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Conserved domains on  [gi|1393936758|gb|AWO49524|]
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phosphonate dehydrogenase (plasmid) [Klebsiella pneumoniae]

Protein Classification

phosphonate dehydrogenase( domain architecture ID 10187373)

phosphonate dehydrogenase PtxD catalyzes the NAD(+)-dependent conversion of phosphite to phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
2-318 0e+00

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: 557.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   2 LPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:cd12157     1 KPKVVITHKVHPEVLELLKPHCEVISNQTDEPLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd12157    81 DVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGGWRPKFYGTGLDGKTVGILGMGALGRAIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVV 241
Cdd:cd12157   161 RRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936758 242 DEAAVLAALERGQLGGYAADVFEMEDWARADRPR-LIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd12157   241 DEAAVAEALKSGHLGGYAADVFEMEDWARPDRPRsIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
 
Name Accession Description Interval E-value
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
2-318 0e+00

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: 557.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   2 LPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:cd12157     1 KPKVVITHKVHPEVLELLKPHCEVISNQTDEPLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd12157    81 DVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGGWRPKFYGTGLDGKTVGILGMGALGRAIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVV 241
Cdd:cd12157   161 RRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936758 242 DEAAVLAALERGQLGGYAADVFEMEDWARADRPR-LIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd12157   241 DEAAVAEALKSGHLGGYAADVFEMEDWARPDRPRsIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
4-326 1.81e-112

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: 328.97  E-value: 1.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVIT--HRVHDEILQLLA-PHCELVTNqtDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDN 80
Cdd:COG1052     2 PILVLdpRTLPDEVLERLEaEHFEVTVY--EDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  81 FDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAIGLAM 160
Cdd:COG1052    80 IDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWS-WSPGLLGRDLSGKTLGIIGLGRIGQAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 161 AERLQGWGATLQYHEAKALDTQTEqrLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSV 240
Cdd:COG1052   159 ARRAKGFGMKVLYYDRSPKPEVAE--LGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 241 VDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGAR 320
Cdd:COG1052   237 VDEAALIEALKSGRIAGAGLDVFEEE-------PPPPDHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEP 309

                  ....*.
gi 1393936758 321 PINAAN 326
Cdd:COG1052   310 PPNPVN 315
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
6-326 1.47e-75

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: 234.88  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   6 VITHRVHDEILQLLAPHcELVTNQTdstLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDA 85
Cdd:pfam00389   2 LILDPLSPEALELLKEG-EVEVHDE---LLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  86 CTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQ 165
Cdd:pfam00389  78 ATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 166 GWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAA 245
Cdd:pfam00389 158 GMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDLPESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 246 VLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPINAA 325
Cdd:pfam00389 238 ALDALLEEGIAAAADLDVEEE-------PPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAV 310

                  .
gi 1393936758 326 N 326
Cdd:pfam00389 311 N 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
1-327 2.90e-75

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 234.69  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   1 MLPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDN 80
Cdd:PRK13243    1 MKPKVFITREIPENGIEMLEEHFEVEVWEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  81 FDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQ----GWQPQ-FYGTGLDNATVGILGMGA 155
Cdd:PRK13243   81 IDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKrrgvAWHPLmFLGYDVYGKTIGIIGFGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 156 IGLAMAERLQGWGATLQYHeAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNP 235
Cdd:PRK13243  161 IGQAVARRAKGFGMRILYY-SRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 236 CRGSVVDEAAVLAALERGQLGGYAADVFEMEDwaradrprLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQV 315
Cdd:PRK13243  240 ARGKVVDTKALVKALKEGWIAGAGLDVFEEEP--------YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAF 311
                         330
                  ....*....|..
gi 1393936758 316 LAGARPINAANR 327
Cdd:PRK13243  312 KRGEVPPTLVNR 323
 
Name Accession Description Interval E-value
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
2-318 0e+00

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: 557.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   2 LPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:cd12157     1 KPKVVITHKVHPEVLELLKPHCEVISNQTDEPLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd12157    81 DVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGGWRPKFYGTGLDGKTVGILGMGALGRAIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVV 241
Cdd:cd12157   161 RRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936758 242 DEAAVLAALERGQLGGYAADVFEMEDWARADRPR-LIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd12157   241 DEAAVAEALKSGHLGGYAADVFEMEDWARPDRPRsIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
4-326 1.81e-112

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: 328.97  E-value: 1.81e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVIT--HRVHDEILQLLA-PHCELVTNqtDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDN 80
Cdd:COG1052     2 PILVLdpRTLPDEVLERLEaEHFEVTVY--EDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  81 FDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAIGLAM 160
Cdd:COG1052    80 IDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWS-WSPGLLGRDLSGKTLGIIGLGRIGQAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 161 AERLQGWGATLQYHEAKALDTQTEqrLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSV 240
Cdd:COG1052   159 ARRAKGFGMKVLYYDRSPKPEVAE--LGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 241 VDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGAR 320
Cdd:COG1052   237 VDEAALIEALKSGRIAGAGLDVFEEE-------PPPPDHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEP 309

                  ....*.
gi 1393936758 321 PINAAN 326
Cdd:COG1052   310 PPNPVN 315
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
3-318 1.57e-105

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: 311.25  E-value: 1.57e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   3 PKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFD 82
Cdd:cd05301     1 PKVLVTRRLPEEALALLREGFEVEVWDEDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  83 VDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQP-QFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd05301    81 VDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSPtLLLGTDLHGKTLGIVGMGRIGQAVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYHEAKALDtQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVV 241
Cdd:cd05301   161 RRAKGFGMKILYHNRSRKP-EAEEELGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVV 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936758 242 DEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd05301   240 DEDALVEALKSGKIAGAGLDVFEPE-------PLPADHPLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
4-315 5.09e-99

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: 294.54  E-value: 5.09e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRV-HDEILQLLAP-HCELVTNQTDSTltrEEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:cd05198     1 KVLVLEPLfPPEALEALEAtGFEVIVADDLLA---DELEALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPqFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd05198    78 DLDAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWGWLWAG-FPGYELEGKTVGIVGLGRIGQRVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYHEAKALDTQTEqRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVV 241
Cdd:cd05198   157 KRLQAFGMKVLYYDRTRKPEPEE-DLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLV 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936758 242 DEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQV 315
Cdd:cd05198   236 DEDALLRALKSGKIAGAALDVFEPE-------PLPADHPLLELPNVILTPHIAGYTEEARERMAEIAVENLERF 302
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
4-317 3.67e-86

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: 261.65  E-value: 3.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVIT----HRVHDEILQLL-APHCELVTNQTDSTLTREEILRRCRDAQAMMAFMpDRVDADFLQACPELRVVGCALKGF 78
Cdd:cd12172     1 KVLVTprsfSKYSEEAKELLeAAGFEVVLNPLGRPLTEEELIELLKDADGVIAGL-DPITEEVLAAAPRLKVISRYGVGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  79 DNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfqgWqPQFYGTGLDNATVGILGMGAIGL 158
Cdd:cd12172    80 DNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGG---W-DRPVGTELYGKTLGIIGLGRIGK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 159 AMAERLQGWGATLQYHEaKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRG 238
Cdd:cd12172   156 AVARRLSGFGMKVLAYD-PYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936758 239 SVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLA 317
Cdd:cd12172   235 GLVDEEALYEALKSGRIAGAALDVFEEE-------PPPADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDVLA 306
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
4-326 2.23e-84

