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Conserved domains on  [gi|33990002|gb|AAH56334|]
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Zgc:65956 [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 2.10e-176

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: 498.48  E-value: 2.10e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173   1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173 161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33990002 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGK 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 2.10e-176

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: 498.48  E-value: 2.10e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173   1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173 161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33990002 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGK 310
Cdd:cd12173 241 ALKSGKIAGAALDVFEQEPPPaDSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
8-487 3.56e-176

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: 506.48  E-value: 3.56e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002     8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002    88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   168 GMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   247 RALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNAQVLASTFS 326
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPPTDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADVM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   327 PDSQQWIRLGESMGKVLKACSAstQPCSQLHVTSLGEALKKSTGFLSSAAVVGLLTEAPHNGPNLVNALPLAKETGITVH 406
Cdd:TIGR01327 321 EKLKPYLDLAEKLGKLAGQLLD--GAVQSVEVTYRGELATENSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGITVE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   407 TDHKASDEREACVMEVSVNG--SSYKAVGSVQAG-VPVLLELNGsvFRQPVPLTGHLLFFRANCSTEFLSSITGVLATAG 483
Cdd:TIGR01327 399 ESKSESSPDYKNYLSVTVTGdsGTVSVAGTVFGGfSPRIVEIDG--FHVDLEPEGIMLIILHLDKPGVIGKVGTLLGTAG 476

                  ....
gi 33990002   484 VELQ 487
Cdd:TIGR01327 477 INIA 480
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
8-317 1.20e-131

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: 384.93  E-value: 1.20e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQEN-GIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:COG0111   2 KILILDDLPPEALEALEAApGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:COG0111  82 AATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVARRLRA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 167 FGMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:COG0111 162 FGMRVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDAL 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33990002 246 LRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:COG0111 242 LAALDSGRLAGAALDVFEPEPlPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPLRNLVN 314
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
9-317 1.29e-107

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: 323.47  E-value: 1.29e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002     9 VLISESVDPCCKTVLQENGIVVteKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAA 88
Cdd:pfam00389   1 VLILDPLSPEALELLKEGEVEV--HDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002    89 TKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFG 168
Cdd:pfam00389  79 TERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   169 MKTIGYDPITPPEVSASWGVEQMTLDQLW----PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAA 244
Cdd:pfam00389 159 MGVVAYDPYPNPERAEAGGVEVLSLLLLLldlpESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33990002   245 LLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:pfam00389 239 LDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
25-321 1.65e-66

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 218.12  E-value: 1.65e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   25 ENGI----------VVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGII 94
Cdd:PRK13243  13 ENGIemleehfeveVWEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   95 VMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK-------FMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:PRK13243  93 VTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFGRIGQAVARRAKGF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:PRK13243 173 GMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVK 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33990002  248 ALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNAQVL 321
Cdd:PRK13243 253 ALKEGWIAGAGLDVFEEEPYYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVNREVV 326
 
Name Accession Description Interval E-value
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-310 2.10e-176

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: 498.48  E-value: 2.10e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12173   1 KVLVTDPIDEEGLELLREAGIEVDVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12173 161 GMKVLAYDPYISAERAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALAD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33990002 248 ALESGQCGGAGLDVFVEEPPR-ERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGK 310
Cdd:cd12173 241 ALKSGKIAGAALDVFEQEPPPaDSPLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLAVLAGE 304
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
8-487 3.56e-176

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: 506.48  E-value: 3.56e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002     8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDVQTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002    88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:TIGR01327  81 ATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   168 GMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:TIGR01327 161 GMKVLAYDPYISPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   247 RALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNAQVLASTFS 326
Cdd:TIGR01327 241 EALEEGHVRAAALDVFEKEPPTDNPLFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPVPNAVNAPGIDADVM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   327 PDSQQWIRLGESMGKVLKACSAstQPCSQLHVTSLGEALKKSTGFLSSAAVVGLLTEAPHNGPNLVNALPLAKETGITVH 406
Cdd:TIGR01327 321 EKLKPYLDLAEKLGKLAGQLLD--GAVQSVEVTYRGELATENSEPLTRAALKGLLSPVLDDEVNMVNAPAVAKERGITVE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   407 TDHKASDEREACVMEVSVNG--SSYKAVGSVQAG-VPVLLELNGsvFRQPVPLTGHLLFFRANCSTEFLSSITGVLATAG 483
Cdd:TIGR01327 399 ESKSESSPDYKNYLSVTVTGdsGTVSVAGTVFGGfSPRIVEIDG--FHVDLEPEGIMLIILHLDKPGVIGKVGTLLGTAG 476

