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Conserved domains on  [gi|919184507|ref|NP_955871|]
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D-3-phosphoglycerate dehydrogenase [Danio rerio]

Protein Classification

hydroxyacid dehydrogenase( domain architecture ID 10187407)

hydroxyacid dehydrogenase such as Chromohalobacter salexigens (S)-sulfolactate dehydrogenase that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, and human 3-phosphoglycerate dehydrogenase that catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0070403|GO:0016491
PubMed:  30945211|30577795
SCOP:  3000044

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-310 4.27e-177

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: 500.41  E-value: 4.27e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173    1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173   81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173  161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919184507 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGK 310
Cdd:cd12173  241 ALKSGKIAGAALDVFEQEPPPaDSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
 
Name Accession Description Interval E-value
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-310 4.27e-177

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: 500.41  E-value: 4.27e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173    1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173   81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173  161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919184507 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGK 310
Cdd:cd12173  241 ALKSGKIAGAALDVFEQEPPPaDSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
8-499 6.67e-177

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 508.40  E-value: 6.67e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507    8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  168 GMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  247 RALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNAQVLASTFS 326
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPPTDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADVM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  327 PDSQQWIRLGESMGKVLKACSAstQPCSQLHVTSLGEALKKSTGFLSSAAVVGLLTEAPHNGPNLVNALPLAKETGITVH 406
Cdd:TIGR01327 321 EKLKPYLDLAEKLGKLAGQLLD--GAVQSVEVTYRGELATENSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGITVE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  407 TDHKASDEREACVMEVSVNGSR--YKAVGSVQAG-VPVLLELNGsvFRQPVPLTGHLLFFRANCSTEFLSSITGVLATAG 483
Cdd:TIGR01327 399 ESKSESSPDYKNYLSVTVTGDSgtVSVAGTVFGGfSPRIVEIDG--FHVDLEPEGIMLIILHLDKPGVIGKVGTLLGTAG 476
                         490
                  ....*....|....*.
gi 919184507  484 VELQSFSASSSSSGGE 499
Cdd:TIGR01327 477 INIASMQLGRKEKGGE 492
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
8-317 2.89e-133

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: 389.17  E-value: 2.89e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQEN-GIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:COG0111    2 KILILDDLPPEALEALEAApGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:COG0111   82 AATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVARRLRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 167 FGMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:COG0111  162 FGMRVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDAL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919184507 246 LRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:COG0111  242 LAALDSGRLAGAALDVFEPEPlPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPLRNLVN 314
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
9-317 6.88e-108

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: 324.24  E-value: 6.88e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507    9 VLISESVDPCCKSVLQENgiEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAA 88
Cdd:pfam00389   1 VLILDPLSPEALELLKEG--EVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   89 TKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFG 168
Cdd:pfam00389  79 TERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  169 MKTIGYDPITPPEVSASWGVEQMTLDQLW----PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAA 244
Cdd:pfam00389 159 MGVVAYDPYPNPERAEAGGVEVLSLLLLLldlpESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919184507  245 LLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:pfam00389 239 LDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
8-321 1.73e-68

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 223.52  E-value: 1.73e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQEN-GIEVTEKQQ-MTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDV 85
Cdd:PRK13243   4 KVFITREIPENGIEMLEEHfEVEVWEDEReIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNIDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  86 DAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK-------FMGSELYGKVLGIVGLGRIGK 158
Cdd:PRK13243  84 EEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFGRIGQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 159 EVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGG 238
Cdd:PRK13243 164 AVARRAKGFGMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 239 IIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNA 318
Cdd:PRK13243 244 VVDTKALVKALKEGWIAGAGLDVFEEEPYYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVNR 323

                 ...
gi 919184507 319 QVL 321
Cdd:PRK13243 324 EVV 326
 
Name Accession Description Interval E-value
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-310 4.27e-177

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: 500.41  E-value: 4.27e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173    1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173   81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173  161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919184507 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGK 310
Cdd:cd12173  241 ALKSGKIAGAALDVFEQEPPPaDSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
8-499 6.67e-177

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 508.40  E-value: 6.67e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507    8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  168 GMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  247 RALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNAQVLASTFS 326
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPPTDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADVM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  327 PDSQQWIRLGESMGKVLKACSAstQPCSQLHVTSLGEALKKSTGFLSSAAVVGLLTEAPHNGPNLVNALPLAKETGITVH 406
Cdd:TIGR01327 321 EKLKPYLDLAEKLGKLAGQLLD--GAVQSVEVTYRGELATENSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGITVE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  407 TDHKASDEREACVMEVSVNGSR--YKAVGSVQAG-VPVLLELNGsvFRQPVPLTGHLLFFRANCSTEFLSSITGVLATAG 483
Cdd:TIGR01327 399 ESKSESSPDYKNYLSVTVTGDSgtVSVAGTVFGGfSPRIVEIDG--FHVDLEPEGIMLIILHLDKPGVIGKVGTLLGTAG 476
                         490
                  ....*....|....*.
gi 919184507  484 VELQSFSASSSSSGGE 499
Cdd:TIGR01327 477 INIASMQLGRKEKGGE 492
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
8-305 9.84e-134

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: 389.97  E-value: 9.84e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd05303    2 KILITDGIDEIAIEKLEEAGFEVDYEPLIAKEELLEKIKDYDVLIVRSRTKVTKEVIDAAKNLKIIARAGVGLDNIDVEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd05303   82 AKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd05303  162 GMNVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLE 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919184507 248 ALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd05303  242 ALKSGKLAGAALDVFENEPPPGSKLLELPNVSLTPHIGASTKEAQERIGEELANKIIE 299
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
8-317 2.89e-133

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: 389.17  E-value: 2.89e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQEN-GIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:COG0111    2 KILILDDLPPEALEALEAApGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:COG0111   82 AATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVARRLRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 167 FGMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:COG0111  162 FGMRVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDAL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919184507 246 LRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:COG0111  242 LAALDSGRLAGAALDVFEPEPlPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
8-305 1.53e-114

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: 341.00  E-value: 1.53e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLIS----ESVDPCCKSVLQENGIEVTEK---QQMTKEELIAEIRNYDGLIVrSATKVTADVINAGSSLKIIGRAGTGV 80
Cdd:cd12172    1 KVLVTprsfSKYSEEAKELLEAAGFEVVLNplgRPLTEEELIELLKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  81 DNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRkkFMGSELYGKVLGIVGLGRIGKEV 160
Cdd:cd12172   80 DNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWDR--PVGTELYGKTLGIIGLGRIGKAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 161 ATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd12172  158 ARRLSGFGMKVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLV 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919184507 241 DEAALLRALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd12172  238 DEEALYEALKSGRIAGAALDVFEEEPPPaDSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVID 303
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
7-305 7.06e-114