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: 257.43  E-value: 2.23e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLL--APHCELVTNqtdSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:COG0111     2 KILILDDLPPEALEALeaAPGIEVVYA---PGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgwQPQFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:COG0111    79 DLAAATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWD--RSAFRGRELRGKTVGIVGLGRIGRAVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWGATLQYH-----EAKALDTQTEQRLGLRqvacsELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPC 236
Cdd:COG0111   157 RRLRAFGMRVLAYdpspkPEEAADLGVGLVDSLD-----ELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 237 RGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVL 316
Cdd:COG0111   232 RGGVVDEDALLAALDSGRLAGAALDVFEPE-------PLPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFL 304
                         330
                  ....*....|
gi 1393936758 317 AGARPINAAN 326
Cdd:COG0111   305 AGEPLRNLVN 314
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
4-326 7.84e-84

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


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 256.01  E-value: 7.84e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDV 83
Cdd:cd12178     2 KVLVTGWIPKEALEELEENFEVTYYDGLGLISKEELLERIADYDALITPLSTPVDKEIIDAAKNLKIIANYGAGFDNIDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  84 DACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFY-GTGLDNATVGILGMGAIGLAMAE 162
Cdd:cd12178    82 DYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRGGFLGWAPLFFlGHELAGKTLGIIGMGRIGQAVAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 163 RLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVD 242
Cdd:cd12178   162 RAKAFGMKILYYNRHRLSEETEKELGATYVDLDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 243 EAAVLAALERGQLGGYAADVFEMEDWaradrprlIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPI 322
Cdd:cd12178   242 EKALVDALKTGEIAGAALDVFEFEPE--------VSPELKKLDNVILTPHIGNATVEARDAMAKEAADNIISFLEGKRPK 313

                  ....
gi 1393936758 323 NAAN 326
Cdd:cd12178   314 NIVN 317
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
4-318 8.47e-78

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: 240.40  E-value: 8.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLLAPH-CELVTnqtDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFD 82
Cdd:cd12173     1 KVLVTDPIDEEGLELLREAgIEVDV---APGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNID 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  83 VDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFqgWQPQFYGTGLDNATVGILGMGAIGLAMAE 162
Cdd:cd12173    78 VEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKW--DRKKFMGVELRGKTLGIVGLGRIGREVAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 163 RLQGWGATLQYH-----EAKALDtqteqrLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCR 237
Cdd:cd12173   156 RARAFGMKVLAYdpyisAERAAA------GGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTAR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 238 GSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGS----AVRAVRLEiercAAQNII 313
Cdd:cd12173   230 GGIVDEAALADALKSGKIAGAALDVFEQE-------PPPADSPLLGLPNVILTPHLGAsteeAQERVAVD----AAEQVL 298

                  ....*
gi 1393936758 314 QVLAG 318
Cdd:cd12173   299 AVLAG 303
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
6-326 1.47e-75

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: 234.88  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   6 VITHRVHDEILQLLAPHcELVTNQTdstLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDA 85
Cdd:pfam00389   2 LILDPLSPEALELLKEG-EVEVHDE---LLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  86 CTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQ 165
Cdd:pfam00389  78 ATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 166 GWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAA 245
Cdd:pfam00389 158 GMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDLPESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 246 VLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPINAA 325
Cdd:pfam00389 238 ALDALLEEGIAAAADLDVEEE-------PPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAV 310

                  .
gi 1393936758 326 N 326
Cdd:pfam00389 311 N 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
1-327 2.90e-75

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 234.69  E-value: 2.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   1 MLPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDN 80
Cdd:PRK13243    1 MKPKVFITREIPENGIEMLEEHFEVEVWEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  81 FDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQ----GWQPQ-FYGTGLDNATVGILGMGA 155
Cdd:PRK13243   81 IDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKrrgvAWHPLmFLGYDVYGKTIGIIGFGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 156 IGLAMAERLQGWGATLQYHeAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNP 235
Cdd:PRK13243  161 IGQAVARRAKGFGMRILYY-SRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 236 CRGSVVDEAAVLAALERGQLGGYAADVFEMEDwaradrprLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQV 315
Cdd:PRK13243  240 ARGKVVDTKALVKALKEGWIAGAGLDVFEEEP--------YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAF 311
                         330
                  ....*....|..
gi 1393936758 316 LAGARPINAANR 327
Cdd:PRK13243  312 KRGEVPPTLVNR 323
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
4-321 1.88e-73

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


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 229.38  E-value: 1.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLL------APHCELVTnqtdsTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKG 77
Cdd:cd12175     1 KVLFLGPEFPDAEELLrallppAPGVEVVT-----AAELDEEAALLADADVLVPGMRKVIDAELLAAAPRLRLIQQPGVG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  78 FDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfQGWQPQFYGTGLDNATVGILGMGAIG 157
Cdd:cd12175    76 LDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGR-WGRPEGRPSRELSGKTVGIVGLGNIG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 158 LAMAERLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCR 237
Cdd:cd12175   155 RAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTAR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 238 GSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLA 317
Cdd:cd12175   235 GGLVDEEALLAALRSGHLAGAGLDVFWQE-------PLPPDDPLLRLDNVILTPHIAGVTDESYQRMAAIVAENIARLLR 307

                  ....
gi 1393936758 318 GARP 321
Cdd:cd12175   308 GEPP 311
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
10-320 6.49e-70

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


Pssm-ID: 240645 [Multi-domain]  Cd Length: 321  Bit Score: 220.50  E-value: 6.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  10 RVHDEILQLLAPHCELVTnqtDSTLTREEILRRCR-----DAQAMM-----AFMPDRVDADFLQACPE-LRVVGCALKGF 78
Cdd:cd12168    11 IHAHDEWKELSSIAEVIY---PTSGTREEFIEALKegkygDFVAIYrtfgsAGETGPFDEELISPLPPsLKIIAHAGAGY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  79 DNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGL 158
Cdd:cd12168    88 DQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLDLTLAHDPRGKTLGILGLGGIGK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 159 AMAERLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRG 238
Cdd:cd12168   168 AIARKAAAFGMKIIYHNRSRLPEELEKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAKMKDGVIIVNTARG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 239 SVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRlIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd12168   248 AVIDEDALVDALESGKVASAGLDVFENE-------PE-VNPGLLKMPNVTLLPHMGTLTVETQEKMEELVLENIEAFLET 319

                  ..
gi 1393936758 319 AR 320
Cdd:cd12168   320 GK 321
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
3-323 9.83e-70

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: 219.69  E-value: 9.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   3 PKLVITHRVHDEI---LQLLAPH-CELVTNQTDSTltrEEILRRCRDAQAMMAFmPDRVDADFLQACPELRVVGCALKGF 78
Cdd:cd05299     1 PKVVITDYDFPDLdieREVLEEAgVELVDAQSRTE---DELIEAAADADALLVQ-YAPVTAEVIEALPRLKVIVRYGVGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  79 DNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGefqGWQPQFYG--TGLDNATVGILGMGAI 156
Cdd:cd05299    77 DNVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAG---GWDWTVGGpiRRLRGLTLGLVGFGRI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 157 GLAMAERLQGWGATLQYHEaKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPC 236
Cdd:cd05299   154 GRAVAKRAKAFGFRVIAYD-PYVPDGVAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 237 RGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVL 316
Cdd:cd05299   233 RGGLVDEAALARALKSGRIAGAALDVLEEE-------PPPADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVL 305