                  ....
gi 33990002   484 VELQ 487
Cdd:TIGR01327 477 INIA 480
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
8-305 1.57e-132

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: 386.89  E-value: 1.57e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd05303   2 KILITDGIDEIAIEKLEEAGFEVDYEPLIAKEELLEKIKDYDVLIVRSRTKVTKEVIDAAKNLKIIARAGVGLDNIDVEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd05303  82 AKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARAL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd05303 162 GMNVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLE 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33990002 248 ALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd05303 242 ALKSGKLAGAALDVFENEPPPGSKLLELPNVSLTPHIGASTKEAQERIGEELANKIIE 299
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
8-317 1.20e-131

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: 384.93  E-value: 1.20e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQEN-GIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:COG0111   2 KILILDDLPPEALEALEAApGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:COG0111  82 AATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVARRLRA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 167 FGMKTIGYDPITPPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:COG0111 162 FGMRVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDAL 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33990002 246 LRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:COG0111 242 LAALDSGRLAGAALDVFEPEPlPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
8-305 4.80e-113

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: 337.15  E-value: 4.80e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLIS----ESVDPCCKTVLQENGIVVTEK---QQMTKEELIAEIQNYDGLIVrSATKVTADVINAGSSLKIIGRAGTGV 80
Cdd:cd12172   1 KVLVTprsfSKYSEEAKELLEAAGFEVVLNplgRPLTEEELIELLKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  81 DNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRkkFMGSELYGKVLGIVGLGRIGKEV 160
Cdd:cd12172  80 DNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWDR--PVGTELYGKTLGIIGLGRIGKAV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 161 ATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd12172 158 ARRLSGFGMKVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLV 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33990002 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 5.00e-112

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: 334.60  E-value: 5.00e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   7 KRVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:cd05198   1 KVLVLEPLFPPEALEALEATGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGK-WDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQ 165
Cdd:cd05198  81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWgWLWAGFPGYELEGKTVGIVGLGRIGQRVAKRLQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 166 SFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAAL 245
Cdd:cd05198 161 AFGMKVLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDAL 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33990002 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 1.29e-107

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: 323.47  E-value: 1.29e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002     9 VLISESVDPCCKTVLQENGIVVteKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAA 88
Cdd:pfam00389   1 VLILDPLSPEALELLKEGEVEV--HDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002    89 TKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFG 168
Cdd:pfam00389  79 TERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   169 MKTIGYDPITPPEVSASWGVEQMTLDQLW----PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAA 244
Cdd:pfam00389 159 MGVVAYDPYPNPERAEAGGVEVLSLLLLLldlpESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEAA 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33990002   245 LLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:pfam00389 239 LDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAVN 311
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
29-318 7.89e-107

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: 321.65  E-value: 7.89e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  29 VVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAE 108
Cdd:COG1052  26 VTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDLAAAKERGITVTNTPGYLTEAVAE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 109 LTCALVMSLSRHIPQAVISMKDGKWDRKKFM-GSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPiTPPEVSASWG 187
Cdd:COG1052 106 HAVALLLALARRIVEADRRVRAGDWSWSPGLlGRDLSGKTLGIIGLGRIGQAVARRAKGFGMKVLYYDR-SPKPEVAELG 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 188 VEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPP 267
Cdd:COG1052 185 AEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPP 264
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 33990002 268 RE-RALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNA 318
Cdd:COG1052 265 PPdHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPPPNPVNP 316
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
47-317 9.85e-95

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: 290.23  E-value: 9.85e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  47 NYDGLIVRSaTKVtaDVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAV- 125
Cdd:cd12174  31 DPDALIVRS-DKL--HDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIk 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 126 --------ISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEvsASWG----VEQMT- 192
Cdd:cd12174 108 wvtngdgdDISKGVEKGKKQFVGTELRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVE--AAWKlsveVQRVTs 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 193 LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVfveepPRERAL 272
Cdd:cd12174 186 LEELLATADYITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDF-----PEPALL 260
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 33990002 273 VNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:cd12174 261 GHLPNVIATPHLGASTEEAEENCAVMAARQIMDFLETGNITNSVN 305
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
39-312 2.66e-92