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: 339.22  E-value: 7.06e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   7 KRVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:cd05198    1 KVLVLEPLFPPEALEALEATGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGK-WDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQ 165
Cdd:cd05198   81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWgWLWAGFPGYELEGKTVGIVGLGRIGQRVAKRLQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 166 SFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:cd05198  161 AFGMKVLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDAL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919184507 246 LRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd05198  241 LRALKSGKIAGAALDVFEPEPlPADHPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
9-317 6.88e-108

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: 324.24  E-value: 6.88e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507    9 VLISESVDPCCKSVLQENgiEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAA 88
Cdd:pfam00389   1 VLILDPLSPEALELLKEG--EVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   89 TKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFG 168
Cdd:pfam00389  79 TERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  169 MKTIGYDPITPPEVSASWGVEQMTLDQLW----PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAA 244
Cdd:pfam00389 159 MGVVAYDPYPNPERAEAGGVEVLSLLLLLldlpESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919184507  245 LLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:pfam00389 239 LDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAVN 311
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
9-318 8.95e-108

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: 324.35  E-value: 8.95e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   9 VLISESVDPCCKSVLQENGIEVTE-KQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:COG1052    5 VLDPRTLPDEVLERLEAEHFEVTVyEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDLAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFM-GSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:COG1052   85 AKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLlGRDLSGKTLGIIGLGRIGQAVARRAKG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 167 FGMKTIGYDPiTPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:COG1052  165 FGMKVLYYDR-SPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLVDEAALI 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919184507 247 RALESGQCGGAGLDVFVEEPPRE-RALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNA 318
Cdd:COG1052  244 EALKSGRIAGAGLDVFEEEPPPPdHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPPPNPVNP 316
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
8-317 6.55e-96

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: 293.31  E-value: 6.55e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKqqmtkeeliaEIRNYDGLIVRSaTKVtaDVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12174    2 KILTANKISKKGLERFKKDKYEVKED----------ALEDPDALIVRS-DKL--HDMDFAPSLKAIARAGAGVNNIDVDA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAV---------ISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGK 158
Cdd:cd12174   69 ASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIkwvtngdgdDISKGVEKGKKQFVGTELRGKTLGVIGLGNIGR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 159 EVATRMQSFGMKTIGYDPITPPEvsASWG----VEQMT-LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVN 233
Cdd:cd12174  149 LVANAALALGMKVIGYDPYLSVE--AAWKlsveVQRVTsLEELLATADYITLHVPLTDETRGLINAELLAKMKPGAILLN 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 234 CARGGIIDEAALLRALESGQCGGAGLDVfveepPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD-MATGKAl 312
Cdd:cd12174  227 FARGEIVDEEALLEALDEGKLGGYVTDF-----PEPALLGHLPNVIATPHLGASTEEAEENCAVMAARQIMDfLETGNI- 300

                 ....*
gi 919184507 313 VGAVN 317
Cdd:cd12174  301 TNSVN 305
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
39-312 7.58e-93

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: 285.62  E-value: 7.58e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  39 EELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLS 118
Cdd:cd12175   35 DEEAALLADADVLVPGMRKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 119 RHIPQAVISMKDGKWDRKKFMGS-ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDP-ITPPEVSASWGVEQMTLDQL 196
Cdd:cd12175  115 RRLPEADRELRAGRWGRPEGRPSrELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRfRDPEAEEKDLGVRYVELDEL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 197 WPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNH 275
Cdd:cd12175  195 LAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPlPPDDPLLRL 274
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 919184507 276 PNVISCPHLGASTKEAQARCGKDIALQIVDMATGKAL 312
Cdd:cd12175  275 DNVILTPHIAGVTDESYQRMAAIVAENIARLLRGEPP 311
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
8-312 1.37e-91

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: 282.48  E-value: 1.37e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCC---KSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSAtKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd05299    2 KVVITDYDFPDLdieREVLEEAGVELVDAQSRTEDELIEAAADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVDNVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  85 VDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMG-SELYGKVLGIVGLGRIGKEVATR 163
Cdd:cd05299   81 VAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTVGGPiRRLRGLTLGLVGFGRIGRAVAKR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 164 MQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEA 243
Cdd:cd05299  161 AKAFGFRVIAYDPYVPDGVAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGGLVDEA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 244 ALLRALESGQCGGAGLDVFVEEPP-RERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKAL 312
Cdd:cd05299  241 ALARALKSGRIAGAALDVLEEEPPpADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEPP 310
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
7-291 1.23e-89

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: 277.35  E-value: 1.23e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   7 KRVLISESVDPCCKSVLQEnGIEVT---EKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNV 83
Cdd:cd05301    1 PKVLVTRRLPEEALALLRE-GFEVEvwdEDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  84 DVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK---FMGSELYGKVLGIVGLGRIGKEV 160
Cdd:cd05301   80 DVDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSptlLLGTDLHGKTLGIVGMGRIGQAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 161 ATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd05301  160 ARRAKGFGMKILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVV 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919184507 241 DEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEA 291
Cdd:cd05301  240 DEDALVEALKSGKIAGAGLDVFEPEPlPADHPLLTLPNVVLLPHIGSATVET 291
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
37-317 5.34e-86

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: 268.34  E-value: 5.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  37 TKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:cd12178   33 SKEELLERIADYDALITPLSTPVDKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 117 LSRHIPQAVISMKDGK---WDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI-TPPEVSASWGVEQMT 192
Cdd:cd12178  113 LARRIAEGDRLMRRGGflgWAPLFFLGHELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 193 LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERAL 272
Cdd:cd12178  193 LDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEPEVSPEL 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 919184507 273 VNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:cd12178  273 KKLDNVILTPHIGNATVEARDAMAKEAADNIISFLEGKRPKNIVN 317
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
28-300 1.66e-85

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: 266.71  E-value: 1.66e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  28 IEVTEK----QQMTKEELIAEIRNYDGLIVRSATkVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNT 103
Cdd:cd12171   23 ILVVEKsgpeAVEPEEELLEALKDADILITHFAP-VTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 104 LSAAELTCALVMSLSRHIPQAVISMKDGKWDRK----KFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITP 179
Cdd:cd12171  102 EAVAEFTVGLMLAETRNIARAHAALKDGEWRKDyynyDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 180 PEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGL 259
Cdd:cd12171  182 PEKIEADGVKKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAAL 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 919184507 260 DVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIA 300
Cdd:cd12171  262 DVFPEEPlPADHPLLKLDNVTLTPHIAGATRDVAERSPEIIA 303
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
35-317 1.24e-80