                  ....*..
gi 1393936758 317 AGARPIN 323
Cdd:cd05299   306 RGEPPRN 312
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
3-317 3.04e-62

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: 200.39  E-value: 3.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   3 PKLVITHRVHDEILQLLAPHCELVtnQTDSTLTREEILRRCR-DAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNF 81
Cdd:cd12156     1 PDVLQLGPLPPELLAELEARFTVH--RLWEAADPAALLAEHGgRIRAVVTNGETGLSAALIAALPALELIASFGVGYDGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfqgWQPQFY--GTGLDNATVGILGMGAIGLA 159
Cdd:cd12156    79 DLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAGR---WPKGAFplTRKVSGKRVGIVGLGRIGRA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 160 MAERLQGWGATLQYHEAKALDTQTEQRLG-LRqvacsELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRG 238
Cdd:cd12156   156 IARRLEAFGMEIAYHGRRPKPDVPYRYYAsLL-----ELAAESDVLVVACPGGPATRHLVNAEVLEALGPDGVLVNVARG 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936758 239 SVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRlIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLA 317
Cdd:cd12156   231 SVVDEAALIAALQEGRIAGAGLDVFENE-------PN-VPAALLDLDNVVLTPHIASATVETRRAMGDLVLANLEAFFA 301
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
37-300 1.12e-59

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


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 193.91  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  37 EEILRRCRDAQAMMAFMpDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLG 116
Cdd:cd12171    38 EELLEALKDADILITHF-APVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAET 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 117 RHLRAADAFVRSGEFQG--WQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEaKALDTQTEQRLGLRQVAC 194
Cdd:cd12171   117 RNIARAHAALKDGEWRKdyYNYDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYD-PYVDPEKIEADGVKKVSL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 195 SELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdWARADRP 274
Cdd:cd12171   196 EELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEE-PLPADHP 274
                         250       260
                  ....*....|....*....|....*.
gi 1393936758 275 rlidpaLLAHPNTLFTPHIGSAVRAV 300
Cdd:cd12171   275 ------LLKLDNVTLTPHIAGATRDV 294
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
109-294 1.37e-59

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: 189.24  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 109 IGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLG 188
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWA-SPDALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 189 LRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdw 268
Cdd:pfam02826  80 ARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPE-- 157
                         170       180
                  ....*....|....*....|....*.
gi 1393936758 269 aradrPRLIDPALLAHPNTLFTPHIG 294
Cdd:pfam02826 158 -----PLPADHPLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
4-316 4.56e-58

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: 189.67  E-value: 4.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLLAPHCELVTNQTDSTltREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDV 83
Cdd:cd05303     2 KILITDGIDEIAIEKLEEAGFEVDYEPLIA--KEELLEKIKDYDVLIVRSRTKVTKEVIDAAKNLKIIARAGVGLDNIDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  84 DACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFqgWQPQFYGTGLDNATVGILGMGAIGLAMAER 163
Cdd:cd05303    80 EYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKW--NKKKYKGIELRGKTLGIIGFGRIGREVAKI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 164 LQGWGATLQYHEAKALDTQTEqRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDE 243
Cdd:cd05303   158 ARALGMNVIAYDPYPKDEQAV-ELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDE 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936758 244 AAVLAALERGQLGGYAADVFEMEdwaradrPrLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVL 316
Cdd:cd05303   237 EALLEALKSGKLAGAALDVFENE-------P-PPGSKLLELPNVSLTPHIGASTKEAQERIGEELANKIIEFL 301
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
1-326 9.98e-58

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 189.19  E-value: 9.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   1 MLPKLVITHRVHDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAfMPDRVDADFLQACPELRVVGCALKGFDN 80
Cdd:PRK15409    1 MKPSVILYKALPDDLLQRLEEHFTVTQVANLSPETVEQHAAAFAEAEGLLG-SGEKVDAALLEKMPKLRAASTISVGYDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  81 FDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQG-WQPQFYGTGLDNATVGILGMGAIGLA 159
Cdd:PRK15409   80 FDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTAsIGPDWFGTDVHHKTLGIVGMGRIGMA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 160 MAERLQ-GWGATLQYHeAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRG 238
Cdd:PRK15409  160 LAQRAHfGFNMPILYN-ARRHHKEAEERFNARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 239 SVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:PRK15409  239 PVVDENALIAALQKGEIHAAGLDVFEQE-------PLSVDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQG 311

                  ....*...
gi 1393936758 319 ARPINAAN 326
Cdd:PRK15409  312 KVEKNCVN 319
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
12-312 5.51e-55

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


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 181.88  E-value: 5.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  12 HDEILQLLAPHCELVTnqTDSTlTREEILRRCRDAQAMMAfmpDRV--DADFLQACPELRVVGCALKGFDNFDVDACTAR 89
Cdd:cd12162    14 GDLSWDPLEFLGELTV--YDRT-SPEEVVERIKDADIVIT---NKVvlDAEVLAQLPNLKLIGVLATGYNNVDLAAAKER 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  90 GVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfqgWQ--PQF----YGTG-LDNATVGILGMGAIGLAMAE 162
Cdd:cd12162    88 GITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGE---WQksPDFcfwdYPIIeLAGKTLGIIGYGNIGQAVAR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 163 RLQGWGATLQYHEAKAldtqtEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVD 242
Cdd:cd12162   165 IARAFGMKVLFAERKG-----APPLREGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 243 EAAVLAALERGQLGGYAADVFEMEDwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNI 312
Cdd:cd12162   240 EQALADALNSGKIAGAGLDVLSQEP------PRADNPLLKAAPNLIITPHIAWASREARQRLMDILVDNI 303
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
31-326 1.20e-53

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 178.67  E-value: 1.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  31 DSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVP-TAELAI 109
Cdd:cd12177    33 PPDISGKALAEKLKGYDIIIASVTPNFDKEFFEYNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPGAVERDaVAEHAV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 110 GLAVGLGRHLRAADAFVRSGEfqgWQ--PQFYGTGLDNATVGILGMGAIGLAMAERL-QGWGA-TLQYHEAKAldTQTEQ 185
Cdd:cd12177   113 ALILTVLRKINQASEAVKEGK---WTerANFVGHELSGKTVGIIGYGNIGSRVAEILkEGFNAkVLAYDPYVS--EEVIK 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 186 RLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEM 265
Cdd:cd12177   188 KKGAKPVSLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEE 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936758 266 EDwARADRPrlidpaLLAHPNTLFTPHIGSAVR-AVRLEIERCAAqNIIQVLAGARPINAAN 326
Cdd:cd12177   268 EP-IKADHP------LLHYENVVITPHIGAYTYeSLYGMGEKVVD-DIEDFLAGKEPKGILN 321
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
14-323 5.57e-53

