-binding enzyme [General function prediction only];

Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 36.30 E-value: 5.44e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046889495  11 VGIVGLGRIGQAIARRLKPFGVQRFLyTGRQP-RPQEAAEF---QAEFVPIAQLAAESDFIVVS 70
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVI-GSRDPeKAAALAAElgpGARAGTNAEAAAAADVVVLA 63

NAD_binding_2

pfam03446

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...

10-114

8.14e-03

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.

Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 35.14 E-value: 8.14e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046889495  10 TVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVP-IAQLAAESDFIVVSCSLTPATRG-LCNKDFFQ 87
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAsPAEFVAGLDVVITMVPAGAAVDAvIFGEGLLP 80

                          90       100
                  ....*....|....*....|....*..
gi 1046889495  88 KMKNTAVFINISRGDVVNQEDLYQALA 114
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELK 107

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