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: 254.55  E-value: 1.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  35 QMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTP-SGNTLSAAELTCAL 113
Cdd:cd12177   35 DISGKALAEKLKGYDIIIASVTPNFDKEFFEYNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPgAVERDAVAEHAVAL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 114 VMSLSRHIPQAVISMKDGKW-DRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS-FGMKTIGYDPITPPEVSASWGVEQM 191
Cdd:cd12177  115 ILTVLRKINQASEAVKEGKWtERANFVGHELSGKTVGIIGYGNIGSRVAEILKEgFNAKVLAYDPYVSEEVIKKKGAKPV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 192 TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRE-R 270
Cdd:cd12177  195 SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKAdH 274
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 919184507 271 ALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:cd12177  275 PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDFLAGKEPKGILN 321
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
29-294 1.49e-78

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: 249.00  E-value: 1.49e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  29 EVTEKQQMTKEELIAEIRN--YDGL--IVRSATKV------TADVINA-GSSLKIIGRAGTGVDNVDVDAATKRGIIVMN 97
Cdd:cd12168   25 EVIYPTSGTREEFIEALKEgkYGDFvaIYRTFGSAgetgpfDEELISPlPPSLKIIAHAGAGYDQIDVDALTKRGIQVSN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  98 TPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGS--ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12168  105 TPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLDLTLahDPRGKTLGILGLGGIGKAIARKAAAFGMKIIYHN 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 176 PI-TPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQC 254
Cdd:cd12168  185 RSrLPEELEKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKV 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 919184507 255 GGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12168  265 ASAGLDVFENEPEVNPGLLKMPNVTLLPHMGTLTVETQEK 304
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-300 5.84e-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: 240653  Cd Length: 304  Bit Score: 247.11  E-value: 5.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEV-TEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:cd12176    2 KILLLENIHPSADELFRAGGIEVeRLKGALDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:cd12176   82 AAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 167 FGMKTIGYDPITPPEVSASWGVEqmTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:cd12176  162 LGMRVIFYDIAEKLPLGNARQVS--SLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALA 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919184507 247 RALESGQCGGAGLDVFVEEP-----PRERALVNHPNVISCPHLGASTKEAQARCGKDIA 300
Cdd:cd12176  240 EALRSGHLAGAAVDVFPEEPasngePFSSPLQGLPNVILTPHIGGSTEEAQENIGLEVA 298
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
29-294 8.59e-74

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: 236.19  E-value: 8.59e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  29 EVTEKQQMTKEELIAEIRNYDGLIVrSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAE 108
Cdd:cd12162   26 ELTVYDRTSPEEVVERIKDADIVIT-NKVVLDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 109 LTCALVMSLSRHIPQAVISMKDGKWDRKK---FMG---SELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEV 182
Cdd:cd12162  105 HTFALLLALARLVAYHNDVVKAGEWQKSPdfcFWDypiIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 183 saswGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVF 262
Cdd:cd12162  185 ----REGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVL 260
                        250       260       270
                 ....*....|....*....|....*....|....
gi 919184507 263 VEEPPRE--RALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12162  261 SQEPPRAdnPLLKAAPNLIITPHIAWASREARQR 294
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
112-285 8.85e-72

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: 226.61  E-value: 8.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  112 ALVMSLSRHIPQAVISMKDGKWD-RKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSAS-WGVE 189
Cdd:pfam02826   2 ALLLALARRIPEADRQVRAGRWAsPDALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEeLGAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  190 QMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PR 268
Cdd:pfam02826  82 YVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPlPA 161
                         170
                  ....*....|....*..
gi 919184507  269 ERALVNHPNVISCPHLG 285
Cdd:pfam02826 162 DHPLLDLPNVILTPHIA 178
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
26-310 1.69e-71

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: 231.04  E-value: 1.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  26 NGIEVTEKQqMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLS 105
Cdd:cd01619   25 VDVEIVTYL-LNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPEYSPNA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 106 AAELTCALVMSLSRHipQAVISMKDGKWDR--KKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVs 183
Cdd:cd01619  104 VAEHTIALILALLRN--RKYIDERDKNQDLqdAGVIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNPEL- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 184 ASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFV 263
Cdd:cd01619  181 EDKGVKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDVLE 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919184507 264 EE--------------PPRERALVNHPNVISCPHLGASTKEAQARCgKDIALQ-IVDMATGK 310
Cdd:cd01619  261 DEtpdllkdlegeifkDALNALLGRRPNVIITPHTAFYTDDALKNM-VEISCEnIVDFLEGE 321
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
8-305 1.81e-69

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: 225.25  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12179    1 KILIIDKNHPSLTELLEALGFEVDYDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12179   81 AKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGIIGYGNMGKAFAKRLSGF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 168 GMKTIGYDPItppEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12179  161 GCKVIAYDKY---KNFGDAYAEQVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVK 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919184507 248 ALESGQCGGAGLDVFVEE----------PPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd12179  238 ALKSGKILGACLDVLEYEkasfesifnqPEAFEYLIKSPKVILTPHIAGWTFESYEKIAEVLVDKIKA 305
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
38-291 3.34e-69

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: 224.31  E-value: 3.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  38 KEELIAEIRNYDGLIV-RSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTlSAAELTCALVMS 116
Cdd:cd12169   37 EDALAERLAPFDAIVLmRERTPFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCGTGGGPT-ATAELTWALILA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 117 LSRHIPQAVISMKDGKWDRKkfMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQM-TLDQ 195
Cdd:cd12169  116 LARNLPEEDAALRAGGWQTT--LGTGLAGKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLTAERAAAAGVEAAvSKEE 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 196 LWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVN 274
Cdd:cd12169  194 LFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEPlPADHPLRG 273
                        250
                 ....*....|....*..
gi 919184507 275 HPNVISCPHLGASTKEA 291
Cdd:cd12169  274 LPNVLLTPHIGYVTEEA 290
PRK13243 PRK13243
glyoxylate reductase; Reviewed
8-321 1.73e-68

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 223.52  E-value: 1.73e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   8 RVLISESVDPCCKSVLQEN-GIEVTEKQQ-MTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDV 85
Cdd:PRK13243   4 KVFITREIPENGIEMLEEHfEVEVWEDEReIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNIDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  86 DAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK-------FMGSELYGKVLGIVGLGRIGK 158
Cdd:PRK13243  84 EEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFGRIGQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 159 EVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGG 238
Cdd:PRK13243 164 AVARRAKGFGMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 239 IIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNA 318
Cdd:PRK13243 244 VVDTKALVKALKEGWIAGAGLDVFEEEPYYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVNR 323