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: 177.08  E-value: 5.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  14 EILQLLAPHCELVTNQTDSTLTREEILRrcrDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWL 93
Cdd:cd12187    13 EYFQELLPGHKVVFTSQELLDDNVEEFK---DAEVISVFVYSRLDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  94 TFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgwQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQY 173
Cdd:cd12187    90 CNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFS--QAGLRGFELAGKTLGVVGTGRIGRRVARIARGFGMKVLA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 174 HEAKaLDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERG 253
Cdd:cd12187   168 YDVV-PDEELAERLGFRYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 254 QLGGYAADVFEMEDWARADRPRLIDP-------------ALLAHPNTLFTPHIG-SAVRAVRlEIERCAAQNIIQVLAGa 319
Cdd:cd12187   247 KLAGAGLDVLEQEEVLREEAELFREDvspedlkklladhALLRKPNVIITPHVAyNTKEALE-RILDTTVENIKAFAAG- 324

                  ....
gi 1393936758 320 RPIN 323
Cdd:cd12187   325 QPQN 328
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
30-318 3.43e-52

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: 174.80  E-value: 3.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  30 TDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAI 109
Cdd:cd01619    30 VTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPEYSPNAVAEHTI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 110 GLAVGLGRHLRAADafVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGAT-LQY--HEAKALdtqteQR 186
Cdd:cd01619   110 ALILALLRNRKYID--ERDKNQDLQDAGVIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKvIAYdpFRNPEL-----ED 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 187 LGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEME 266
Cdd:cd01619   183 KGVKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDVLEDE 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936758 267 ------DWARADRPRLIDPALLAHPNTLFTPHIGS-AVRAVRlEIERCAAQNIIQVLAG 318
Cdd:cd01619   263 tpdllkDLEGEIFKDALNALLGRRPNVIITPHTAFyTDDALK-NMVEISCENIVDFLEG 320
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
31-323 1.17e-51

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: 173.17  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  31 DSTLTREEILRRCRDAQA-MMAFMPDRvdADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAI 109
Cdd:cd12161    34 TKTTDTAELIERSKDADIvMIANMPLP--GEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 110 GLAVGLGRHLRAADAFVRSGEFQGwqpQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKalDTQTEQRLGL 189
Cdd:cd12161   112 GLAIDLLRNIVPCDAAVRAGGTKA---GLIGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRS--EKEEAKALGI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 190 RQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWA 269
Cdd:cd12161   187 EYVSLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPL 266
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936758 270 RADRPrlidpaLLAHPNTLFTPHIGSAVR---AVRLEIercAAQNIIQVLAGaRPIN 323
Cdd:cd12161   267 PADYP------LLHAPNTILTPHVAFATEeamEKRAEI---VFDNIEAWLAG-KPQN 313
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
30-318 1.00e-49

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: 168.07  E-value: 1.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  30 TDSTLTREEILRRCRDAQAMMAfMPDR--VDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTvPTAEL 107
Cdd:cd12169    31 NDHLLDEDALAERLAPFDAIVL-MRERtpFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCGTGGGPT-ATAEL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 108 AIGLAVGLGRHLRAADAFVRSGefqGWQPQFyGTGLDNATVGILGMGAIGLAMAE-------RLQGWGATLQYHEAKALD 180
Cdd:cd12169   109 TWALILALARNLPEEDAALRAG---GWQTTL-GTGLAGKTLGIVGLGRIGARVARigqafgmRVIAWSSNLTAERAAAAG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 181 TQteqrlglRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAA 260
Cdd:cd12169   185 VE-------AAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAAL 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936758 261 DVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:cd12169   258 DVFDVE-------PLPADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
12-309 3.92e-47

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 161.96  E-value: 3.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  12 HDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAF--MPdRVDADFLQACPELRVVGCALKGFDNFDVDACTAR 89
Cdd:cd12167    16 GPAALARLAALAEVLPPTPDADFAAEELRALLAGVEVLVTGwgTP-PLDAELLARAPRLRAVVHAAGSVRGLVTDAVWER 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  90 GVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGA 169
Cdd:cd12167    95 GILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWGWPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 170 TLQYHEaKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAA 249
Cdd:cd12167   175 RVLVYD-PYLPAAEAAALGVELVSLDELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAE 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 250 LERGQLGGyAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAvrlEIERCAA 309
Cdd:cd12167   254 LRSGRLRA-ALDVTDPE-------PLPPDSPLRTLPNVLLTPHIAGSTGD---ERRRLGD 302
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
66-301 5.01e-45

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


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 155.80  E-value: 5.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  66 PELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEF-----QGW--QPQF 138
Cdd:cd12174    49 PSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKWVTNGDGddiskGVEkgKKQF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 139 YGTGLDNATVGILGMGAIGLAMAERLQGWGAT-------LQYHEAKALDTQTEQRLGLrqvacSELFASSDFILLALPLN 211
Cdd:cd12174   129 VGTELRGKTLGVIGLGNIGRLVANAALALGMKvigydpyLSVEAAWKLSVEVQRVTSL-----EELLATADYITLHVPLT 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 212 ADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEmedwaradrprlidPALLAH-PNTLFT 290
Cdd:cd12174   204 DETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPE--------------PALLGHlPNVIAT 269
                         250       260
                  ....*....|....*....|
gi 1393936758 291 PHIG---------SAVRAVR 301
Cdd:cd12174   270 PHLGasteeaeenCAVMAAR 289
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
77-294 2.94e-44

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: 154.23  E-value: 2.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  77 GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAI 156
Cdd:cd12186    78 GVDMIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGDFR-WAPGLIGREIRDLTVGIIGTGRI 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 157 GLAMAERLQGWGATL----QYHEAKALDtqteqrLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALL 232
Cdd:cd12186   157 GSAAAKIFKGFGAKViaydPYPNPELEK------FLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAIL 230
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936758 233 VNPCRGSVVDEAAVLAALERGQLGGYAADVFEME------DWaradRPRLIDPA----LLAHPNTLFTPHIG 294
Cdd:cd12186   231 VNAARGGLVDTKALIDALDSGKIAGAALDTYENEtgyfnkDW----SGKEIEDEvlkeLIAMPNVLITPHIA 298
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
44-292 2.45e-41

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: 146.82  E-value: 2.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  44 RDAQAMMAFMPDRVDADFLQACPELRVVGCALK--GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRA 121
Cdd:cd12183    43 KGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRcaGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 122 ADAFVRSGEF--QGwqpqFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEqrLGLRQVACSELFA 199
Cdd:cd12183   123 AYNRVREGNFslDG----LLGFDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAK--LGVEYVDLDELLA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 200 SSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMED------------ 267
Cdd:cd12183   197 ESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAglffedhsdeii 276
                         250       260
                  ....*....|....*....|....*....
gi 1393936758 268 ----WARadrprlidpaLLAHPNTLFTPH 292
Cdd:cd12183   277 qddvLAR----------LLSFPNVLITGH 295
PLN02928 PLN02928
oxidoreductase family protein
35-294 1.30e-40

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 145.21  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  35 TREEILRRCRDAQAMMAFMpDRVDADFLQACPELRVV---GCALKGFDnfdVDACTARGVWLTFVPDLLT---VPTAELA 108
Cdd:PLN02928   51 AREDVPDVIANYDICVPKM-MRLDADIIARASQMKLImqfGVGLEGVD---VDAATKHGIKVARIPSEGTgnaASCAEMA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 109 IGLAVGLGRHLRAADAFVRS---GEfqgwqPqfYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEaKALDTQTEQ 185
Cdd:PLN02928  127 IYLMLGLLRKQNEMQISLKArrlGE-----P--IGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATR-RSWTSEPED 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 186 RLGLRQVACSEL------------FAS-SDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALER 252
Cdd:PLN02928  199 GLLIPNGDVDDLvdekgghediyeFAGeADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALES 278
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1393936758 253 GQLGGYAADVFEMEDWaradrprliDP--ALLAHPNTLFTPHIG 294
Cdd:PLN02928  279 GHLGGLAIDVAWSEPF---------DPddPILKHPNVIITPHVA 313
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
3-327 5.69e-39