                 ...
gi 919184507 319 QVL 321
Cdd:PRK13243 324 EVV 326
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
7-309 3.64e-68

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: 222.16  E-value: 3.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   7 KRVLISESVDPCCKSVLQENGiEVTEKQQ---MTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNV 83
Cdd:cd12157    2 PKVVITHKVHPEVLELLKPHC-EVISNQTdepLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  84 DVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWD--RKKFMGSELYGKVLGIVGLGRIGKEVA 161
Cdd:cd12157   81 DVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGgwRPKFYGTGLDGKTVGILGMGALGRAIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 162 TRMQSFGMKTIGYDPIT-PPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd12157  161 RRLSGFGATLLYYDPHPlDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVV 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919184507 241 DEAALLRALESGQCGGAGLDVF----VEEPPRERA-----LVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATG 309
Cdd:cd12157  241 DEAAVAEALKSGHLGGYAADVFemedWARPDRPRSipqelLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
14-294 4.82e-67

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: 219.45  E-value: 4.82e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  14 SVDPCCKSVLQE--NGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKR 91
Cdd:cd12187    6 ETEEWEQEYFQEllPGHKVVFTSQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKLPRLKLIATRSTGFDHIDLEACRER 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  92 GIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKT 171
Cdd:cd12187   86 GIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRRVARIARGFGMKV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 172 IGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALES 251
Cdd:cd12187  166 LAYDVVPDEELAERLGFRYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKE 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919184507 252 GQCGGAGLDVFVEEP------PRER---------------ALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12187  246 GKLAGAGLDVLEQEEvlreeaELFRedvspedlkklladhALLRKPNVIITPHVAYNTKEALER 309
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
1-291 6.90e-66

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: 215.93  E-value: 6.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   1 MAPISVKRVLISESVDPccksvLQENGIEVTEKQQMTK--EELIAEIRNYDGLIVrSATKVTADVINAGSSLKIIGRAGT 78
Cdd:cd12161    5 LEPLGVSEEKIEELAAP-----LEEQGHEFVYYDTKTTdtAELIERSKDADIVMI-ANMPLPGEVIEACKNLKMISVAFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  79 GVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKwDRKKFMGSELYGKVLGIVGLGRIGK 158
Cdd:cd12161   79 GVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGG-TKAGLIGRELAGKTVGIVGTGAIGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 159 EVATRMQSFGMKTIGYDPiTPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGG 238
Cdd:cd12161  158 RVARLFKAFGCKVLAYSR-SEKEEAKALGIEYVSLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGP 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 919184507 239 IIDEAALLRALESGQCGGAGLDVFVEEPP--RERALVNHPNVISCPHLGASTKEA 291
Cdd:cd12161  237 VVDNEALADALNEGKIAGAGIDVFDMEPPlpADYPLLHAPNTILTPHVAFATEEA 291
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
1-317 7.98e-65

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 216.20  E-value: 7.98e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   1 MAPISVK----RVLISESVDPCCKSVLQENG---IEvTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKII 73
Cdd:PRK11790   1 MAKVSLPkdkiKFLLLEGVHQSAVEVLRAAGytnIE-YHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAEKLVAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  74 GRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDrKKFMGS-ELYGKVLGIVG 152
Cdd:PRK11790  80 GCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWN-KSAAGSfEVRGKTLGIVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 153 LGRIGKEVATRMQSFGMKTIGYDPITP-PEVSAswgvEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVK 230
Cdd:PRK11790 159 YGHIGTQLSVLAESLGMRVYFYDIEDKlPLGNA----RQVgSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 231 VVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-----PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:PRK11790 235 LINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPksngdPFESPLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVK 314
                        330
                 ....*....|..
gi 919184507 306 MATGKALVGAVN 317
Cdd:PRK11790 315 YSDNGSTLSAVN 326
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
24-291 5.83e-64

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: 211.63  E-value: 5.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  24 QENGIEVTekqqMTKEEL----IAEIRNYDGLIVRSATKVTADVIN--AGSSLKIIGRAGTGVDNVDVDAATKRGIIVMN 97
Cdd:cd12186   21 KEHPVEVD----TTTELLtpetVDLAKGYDGVVVQQTLPYDEEVYEklAEYGIKQIALRSAGVDMIDLDLAKENGLKITN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  98 TPSGNTLSAAELTCALVMSLSRHIPQAVISMKDG--KWDrKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12186   97 VPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGdfRWA-PGLIGREIRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 176 PITPPEVsASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCG 255
Cdd:cd12186  176 PYPNPEL-EKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIA 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 919184507 256 GAGLDVF--------------VEEPPRERALVNHPNVISCPHLGASTKEA 291
Cdd:cd12186  255 GAALDTYenetgyfnkdwsgkEIEDEVLKELIAMPNVLITPHIAFYTDTA 304
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
37-322 1.10e-62

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 208.18  E-value: 1.10e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  37 TKEELIAEIRNYDGLIV-RSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVM 115
Cdd:cd12167   39 AAEELRALLAGVEVLVTgWGTPPLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAIL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 116 SLSRHIPQAVISMKDGKWD--RKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTL 193
Cdd:cd12167  119 LALRRIPRFAAAYRAGRDWgwPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVSL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 194 DQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQcGGAGLDVFVEEP-PRERAL 272
Cdd:cd12167  199 DELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGR-LRAALDVTDPEPlPPDSPL 277
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 919184507 273 VNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNAQVLA 322
Cdd:cd12167  278 RTLPNVLLTPHIAGSTGDERRRLGDYALDELERFLAGEPLLHEVTPERLA 327
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
58-291 5.20e-59

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: 198.44  E-value: 5.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  58 KVTADVINAGSSL--KIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDR 135
Cdd:cd12183   55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 136 KKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVsASWGVEQMTLDQLWPQCDYITVHTPLMASTTG 215
Cdd:cd12183  135 DGLLGFDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPEL-AKLGVEYVDLDELLAESDIISLHCPLTPETHH 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 216 LLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPR---------------ERaLVNHPNVIS 280
Cdd:cd12183  214 LINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLffedhsdeiiqddvlAR-LLSFPNVLI 292
                        250
                 ....*....|.
gi 919184507 281 CPHLGASTKEA 291
Cdd:cd12183  293 TGHQAFFTKEA 303
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
39-291 2.80e-58

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: 195.77  E-value: 2.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  39 EELIAEIRnydGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLS 118
Cdd:cd12156   37 AEHGGRIR---AVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 119 RHIPQAVISMKDGKWDRKKF-MGSELYGKVLGIVGLGRIGKEVATRMQSFGMkTIGY-DPITPPEVsaSWGVEQmTLDQL 196
Cdd:cd12156  114 RRIPAADRFVRAGRWPKGAFpLTRKVSGKRVGIVGLGRIGRAIARRLEAFGM-EIAYhGRRPKPDV--PYRYYA-SLLEL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 197 WPQCDYITVHTPLMASTTGLLNdASFAKC--KKGVkVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVN 274
Cdd:cd12156  190 AAESDVLVVACPGGPATRHLVN-AEVLEAlgPDGV-LVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEPNVPAALLD 267
                        250
                 ....*....|....*..
gi 919184507 275 HPNVISCPHLGASTKEA 291
Cdd:cd12156  268 LDNVVLTPHIASATVET 284
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
19-312 1.23e-56

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: 191.69  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  19 CKSVLQENGIEVTEKQQMTKEELIAEIRnydglIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKrGIIVMNT 98
Cdd:cd12165   15 FEAALEGLYAEVPELPDEAAEEALEDAD-----VLVGGRLTKEEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  99 pSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDR---KKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12165   89 -HGNSPAVAEHALALILALAKRIVEYDNDLRRGIWHGragEEPESKELRGKTVGILGYGHIGREIARLLKAFGMRVIGVS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 176 --PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQ 253
Cdd:cd12165  168 rsPKEDEGADFVGTLSD--LDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERP 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919184507 254 CGGAGLDVFVEEPPRERA-------LVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKAL 312
Cdd:cd12165  246 IAGAAIDVWWRYPSRGDPvapsrypFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPL 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
24-291 7.65e-56

Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, NAD-binding and catalytic domains; This group contains various putative dehydrogenases related to D-lactate dehydrogenase (LDH), (R)-2-hydroxyglutarate dehydrogenase (HGDH), and related enzymes, members of the 2-hydroxyacid dehydrogenases family. LDH catalyzes the interconversion of pyruvate and lactate, and HGDH catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Despite often low sequence identity within this 2-hydroxyacid dehydrogenase family, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240661  Cd Length: 322  Bit Score: 189.73  E-value: 7.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  24 QENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSL--KIIGRAGTGVDNVDVDAATKRGIIVMNTP-S 100
Cdd:cd12185   21 KEYNVEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAgvKYISTRSIGYDHIDLDAAKELGIKVSNVTyS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 101 GNtlSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPP 180
Cdd:cd12185  101 PN--SVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 181 EVSAswGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLD 260
Cdd:cd12185  179 EVKK--YAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALD 256
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 919184507 261 VFVEE-------------PPRERALVN-HPNVISCPHLGASTKEA 291
Cdd:cd12185  257 VIEGEdgiyyndrkgdilSNRELAILRsFPNVILTPHMAFYTDQA 301
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
7-317 1.38e-53

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: 183.49  E-value: 1.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507   7 KRVLISESVDPCCKSVLQEN--GIEVTEKqqmTKEELIAEIRNYDGLIvrsATKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd05300    1 MKILVLSPLDDEHLERLRAAapGAELRVV---TAEELTEELADADVLL---GNPPLPELLPAAPRLRWIQSTSAGVDALL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  85 VDAATKRGIIVMNTpSG-NTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGsELYGKVLGIVGLGRIGKEVATR 163
Cdd:cd05300   75 FPELLERDVVLTNA-RGiFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQRRGPVR-ELAGKTVLIVGLGDIGREIARR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 164 MQSFGMKTIGYD---PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd05300  153 AKAFGMRVIGVRrsgRPAPPVVDEVYTPDE--LDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVV 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919184507 241 DEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVN 317
Cdd:cd05300  231 DEDALIEALESGRIAGAALDVFEEEPlPADSPLWDLPNVIITPHISGDSPSYPERVVEIFLENLRRYLAGEPLLNVVD 308
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
37-294 2.12e-52

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 180.67  E-value: 2.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  37 TKEELIAEIRnydGLIVRSATKV--TADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALV 114
Cdd:PRK06487  35 TPEQVAERLR---GAQVAISNKValDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 115 MSLSRHIPQAVISMKDGKWDRKK------FMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKT-IGYDPITPPevsaswG 187
Cdd:PRK06487 112 LALATRLPDYQQAVAAGRWQQSSqfclldFPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVlIGQLPGRPA------R 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 188 VEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPP 267
Cdd:PRK06487 186 PDRLPLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVEPP 265
                        250       260       270
                 ....*....|....*....|....*....|
gi 919184507 268 RE-RALV--NHPNVISCPHLGASTKEAQAR 294
Cdd:PRK06487 266 VNgNPLLapDIPRLIVTPHSAWGSREARQR 295
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
21-310 6.36e-52

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 179.02  E-value: 6.36e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  21 SVLQENGiEVTEKQQMTKEELIAEIRNYDgLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPS 100
Cdd:PRK08410  17 SVFEEFG-DFQIYPTTSPEEVIERIKDAN-IIITNKVVIDKEVLSQLPNLKLICITATGTNNVDIEYAKKKGIAVKNVAG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 101 GNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKF------MGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGY 174
Cdd:PRK08410  95 YSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSESPIfthisrPLGEIKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 175 dpiTPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQC 254
Cdd:PRK08410 175 ---STSGKNKNEEYERVSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDI 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 255 gGAGLDVFVEEP-PRERALV---NHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGK 310
Cdd:PRK08410 252 -YAGLDVLEKEPmEKNHPLLsikNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEGG 310
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
43-275 4.83e-48

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: 169.63  E-value: 4.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  43 AEIRNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRhip 122
Cdd:cd12158   32 EDLKDADVLLVRSVTKVNEALL-EGSKVKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQ--- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 123 qavismkdgkwdRKKFmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI-TPPEVSASWgveqMTLDQLWPQCD 201
Cdd:cd12158  108 ------------RQGF---SLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPrAEAEGDPGF----VSLEELLAEAD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919184507 202 YITVHTPLMAS----TTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNH 275
Cdd:cd12158  169 IITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEIDLELLDK 246
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
59-294 5.40e-48

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: 169.81  E-value: 5.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  59 VTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWD---- 134
Cdd:cd05302   74 MTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNvadv 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 135 -RKKFmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPIT-PPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMA 211
Cdd:cd05302  154 vKRAY---DLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRlPEEVEKELGLTRHaDLEDMVSKCDVVTINCPLHP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 212 STTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKE 290
Cdd:cd05302  231 ETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPaPKDHPWRTMPNNAMTPHISGTTLD 310