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: 139.96  E-value: 5.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   3 PKLVITHRVHDEILQLLAPHCElvtNQTDSTLTREEILRRCRDAQAMMAFMPDRvdaDFLQACPELRVVGCALKGFDNFD 82
Cdd:cd05300     1 MKILVLSPLDDEHLERLRAAAP---GAELRVVTAEELTEELADADVLLGNPPLP---ELLPAAPRLRWIQSTSAGVDALL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  83 VDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfqgWQPQFYGTGLDNATVGILGMGAIGLAMAE 162
Cdd:cd05300    75 FPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAERR---WQRRGPVRELAGKTVLIVGLGDIGREIAR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 163 RLQGWGA-------TLQYHEAKALDTQTEQRLglrqvacSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNP 235
Cdd:cd05300   152 RAKAFGMrvigvrrSGRPAPPVVDEVYTPDEL-------DELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 236 CRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPrLidPA---LLAHPNTLFTPHIGSAVRAVRLEIERCAAQNI 312
Cdd:cd05300   225 GRGSVVDEDALIEALESGRIAGAALDVFEEE-------P-L--PAdspLWDLPNVIITPHISGDSPSYPERVVEIFLENL 294
                         330
                  ....*....|....*
gi 1393936758 313 IQVLAGARPINAANR 327
Cdd:cd05300   295 RRYLAGEPLLNVVDK 309
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
103-323 1.09e-37

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


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 136.60  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 103 PTAELAIGLAVGLGRHLRAADAFVRSGEFQGW-QPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQyheakALDT 181
Cdd:cd12165    94 AVAEHALALILALAKRIVEYDNDLRRGIWHGRaGEEPESKELRGKTVGILGYGHIGREIARLLKAFGMRVI-----GVSR 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 182 QTEQRLGLRQVACS----ELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGG 257
Cdd:cd12165   169 SPKEDEGADFVGTLsdldEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAG 248
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 258 YAADVFemedWARADRPRLIDPA---LLAHPNTLFTPHIGSAVR-AVRLEIERcAAQNIIQVLAGARPIN 323
Cdd:cd12165   249 AAIDVW----WRYPSRGDPVAPSrypFHELPNVIMSPHNAGWTEeTFRRRIDE-AAENIRRYLRGEPLLN 313
PLN02306 PLN02306
hydroxypyruvate reductase
77-336 1.45e-37

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 138.07  E-value: 1.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  77 GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQ-FYGTGLDNATVGILGMGA 155
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHlFVGNLLKGQTVGVIGAGR 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 156 IGLAMAERL-QGWGATLQYHE--------------AKALDTQTEQRLGLRQVAC-SELFASSDFILLALPLNADTQHLVN 219
Cdd:PLN02306  176 IGSAYARMMvEGFKMNLIYYDlyqstrlekfvtayGQFLKANGEQPVTWKRASSmEEVLREADVISLHPVLDKTTYHLIN 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 220 AELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWARadrprlidPALLAHPNTLFTPHIGSAVRA 299
Cdd:PLN02306  256 KERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPYMK--------PGLADMKNAVVVPHIASASKW 327
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1393936758 300 VRLEIERCAAQNIIQVLAGARPINAANRLP------KAEPAAC 336
Cdd:PLN02306  328 TREGMATLAALNVLGKLKGYPVWGDPNRVEpflnenAPPPAAS 370
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
4-294 3.76e-37

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


Pssm-ID: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 135.11  E-value: 3.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHDEILQLLapHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDV 83
Cdd:cd12179     1 KILIIDKNHPSLTELL--EALGFEVDYDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  84 DACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEfqgWQ-PQFYGTGLDNATVGILGMGAIGLAMAE 162
Cdd:cd12179    79 EYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGI---WDrEGNRGVELMGKTVGIIGYGNMGKAFAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 163 RLQGWGATLQYHEAKaldtQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVD 242
Cdd:cd12179   156 RLSGFGCKVIAYDKY----KNFGDAYAEQVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVV 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393936758 243 EAAVLAALERGQLGGYAADVFEMEDWAR---ADRPRLIDpALLAHPNTLFTPHIG 294
Cdd:cd12179   232 TKDLVKALKSGKILGACLDVLEYEKASFesiFNQPEAFE-YLIKSPKVILTPHIA 285
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
35-326 7.33e-37

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 134.83  E-value: 7.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  35 TREEILRRCRDAQAMMAfmpDRV--DADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLA 112
Cdd:PRK06487   35 TPEQVAERLRGAQVAIS---NKValDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 113 VGLGRHLRAADAFVRSGefqGWQ--PQF----YG-TGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKAldtqTEQ 185
Cdd:PRK06487  112 LALATRLPDYQQAVAAG---RWQqsSQFclldFPiVELEGKTLGLLGHGELGGAVARLAEAFGMRVLIGQLPG----RPA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 186 RLGlrQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEM 265
Cdd:PRK06487  185 RPD--RLPLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSV 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936758 266 EDwaradrPRLIDPaLLA--HPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGArPINAAN 326
Cdd:PRK06487  263 EP------PVNGNP-LLApdIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK-PLRVVS 317
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
52-323 1.37e-35

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 130.79  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  52 FMPDRVDADFLQACPELRVVGCALKGFDNF------DVDACTARGVWltfvpdllTVPTAELAIGLAVGlgrHLRAADAF 125
Cdd:cd12166    45 YMAAPPVLEALRALPRLRVVQTLSAGYDGVlpllpeGVTLCNARGVH--------DASTAELAVALILA---SLRGLPRF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 126 VRSGEFQGWQPQFYGTgLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDtqTEQRLGLRQVAcsELFASSDFIL 205
Cdd:cd12166   114 VRAQARGRWEPRRTPS-LADRRVLIVGYGSIGRAIERRLAPFEVRVTRVARTARP--GEQVHGIDELP--ALLPEADVVV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 206 LALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGyAADVFEMEdwaradrPRLIDPALLAHP 285
Cdd:cd12166   189 LIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLRA-ALDVTDPE-------PLPPGHPLWSAP 260
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1393936758 286 NTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPIN 323
Cdd:cd12166   261 GVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLEN 298
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
77-295 5.12e-34

(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: 127.41  E-value: 5.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  77 GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFqGWQPQFYGTGLDNATVGILGMGAI 156
Cdd:cd12184    78 GFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNF-KVDPFMFSKEIRNSTVGIIGTGRI 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 157 GLAMAERLQGWGATLQYHEAKALDTQTEQrlgLRQVACSELFASSDFILLALP-LNADTQHLVNAELLALVRPGALLVNP 235
Cdd:cd12184   157 GLTAAKLFKGLGAKVIGYDIYPSDAAKDV---VTFVSLDELLKKSDIISLHVPyIKGKNDKLINKEFISKMKDGAILINT 233
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936758 236 CRGSVVDEAAVLAALERGQLGGYAADVFEME--------DWARADRP---RLIDpallAHPNTLFTPHIGS 295
Cdd:cd12184   234 ARGELQDEEAILEALESGKLAGFGTDVLNNEkeiffkdfDGDKIEDPvveKLLD----LYPRVLLTPHIGS 300
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
37-318 8.65e-33