                 ....
gi 919184507 291 AQAR 294
Cdd:cd05302  311 AQAR 314
PLN02928 PLN02928
oxidoreductase family protein
18-303 4.92e-46

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 164.47  E-value: 4.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  18 CCKSVLQENG-IEVTEkqqMTKEELIAEIRNYDGLIVRSaTKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVM 96
Cdd:PLN02928  34 YTREYLQKYPfIQVDA---VAREDVPDVIANYDICVPKM-MRLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  97 NTPS---GNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKkfMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIG 173
Cdd:PLN02928 110 RIPSegtGNAASCAEMAIYLMLGLLRKQNEMQISLKARRLGEP--IGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 174 ydpitppeVSASWGVEQMTLDQLW---------------------PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVV 232
Cdd:PLN02928 188 --------TRRSWTSEPEDGLLIPngdvddlvdekgghediyefaGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLV 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919184507 233 NCARGGIIDEAALLRALESGQCGGAGLDVFVEEP--PrERALVNHPNVISCPHLGASTKEAQARCGK---DIALQI 303
Cdd:PLN02928 260 NIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPfdP-DDPILKHPNVIITPHVAGVTEYSYRSMGKivgDAALQL 334
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
37-321 2.77e-45

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 161.84  E-value: 2.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  37 TKEELIAEIRNYDGLIvRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:PRK15409  35 TVEQHAAAFAEAEGLL-GSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 117 LSRHIPQAVISMKDGKWDRK---KFMGSELYGKVLGIVGLGRIGKEVATRMQ-SFGMKTIGYDPITPPEVSASWGVEQMT 192
Cdd:PRK15409 114 TARRVVEVAERVKAGEWTASigpDWFGTDVHHKTLGIVGMGRIGMALAQRAHfGFNMPILYNARRHHKEAEERFNARYCD 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 193 LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERA 271
Cdd:PRK15409 194 LDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPlSVDSP 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 919184507 272 LVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNAQVL 321
Cdd:PRK15409 274 LLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEKNCVNPQVA 323
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
23-294 7.29e-44

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 159.84  E-value: 7.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  23 LQENGIE--VTEKQQMTKEELIAEIRNYDglIVRSA----TKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVM 96
Cdd:PRK07574  64 LEERGHElvVTSDKDGPDSDFEKELPDAD--VVISQpfwpAYLTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  97 NTPSGNTLSAAELTCALVMSLSR-HIPQAVISMKdGKWDRKKFMGS--ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIG 173
Cdd:PRK07574 142 EVTGSNSISVAEHVVMMILALVRnYEPSHRQAVE-GGWNIADCVSRsyDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHY 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 174 YDPI-TPPEVSASWGVE-QMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALES 251
Cdd:PRK07574 221 TDRHrLPEEVEQELGLTyHVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALES 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 919184507 252 GQCGGAGLDV-FVEEPPRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:PRK07574 301 GHLAGYAGDVwFPQPAPADHPWRTMPRNGMTPHISGTTLSAQAR 344
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
63-294 1.29e-41

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: 151.58  E-value: 1.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  63 VINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMgSE 142
Cdd:cd12155   54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMDSSL-LE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 143 LYGKVLGIVGLGRIGKEVATRMQSFGMKTIGydpitppeVSASwG--VEQM----TLDQL---WPQCDYITVHTPLMAST 213
Cdd:cd12155  133 LYGKTILFLGTGSIGQEIAKRLKAFGMKVIG--------VNTS-GrdVEYFdkcyPLEELdevLKEADIVVNVLPLTEET 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 214 TGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQ 292
Cdd:cd12155  204 HHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPlPKDSPLWDLDNVLITPHISGVSEHFN 283

                 ..
gi 919184507 293 AR 294
Cdd:cd12155  284 ER 285
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
27-291 2.75e-41

(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: 151.29  E-value: 2.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  27 GIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVinagssLKIIGRAG--------TGVDNVDVDAATKRGIIVMNT 98
Cdd:cd12184   24 GYDLTLVEEYLNDENVHLAKGHDAVIVRGNCFADKEN------LEIYKEYGikyvftrtVGFNHIDLEAAKELGFKMARV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  99 PSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGS-ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI 177
Cdd:cd12184   98 PSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNFKVDPFMFSkEIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIY 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 178 tpPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTG-LLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGG 256
Cdd:cd12184  178 --PSDAAKDVVTFVSLDELLKKSDIISLHVPYIKGKNDkLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAG 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 919184507 257 AGLDVFVEEP--------------PRERALVN-HPNVISCPHLGASTKEA 291
Cdd:cd12184  256 FGTDVLNNEKeiffkdfdgdkiedPVVEKLLDlYPRVLLTPHIGSYTDEA 305
PLN03139 PLN03139
formate dehydrogenase; Provisional
30-294 1.84e-39

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 147.69  E-value: 1.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  30 VTEKQQMTKEELIAEIRNYDGLIVRS--ATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAA 107
Cdd:PLN03139  80 VTDDKEGPDCELEKHIPDLHVLITTPfhPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVA 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 108 ELTCALVMSLSRHIPQAVISMKDGKWDRKK--FMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPIT-PPEVSA 184
Cdd:PLN03139 160 EDELMRILILLRNFLPGYHQVVSGEWNVAGiaYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKmDPELEK 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 185 SWGVEQMT-LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFV 263
Cdd:PLN03139 240 ETGAKFEEdLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWY 319
                        250       260       270
                 ....*....|....*....|....*....|..
gi 919184507 264 EEP-PRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:PLN03139 320 PQPaPKDHPWRYMPNHAMTPHISGTTIDAQLR 351
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
29-284 3.40e-38

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 142.25  E-value: 3.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  29 EVTEKQQMTKEELIAEIRNYDgLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAE 108
Cdd:PRK06932  26 EWIEYDHTSAEQTIERAKDAD-IVITSKVLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 109 LTCALVMSLSRHIPQAVISMKDGKW-DRKKFMG-----SELYGKVLGIVGLGRIGKEVATRMQSFGMKTI---------- 172
Cdd:PRK06932 105 HVLGMIFALKHSLMGWYRDQLSDRWaTCKQFCYfdypiTDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLyaehkgasvc 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 173 --GYDPitppevsaswgveqmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALE 250
Cdd:PRK06932 185 reGYTP----------------FEEVLKQADIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALE 248
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 919184507 251 SGQCGGAGLDVFVEEPPRE-----RALVNHPNVISCPHL 284
Cdd:PRK06932 249 NGKIAGAALDVLVKEPPEKdnpliQAAKRLPNLLITPHI 287
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
70-319 3.75e-38

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: 141.86  E-value: 3.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  70 LKIIGRAGTGVDNVDVDAATKRGIIV-MNTPsGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYgKVl 148
Cdd:cd12164   59 LKAIFSLGAGVDHLLADPDLPDVPIVrLVDP-GLAQGMAEYVLAAVLRLHRDMDRYAAQQRRGVWKPLPQRPAAER-RV- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 149 GIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCK 226
Cdd:cd12164  136 GVLGLGELGAAVARRLAALGFPVSGWSrsPKDIEGVTCFHGEEG--LDAFLAQTDILVCLLPLTPETRGILNAELLARLP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 227 KGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQArcGKDIALQIVD 305
Cdd:cd12164  214 RGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPlPADHPLWRHPRVTVTPHIAAITDPDSA--AAQVAENIRR 291
                        250
                 ....*....|....
gi 919184507 306 MATGKALVGAVNAQ 319
Cdd:cd12164  292 LEAGEPLPNLVDRA 305
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
24-291 9.89e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 136.03  E-value: 9.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  24 QENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKI--IGRAGTGVDNVDVDAATKRGIIVMNTPSG 101
Cdd:PRK08605  22 EKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIkqIAQRSAGFDTYDLELATKYNLIISNVPSY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 102 NTLSAAELTCALVMSLSRHIP--QAVISMKDGKWdrkkfmGSELYGKVLG-----IVGLGRIGKEVATRM-QSFGMKTIG 173
Cdd:PRK08605 102 SPESIAEFTVTQAINLVRHFNqiQTKVREHDFRW------EPPILSRSIKdlkvaVIGTGRIGLAVAKIFaKGYGSDVVA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 174 YDPItPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQ 253
Cdd:PRK08605 176 YDPF-PNAKAATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGL 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919184507 254 CGGAGLDVFVEEPP------RERA--------LVNHPNVISCPHLGASTKEA 291
Cdd:PRK08605 255 IKGAALDTYEFERPlfpsdqRGQTindpllesLINREDVILTPHIAFYTDAA 306
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
107-318 2.04e-33

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: 129.00  E-value: 2.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 107 AELTCALVMSLSRHIPQAVISmKDGKWDRKKfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGY-DPITPPEVSas 185
Cdd:cd12180  100 AEFVLAAILAAAKRLPEIWVK-GAEQWRREP--LGSLAGSTLGIVGFGAIGQALARRALALGMRVLALrRSGRPSDVP-- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 186 wGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVE 264
Cdd:cd12180  175 -GVEAAaDLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDP 253
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 919184507 265 EP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNA 318
Cdd:cd12180  254 EPlPEGHPLYTHPRVRLSPHTSAIAPDGRRNLADRFLENLARYRAGQPLHDLVDP 308
PLN02306 PLN02306
hydroxypyruvate reductase
79-289 7.61e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.51  E-value: 7.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  79 GVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGK---WDRKKFMGSELYGKVLGIVGLGR 155
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLyegWLPHLFVGNLLKGQTVGVIGAGR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 156 IGKEVATRM-QSFGMKTIGYDPI-----------------TPPEVSASWGvEQMTLDQLWPQCDYITVHTPLMASTTGLL 217
Cdd:PLN02306 176 IGSAYARMMvEGFKMNLIYYDLYqstrlekfvtaygqflkANGEQPVTWK-RASSMEEVLREADVISLHPVLDKTTYHLI 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919184507 218 NDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTK 289
Cdd:PLN02306 255 NKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPYMKPGLADMKNAVVVPHIASASK 326
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
78-316 7.07e-31

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: 121.54  E-value: 7.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  78 TGVDNVDvdAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKkFMGSeLYGKVLGIVGLGRIG 157
Cdd:cd12166   69 AGYDGVL--PLLPEGVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPR-RTPS-LADRRVLIVGYGSIG 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 158 KEVATRMQSFGMKT--IGYDPITPPEVSaswGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCA 235
Cdd:cd12166  145 RAIERRLAPFEVRVtrVARTARPGEQVH---GIDE--LPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVA 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 236 RGGIIDEAALLRALESGQCgGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVG 314
Cdd:cd12166  220 RGPVVDTDALVAELASGRL-RAALDVTDPEPlPPGHPLWSAPGVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLEN 298

                 ..
gi 919184507 315 AV 316
Cdd:cd12166  299 VV 300
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
43-294 2.09e-30

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 122.07  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  43 AEIRNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAE--LTCALVMSLSRh 120
Cdd:PRK00257  33 AAVRDADVLLVRSVTRVDRALL-EGSRVRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDyvLGSLLTLAERE- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 121 ipqavismkdgkwdrkkfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPitpPEVSASWGVEQMTLDQLWPQC 200
Cdd:PRK00257 111 -------------------GVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDP---PRQEAEGDGDFVSLERILEEC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 201 DYITVHTPLM----ASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHP 276
Cdd:PRK00257 169 DVISLHTPLTkegeHPTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQIDLELADLC 248
                        250
                 ....*....|....*...
gi 919184507 277 nVISCPHLGASTKEAQAR 294
Cdd:PRK00257 249 -TIATPHIAGYSLDGKAR 265
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
68-317 3.58e-30

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: 120.46  E-value: 3.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  68 SSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSG-NTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFM--GSELY 144
Cdd:cd12163   53 PNLRLVQLFSAGADHWLGHPLYKDPEVPLCTASGiHGPQIAEWVIGTWLVLSHHFLQYIELQKEQTWGRRQEAysVEDSV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 145 GKVLGIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPE------------------VSASW--GVEQMTLDQ-LWPQCD 201
Cdd:cd12163  133 GKRVGILGYGSIGRQTARLAQALGMEVYAYTrsPRPTPEsrkddgyivpgtgdpdgsIPSAWfsGTDKASLHEfLRQDLD 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 202 YITVHTPLMASTTGLLNDASFAKC-KKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVI 279
Cdd:cd12163  213 LLVVSLPLTPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPlPADHPLWSAPNVI 292
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 919184507 280 SCPHLGASTKEAQarcgkDIALQIVD-----MATGKALVGAVN 317
Cdd:cd12163  293 ITPHVSWQTQEYF-----DRALDVLEenlerLRKGEPLINLVD 330
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
42-294 3.89e-30