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 123.56  E-value: 8.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  37 EEILRRCRDAQAMMAfmpDRV--DADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVG 114
Cdd:PRK08410   34 EEVIERIKDANIIIT---NKVviDKEVLSQLPNLKLICITATGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 115 LGRHLRAADAFVRSGEFQGwQPQF------YGTgLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTE-QRL 187
Cdd:PRK08410  111 LLGRINYYDRYVKSGEYSE-SPIFthisrpLGE-IKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYYSTSGKNKNEEyERV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 188 GLRqvacsELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLgGYAADVFEMEd 267
Cdd:PRK08410  189 SLE-----ELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKE- 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1393936758 268 waradrPRLIDPALL---AHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAG 318
Cdd:PRK08410  262 ------PMEKNHPLLsikNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
43-327 2.91e-32

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: 122.22  E-value: 2.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  43 CRDAQAMMAFMPDrvdADFLQACPELRVVGCALKGFDNFDVDAcTARGVWLT-FVPDLLTVPTAELAIGLAVglgRHLRA 121
Cdd:cd12164    37 PADVDYALVWKPP---PGLLARLPNLKAIFSLGAGVDHLLADP-DLPDVPIVrLVDPGLAQGMAEYVLAAVL---RLHRD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 122 ADAFVRSGEFQGWQPQFYGTGLDnATVGILGMGAIGLAMAERLQGWGATLQ--------------YHEAKALDtqteqrl 187
Cdd:cd12164   110 MDRYAAQQRRGVWKPLPQRPAAE-RRVGVLGLGELGAAVARRLAALGFPVSgwsrspkdiegvtcFHGEEGLD------- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 188 glrqvacsELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEd 267
Cdd:cd12164   182 --------AFLAQTDILVCLLPLTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQE- 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 268 waradrPRLIDPALLAHPNTLFTPHIGSAVRAVrlEIERCAAQNIIQVLAGARPINAANR 327
Cdd:cd12164   253 ------PLPADHPLWRHPRVTVTPHIAAITDPD--SAAAQVAENIRRLEAGEPLPNLVDR 304
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
52-322 1.08e-31

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 122.47  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  52 FMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGef 131
Cdd:PRK07574   99 FWPAYLTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEG-- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 132 qGWQPQFYGTG---LDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLGLR-QVACSELFASSDFILLA 207
Cdd:PRK07574  177 -GWNIADCVSRsydLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHRLPEEVEQELGLTyHVSFDSLVSVCDVVTIH 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 208 LPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVfemedW----ARADRP-RLIdpall 282
Cdd:PRK07574  256 CPLHPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDV-----WfpqpAPADHPwRTM----- 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1393936758 283 ahPNTLFTPHI-GSAVRAVrleiERCAA--QNIIQVLAGARPI 322
Cdd:PRK07574  326 --PRNGMTPHIsGTTLSAQ----ARYAAgtREILECFFEGRPI 362
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
52-293 7.46e-31

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: 119.35  E-value: 7.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  52 FMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEF 131
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 132 QGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLGLRQVA-CSELFASSDFILLALPL 210
Cdd:cd05302   149 NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRLPEEVEKELGLTRHAdLEDMVSKCDVVTINCPL 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 211 NADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVfemedW----ARADRPrlidpaLLAHPN 286
Cdd:cd05302   229 HPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDV-----WfpqpAPKDHP------WRTMPN 297

                  ....*..
gi 1393936758 287 TLFTPHI 293
Cdd:cd05302   298 NAMTPHI 304
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
34-294 9.56e-31

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


Pssm-ID: 240653  Cd Length: 304  Bit Score: 118.06  E-value: 9.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  34 LTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAV 113
Cdd:cd12176    31 LDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEII 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 114 GLGRHLRAADAFVRSGEfqgWQPQfyGTG---LDNATVGILGMGAIG--LA-MAERLqgwGATLQYHeakalDTQTEQRL 187
Cdd:cd12176   111 MLARRLPDRNAAAHRGI---WNKS--ATGsheVRGKTLGIIGYGHIGsqLSvLAEAL---GMRVIFY-----DIAEKLPL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 188 G-LRQVAC-SELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEM 265
Cdd:cd12176   178 GnARQVSSlEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPE 257
                         250       260
                  ....*....|....*....|....*....
gi 1393936758 266 EDWARADRprlIDPALLAHPNTLFTPHIG 294
Cdd:cd12176   258 EPASNGEP---FSSPLQGLPNVILTPHIG 283
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
102-327 4.96e-30

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


Pssm-ID: 240657  Cd Length: 308  Bit Score: 116.29  E-value: 4.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 102 VPTAELAIGLAVGLGRHLraADAFVRSGEFqgWQPQFYGTgLDNATVGILGMGAIGLAMAERLQGWGATLQyheAKALDT 181
Cdd:cd12180    97 EAIAEFVLAAILAAAKRL--PEIWVKGAEQ--WRREPLGS-LAGSTLGIVGFGAIGQALARRALALGMRVL---ALRRSG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 182 QTEQRLGLRQVA-CSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAA 260
Cdd:cd12180   169 RPSDVPGVEAAAdLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASL 248
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936758 261 DVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPINAANR 327
Cdd:cd12180   249 DVTDPE-------PLPEGHPLYTHPRVRLSPHTSAIAPDGRRNLADRFLENLARYRAGQPLHDLVDP 308
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
37-312 8.94e-30

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 115.67  E-value: 8.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  37 EEILRRCRDAQAMMAfmpDRV--DADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVG 114
Cdd:PRK06932   36 EQTIERAKDADIVIT---SKVlfTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 115 LGRHLRA------ADAFVRSGEFQGWQPQFygTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLG 188
Cdd:PRK06932  113 LKHSLMGwyrdqlSDRWATCKQFCYFDYPI--TDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAEHKGASVCREGYTP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 189 LRQVacselFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDw 268
Cdd:PRK06932  191 FEEV-----LKQADIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEP- 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1393936758 269 aradrPRLIDPALLAH---PNTLFTPHIGSAV-RAVRLEIERcAAQNI 312
Cdd:PRK06932  265 -----PEKDNPLIQAAkrlPNLLITPHIAWASdSAVTTLVNK-VAQNI 306
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
77-293 2.48e-28

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 111.93  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  77 GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAI 156
Cdd:PRK12480   79 GFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFT-WQAEIMSKPVKNMTVAIIGTGRI 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 157 GLAMAERLQGWGATLQYHEA---KALDTQTEQRlglrqvACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLV 233
Cdd:PRK12480  158 GAATAKIYAGFGATITAYDAypnKDLDFLTYKD------SVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILV 231
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936758 234 NPCRGSVVDEAAVLAALERGQLGGYAADVFEME------DWA--RADRPRLIDpaLLAHPNTLFTPHI 293
Cdd:PRK12480  232 NAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayftnDWTnkDIDDKTLLE--LIEHERILVTPHI 297
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
56-294 5.83e-28

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 112.58  E-value: 5.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  56 RVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGefqGWQ 135
Cdd:PRK11790   64 QLTEEVLAAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRG---GWN 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 136 PQFYGT----GldnATVGILGMGAIGL---AMAERLqgwGATLQYHeakalDTQTEQRLG-LRQVAC-SELFASSDFILL 206
Cdd:PRK11790  141 KSAAGSfevrG---KTLGIVGYGHIGTqlsVLAESL---GMRVYFY-----DIEDKLPLGnARQVGSlEELLAQSDVVSL 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 207 ALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWARADrpRLIDPaLLAHPN 286
Cdd:PRK11790  210 HVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGD--PFESP-LRGLDN 286

                  ....*...
gi 1393936758 287 TLFTPHIG 294
Cdd:PRK11790  287 VILTPHIG 294
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
4-293 2.05e-27

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: 109.21  E-value: 2.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRVHD---EILQLLAPHCELVT-NQTDSTLTREeilrrcrDAQAMMAFMPDrVDADFLQACPELRVVGCALKGFD 79
Cdd:cd12155     1 KKLLTLDYGDekeEQIEDLGYDVDVVFeDELSDEEDLE-------DIEILYGYNPD-FDELDLAKMKNLKWIQLYSAGVD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  80 NFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAadaFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLA 159
Cdd:cd12155    73 YLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKK---AYKNQKEKKWKMDSSLLELYGKTILFLGTGSIGQE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 160 MAERLQGWGATLQY-----HEAKALDtQTeqrlgLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVN 234
Cdd:cd12155   150 IAKRLKAFGMKVIGvntsgRDVEYFD-KC-----YPLEELDEVLKEADIVVNVLPLTEETHHLFDEAFFEQMKKGALFIN 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936758 235 PCRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHI 293
Cdd:cd12155   224 VGRGPSVDEDALIEALKNKQIRGAALDVFEEE-------PLPKDSPLWDLDNVLITPHI 275
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
103-322 2.31e-27

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 108.89  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 103 PTAELAIGLAVGLGRHLRAadaFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQ 182
Cdd:cd12159    86 TVAEHALALLLAGLRQLPA---RARATTWDPAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNRSGRPVE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 183 TEQRLgLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADV 262
Cdd:cd12159   163 GADET-VPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDV 241
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 263 FEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPI 322
Cdd:cd12159   242 TDPE-------PLPDGHPLWSLPNALITPHVANTPEVIRPLLAERVAENVRAFAAGEPLL 294
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
77-293 5.69e-24

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 100.20  E-value: 5.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  77 GFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQgWQPQFYGTGLDNATVGILGMGAI 156
Cdd:PRK08605   79 GFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFR-WEPPILSRSIKDLKVAVIGTGRI 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 157 GLAMAERL-QGWGATL------QYHEAKALDTQTEqrlglrqvACSELFASSDFILLALPLNADTQHLVNAELLALVRPG 229
Cdd:PRK08605  158 GLAVAKIFaKGYGSDVvaydpfPNAKAATYVDYKD--------TIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKG 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936758 230 ALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaRADRPR------LIDP---ALLAHPNTLFTPHI 293
Cdd:PRK08605  230 AVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFE---RPLFPSdqrgqtINDPlleSLINREDVILTPHI 299
PLN03139 PLN03139
formate dehydrogenase; Provisional
52-293 3.39e-23

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 98.77  E-value: 3.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  52 FMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEF 131
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 132 QGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLGLRQVA-CSELFASSDFILLALPL 210
Cdd:PLN03139  186 NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPELEKETGAKFEEdLDAMLPKCDVVVINTPL 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 211 NADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDwARADRP-RLIdpallahPNTLF 289
Cdd:PLN03139  266 TEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQP-APKDHPwRYM-------PNHAM 337

                  ....
gi 1393936758 290 TPHI 293
Cdd:PLN03139  338 TPHI 341
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
56-293 6.49e-22

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: 94.52  E-value: 6.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  56 RVDADFLQACPeLRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGlavglgrhlraadAFVRSGEFQGWQ 135
Cdd:cd12158    47 KVNEALLEGSK-VKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLS-------------ALLVLAQRQGFS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 136 pqfygtgLDNATVGILGMGAIGLAMAERLQGWGA-TLQYHEAKALDTQTEQRLGLrqvacSELFASSDFILLALPLNAD- 213
Cdd:cd12158   113 -------LKGKTVGIVGVGNVGSRLARRLEALGMnVLLCDPPRAEAEGDPGFVSL-----EELLAEADIITLHVPLTRDg 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 214 ---TQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRlIDPALLAHPnTLFT 290
Cdd:cd12158   181 ehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENE-------PE-IDLELLDKV-DIAT 251

                  ...
gi 1393936758 291 PHI 293
Cdd:cd12158   252 PHI 254
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
103-292 2.43e-21

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 92.44  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 103 PTAELAIGLAVGLGRHLRAADAFVR----SGEFQGWQ---PQFYGTGLDNATVGILGMGAIGLAMAERLQGWGAtlqyhE 175
Cdd:cd12160    94 TVAEHTLALILAAVRRLDEMREAQRehrwAGELGGLQplrPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGA-----R 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 176 AKALDTQTEQRLGLRQVACS---ELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALER 252
Cdd:cd12160   169 VTGVARSAGERAGFPVVAEDelpELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALES 248
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1393936758 253 GQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPH 292
Cdd:cd12160   249 GRLGGAALDVTATE-------PLPASSPLWDAPNLILTPH 281
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
82-327 1.34e-18

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 85.02  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  82 DVDACTARGVWltfvpdllTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMA 161
Cdd:cd12163    78 EVPLCTASGIH--------GPQIAEWVIGTWLVLSHHFLQYIELQKEQTWGRRQEAYSVEDSVGKRVGILGYGSIGRQTA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 162 ERLQGWG-----ATLQYHEA--KALDTQ-------------------TEQRLGLRQVACSELfassDFILLALPLNADTQ 215
Cdd:cd12163   150 RLAQALGmevyaYTRSPRPTpeSRKDDGyivpgtgdpdgsipsawfsGTDKASLHEFLRQDL----DLLVVSLPLTPATK 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 216 HLVNAELLA-LVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIG 294
Cdd:cd12163   226 HLLGAEEFEiLAKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPE-------PLPADHPLWSAPNVIITPHVS 298
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1393936758 295 SAV-----RAVRLEIErcaaqNIIQVLAGARPINAANR 327
Cdd:cd12163   299 WQTqeyfdRALDVLEE-----NLERLRKGEPLINLVDR 331
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
4-291 9.76e-17