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 121.55  E-value: 3.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  42 IAEIRNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELT-CALVMSLSRH 120
Cdd:PRK15438  32 VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVfSSLLMLAERD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 121 ipqavismkdgkwdrkkfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPitpPEVSASWGVEQMTLDQLWPQC 200
Cdd:PRK15438 111 -------------------GFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDP---PRADRGDEGDFRSLDELVQEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 201 DYITVHTPLMAS----TTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHP 276
Cdd:PRK15438 169 DILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLKKV 248
                        250
                 ....*....|....*...
gi 919184507 277 NvISCPHLGASTKEAQAR 294
Cdd:PRK15438 249 D-IGTPHIAGYTLEGKAR 265
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
107-318 1.48e-29

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: 118.14  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 107 AELTCALVMSLSRHIPQAVISmkdGKWDRKKFM--GSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSA 184
Cdd:cd12159   88 AEHALALLLAGLRQLPARARA---TTWDPAEEDdlVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNRSGRPVEGA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 185 SWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVE 264
Cdd:cd12159  165 DETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDP 244
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 919184507 265 EP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMATGKALVGAVNA 318
Cdd:cd12159  245 EPlPDGHPLWSLPNALITPHVANTPEVIRPLLAERVAENVRAFAAGEPLLGVVDP 299
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
24-291 2.61e-29

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 118.09  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  24 QENGIEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINA--GSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSG 101
Cdd:PRK12480  22 KKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKleSYGIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 102 NTLSAAELTCALVMSLSRHIPQ--AVISMKDGKWdRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPItp 179
Cdd:PRK12480 102 SPETIAEYSVSIALQLVRRFPDieRRVQAHDFTW-QAEIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAY-- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 180 PEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGL 259
Cdd:PRK12480 179 PNKDLDFLTYKDSVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAI 258
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 919184507 260 DVFVEEPP--------RE------RALVNHPNVISCPHLGASTKEA 291
Cdd:PRK12480 259 DTYENEAAyftndwtnKDiddktlLELIEHERILVTPHIAFFSDEA 304
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
38-283 5.95e-22

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: 96.29  E-value: 5.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  38 KEELIAEIRNYDGLIV-RSATKVTADVINAGSSLKIIGRAGTGVDNV-------DVDAATKRGIivmntpsgNTLSAAEL 109
Cdd:cd12160   27 AAPVPAEHHDAEVLVVwGNSSDNLADAARRLTRLRWVQALAAGPDAVlaagfapEVAVTSGRGL--------HDGTVAEH 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 110 TCALVMSLSRHIPQAVISMKDGKWDR----------KKFMGSELYGKVLgIVGLGRIGKEVATRMQSFGMKTIGydpitp 179
Cdd:cd12160   99 TLALILAAVRRLDEMREAQREHRWAGelgglqplrpAGRLTTLLGARVL-IWGFGSIGQRLAPLLTALGARVTG------ 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 180 peVSASWG-------VEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESG 252
Cdd:cd12160  172 --VARSAGeragfpvVAEDELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESG 249
                        250       260       270
                 ....*....|....*....|....*....|..
gi 919184507 253 QCGGAGLDVFVEEP-PRERALVNHPNVISCPH 283
Cdd:cd12160  250 RLGGAALDVTATEPlPASSPLWDAPNLILTPH 281
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
67-286 1.35e-20

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 92.25  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  67 GSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTpSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFmgSELYGK 146
Cdd:PRK06436  47 GKKTKMIQSLSAGVDHIDVSGIPENVVLCSNA-GAYSISVAEHAFALLLAWAKNICENNYNMKNGNFKQSPT--KLLYNK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 147 VLGIVGLGRIGKEVATRMQSFGMKTIGYdpiTPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCK 226
Cdd:PRK06436 124 SLGILGYGGIGRRVALLAKAFGMNIYAY---TRSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFR 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 227 KGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPprERALVNHPNVISCPHLGA 286
Cdd:PRK06436 201 KGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEP--IITETNPDNVILSPHVAG 258
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
28-297 1.51e-19

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


Pssm-ID: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 88.90  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  28 IEVTEKQQMTKEELIAEIRNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVD----NVDVDAATKRGIIVMNTPSGNT 103
Cdd:cd12170   27 VVFYDDIPESDEEIIERIGDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 104 LSAAE-LTCALVMSLS-------RHIPQavismkdgkwdrkkfmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12170  107 EGVVEyVISELIRLLHgfggkqwKEEPR------------------ELTGLKVGIIGLGTTGQMIADALSFFGADVYYYS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 176 PITPPEVSASwGVEQMTLDQLWPQCDYITVHTPlmaSTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQ-- 253
Cdd:cd12170  169 RTRKPDAEAK-GIRYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKASGyn 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 919184507 254 ---CGGAGldVFVEEpprerALVNHPNVISCPHLGASTKEAQARCGK 297
Cdd:cd12170  245 ifdCDTAG--ALGDE-----ELLRYPNVICTNKSAGWTRQAFERLSQ 284
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
57-266 8.66e-17

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: 81.12  E-value: 8.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507  57 TKVTADVInAGSSLKIIGRAGTGVDNVDV-DAATKRGIIVMNTP-------SGNTLSAAELtcaLVMSLSRHIPQAVISM 128
Cdd:cd12154   76 TNAEYALI-QKLGDRLLFTYTIGADHRDLtEALARAGLTAIAVEgvelpllTSNSIGAGEL---SVQFIARFLEVQQPGR 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 129 KDGKWDrkkfmgseLYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPEVSASWGVEQMTLDQLWPQCDYITVH 206
Cdd:cd12154  152 LGGAPD--------VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDinVEALEQLEELGGKNVEELEEALAEADVIVTT 223
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919184507 207 TPLMASTTGLLNDAS-FAKCKKGVKVVNCARG-GIIDEAALLRALESGQCGGAGLDVFVEEP 266
Cdd:cd12154  224 TLLPGKRAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGP 285
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
148-319 1.56e-16

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 80.61  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 148 LGIVGLGRIGKEVATRMQSFG--MKTIGYDPITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKC 225
Cdd:PRK15469 139 IGILGAGVLGSKVAQSLQTWGfpLRCWSRSRKSWPGVQSFAGREE--LSAFLSQTRVLINLLPNTPETVGIINQQLLEQL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919184507 226 KKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARcgKDIALQIV 304
Cdd:PRK15469 217 PDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPlPPESPLWQHPRVAITPHVAAVTRPAEAV--EYISRTIA 294
                        170
                 ....*....|....*
gi 919184507 305 DMATGKALVGAVNAQ 319
Cdd:PRK15469 295 QLEKGERVCGQVDRA 309
 
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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