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


Pssm-ID: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 79.27  E-value: 9.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758   4 KLVITHRV--HDEILQLLAPHCELVTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVG--CALkgFD 79
Cdd:cd12170     3 KIVAIDPTglNEEAEEELKKYAEEVVFYDDIPESDEEIIERIGDADCVLVSYTTQIDEEVLEACPNIKYIGmcCSL--YS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  80 ----NFDVDACTARGVWLTFVPD-----LLTVPTAELaIGLAVGLGRHLraadafvrsgefqgWQPQfyGTGLDNATVGI 150
Cdd:cd12170    81 eesaNVDIAAARENGITVTGIRDygdegVVEYVISEL-IRLLHGFGGKQ--------------WKEE--PRELTGLKVGI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 151 LGMGAIGLAMAERLQGWGATLQYH--------EAKaldtqteqrlGLRQVACSELFASSDFILLALPLNAdtqHLVNAEL 222
Cdd:cd12170   144 IGLGTTGQMIADALSFFGADVYYYsrtrkpdaEAK----------GIRYLPLNELLKTVDVICTCLPKNV---ILLGEEE 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936758 223 LALVRPGALLVNPCRGSVVDEAAVLAALergQLGGYAadvFEMEDWARAdrprLIDPALLAHPNTLFTP 291
Cdd:cd12170   211 FELLGDGKILFNTSLGPSFEVEALKKWL---KASGYN---IFDCDTAGA----LGDEELLRYPNVICTN 269
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
68-264 2.54e-15

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: 75.34  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  68 LRVVGCALKGFDNFDV-DACTARGVWLTFVPDLLTVPTAELAIGLA-VGLGRHLRAADafVRSGEFQGWQPqfygtGLDN 145
Cdd:cd12154    88 DRLLFTYTIGADHRDLtEALARAGLTAIAVEGVELPLLTSNSIGAGeLSVQFIARFLE--VQQPGRLGGAP-----DVAG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 146 ATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLGLRQV-ACSELFASSDFILLALPLNADTQH-LVNAELL 223
Cdd:cd12154   161 KTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVeELEEALAEADVIVTTTLLPGKRAGiLVPEELV 240
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1393936758 224 ALVRPGALLVNPCRGSVVDEAAVLA-ALERGQLGGYAADVFE 264
Cdd:cd12154   241 EQMKPGSVIVNVAVGAVGCVQALHTqLLEEGHGVVHYGDVNM 282
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
38-293 2.84e-15

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 75.30  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  38 EILRRCRDAQAMMAFmPDRVDADfLQACPELRVVGCALK-------GFDNFDVDAcTARGVWLTFVPDLLTVPTAELAIG 110
Cdd:PRK06436   15 EICRDILDLDDVHWY-PDYYDAE-AILIKGRYVPGKKTKmiqslsaGVDHIDVSG-IPENVVLCSNAGAYSISVAEHAFA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 111 LAVGLGRHLRAADAFVRSGEFQgwqpQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLqyheakALDTQTEQRLGLR 190
Cdd:PRK06436   92 LLLAWAKNICENNYNMKNGNFK----QSPTKLLYNKSLGILGYGGIGRRVALLAKAFGMNI------YAYTRSYVNDGIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 191 QVACS--ELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDW 268
Cdd:PRK06436  162 SIYMEpeDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPI 241
                         250       260
                  ....*....|....*....|....*
gi 1393936758 269 ARADRPRlidpallahpNTLFTPHI 293
Cdd:PRK06436  242 ITETNPD----------NVILSPHV 256
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
147-327 5.30e-15

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 74.45  E-value: 5.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 147 TVGILGMGAIGLAMAERLQGWGATLQ-YHEAKALDTQTEQRLGLRQVacSELFASSDFILLALPLNADTQHLVNAELLAL 225
Cdd:PRK15469  138 TIGILGAGVLGSKVAQSLQTWGFPLRcWSRSRKSWPGVQSFAGREEL--SAFLSQTRVLINLLPNTPETVGIINQQLLEQ 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 226 VRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEdwaradrPRLIDPALLAHPNTLFTPHIGSAVRAVrlEIE 305
Cdd:PRK15469  216 LPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSRE-------PLPPESPLWQHPRVAITPHVAAVTRPA--EAV 286
                         170       180
                  ....*....|....*....|..
gi 1393936758 306 RCAAQNIIQVLAGARPINAANR 327
Cdd:PRK15469  287 EYISRTIAQLEKGERVCGQVDR 308
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
45-266 9.86e-15

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 74.17  E-value: 9.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  45 DAQAMMAFMPDRVDADFLQACPeLRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHlraaDA 124
Cdd:PRK15438   37 DADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER----DG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 125 FvrsgefqgwqpqfygtGLDNATVGILGMGAIGLAMAERLQGWGATLQYHEAKALDTQTEQRLGlrqvACSELFASSDFI 204
Cdd:PRK15438  112 F----------------SLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFR----SLDELVQEADIL 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936758 205 LLALPLNAD----TQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEME 266
Cdd:PRK15438  172 TFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE 237
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
44-293 1.68e-13

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 70.45  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758  44 RDAQAMMAFMPDRVDADFLQACPeLRVVGCALKGFDNFDVD-------------ACTARGVWLTFVPDLLTVptAELAig 110
Cdd:PRK00257   36 RDADVLLVRSVTRVDRALLEGSR-VRFVGTCTIGTDHLDLDyfaeagitwssapGCNARGVVDYVLGSLLTL--AERE-- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 111 lavglgrhlraadafvrsgefqgwqpqfyGTGLDNATVGILGMGAIGLAMAERLQGWGAtlqyhEAKALDTQTEQRLGLR 190
Cdd:PRK00257  111 -----------------------------GVDLAERTYGVVGAGHVGGRLVRVLRGLGW-----KVLVCDPPRQEAEGDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 191 Q-VACSELFASSDFILLALPLNAD----TQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEM 265
Cdd:PRK00257  157 DfVSLERILEECDVISLHTPLTKEgehpTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEG 236
                         250       260
                  ....*....|....*....|....*...
gi 1393936758 266 EdwaradrPRlIDPALLAHPnTLFTPHI 293
Cdd:PRK00257  237 E-------PQ-IDLELADLC-TIATPHI 255
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
102-233 7.32e-05

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


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 43.94  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 102 VPTAELAIGLAVGLG-RHLraadafvrsgEFQGWQPQFYGTGLDNATVGILGMGAIGLAMAERLQGWGATLQyheakALD 180
Cdd:cd01620   128 APNSNIAGYAGVQLGaYEL----------ARIQGGRMGGAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVL-----VYD 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936758 181 TQTEQRLGLRQVACSELFASSD------------FILLALPLNADTQHLVNAELLALVRPGALLV 233
Cdd:cd01620   193 IKEEKLKGVETLGGSRLRYSQKeelekelkqtdiLINAILVDGPRAPILIMEELVGPMKRGAVIV 257
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
147-233 1.28e-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: 38.99  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 147 TVGILGMGAIGLAMAERLQGWGATLQ---YHEAKALDTQTEQRLGLRQVAcsELFASSDFILLALPLNADTQHLVNAE-L 222
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTvynRTPEKVEELVAAGAIAAASPA--EFVAGLDVVITMVPAGAAVDAVIFGEgL 78
                          90
                  ....*....|.
gi 1393936758 223 LALVRPGALLV 233
Cdd:pfam03446  79 LPGLKPGDIII 89
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
146-234 1.31e-03

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 40.10  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936758 146 ATVGILGMGAIGLAMAERLQGWGatlqyHEAKALDTQTEQRLGLR----QVACS--ELFASSDFILLALPLNADTQHLVN 219
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAG-----HEVTVWNRTPAKAEALVaagaRVAASpaEAAAAADVVITMLPDDAAVEEVLL 76
                          90
                  ....*....|....*..
gi 1393936758 220 AE--LLALVRPGALLVN 234
Cdd:COG2084    77 GEdgLLAALRPGAVVVD 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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