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: 284.47  E-value: 2.66e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  39 EELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLS 118
Cdd:cd12175  35 DEEAALLADADVLVPGMRKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 119 RHIPQAVISMKDGKWDRKKFMGS-ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDP-ITPPEVSASWGVEQMTLDQL 196
Cdd:cd12175 115 RRLPEADRELRAGRWGRPEGRPSrELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRfRDPEAEEKDLGVRYVELDEL 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 197 WPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNH 275
Cdd:cd12175 195 LAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPlPPDDPLLRL 274
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 33990002 276 PNVISCPHLGASTKEAQARCGKDIALQIVDMASGKAL 312
Cdd:cd12175 275 DNVILTPHIAGVTDESYQRMAAIVAENIARLLRGEPP 311
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
7-309 6.20e-90

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: 278.12  E-value: 6.20e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   7 KRVLISESVDPCCKTVLQENGIVV--TEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd05301   1 PKVLVTRRLPEEALALLREGFEVEvwDEDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  85 VDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK---FMGSELYGKVLGIVGLGRIGKEVA 161
Cdd:cd05301  81 VDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSptlLLGTDLHGKTLGIVGMGRIGQAVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 162 TRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIID 241
Cdd:cd05301 161 RRAKGFGMKILYHNRSRKPEAEEELGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVD 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33990002 242 EAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASG 309
Cdd:cd05301 241 EDALVEALKSGKIAGAGLDVFEPEPlPADHPLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
8-312 1.11e-89

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: 277.47  E-value: 1.11e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKT---VLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSAtKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd05299   2 KVVITDYDFPDLDIereVLEEAGVELVDAQSRTEDELIEAAADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVDNVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  85 VDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMG-SELYGKVLGIVGLGRIGKEVATR 163
Cdd:cd05299  81 VAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTVGGPiRRLRGLTLGLVGFGRIGRAVAKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 164 MQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEA 243
Cdd:cd05299 161 AKAFGFRVIAYDPYVPDGVAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGGLVDEA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 244 ALLRALESGQCGGAGLDVFVEEPP-RERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKAL 312
Cdd:cd05299 241 ALARALKSGRIAGAALDVLEEEPPpADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEPP 310
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
37-317 1.11e-85

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: 267.56  E-value: 1.11e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  37 TKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:cd12178  33 SKEELLERIADYDALITPLSTPVDKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 117 LSRHIPQAVISMKDGK---WDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI-TPPEVSASWGVEQMT 192
Cdd:cd12178 113 LARRIAEGDRLMRRGGflgWAPLFFLGHELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 193 LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERAL 272
Cdd:cd12178 193 LDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEPEVSPEL 272
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 33990002 273 VNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:cd12178 273 KKLDNVILTPHIGNATVEARDAMAKEAADNIISFLEGKRPKNIVN 317
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
39-300 3.69e-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: 265.94  E-value: 3.69e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  39 EELIAEIQNYDGLIVRSATkVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLS 118
Cdd:cd12171  38 EELLEALKDADILITHFAP-VTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAET 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 119 RHIPQAVISMKDGKWDRK----KFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLD 194
Cdd:cd12171 117 RNIARAHAALKDGEWRKDyynyDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGVKKVSLE 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 195 QLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALV 273
Cdd:cd12171 197 ELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPlPADHPLL 276
                       250       260
                ....*....|....*....|....*..
gi 33990002 274 NHPNVISCPHLGASTKEAQARCGKDIA 300
Cdd:cd12171 277 KLDNVTLTPHIAGATRDVAERSPEIIA 303
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
23-317 6.09e-82

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: 258.02  E-value: 6.09e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  23 LQENGIVVTEK--QQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTP- 99
Cdd:cd12177  21 LKKIGYVDRFEvpPDISGKALAEKLKGYDIIIASVTPNFDKEFFEYNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPg 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 100 SGNTLSAAELTCALVMSLSRHIPQAVISMKDGKW-DRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS-FGMKTIGYDPI 177
Cdd:cd12177 101 AVERDAVAEHAVALILTVLRKINQASEAVKEGKWtERANFVGHELSGKTVGIIGYGNIGSRVAEILKEgFNAKVLAYDPY 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 178 TPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGA 257
Cdd:cd12177 181 VSEEVIKKKGAKPVSLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGA 260
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33990002 258 GLDVFVEEPPRE-RALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:cd12177 261 GLDVLEEEPIKAdHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDFLAGKEPKGILN 321
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
37-294 1.84e-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: 1.84e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  37 TKEELIAEIQN--YDGL--IVRSATKV------TADVINA-GSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLS 105
Cdd:cd12168  33 TREEFIEALKEgkYGDFvaIYRTFGSAgetgpfDEELISPlPPSLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 106 AAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGS--ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI-TPPEV 182
Cdd:cd12168 113 TADTALFLILGALRNFSRAERSARAGKWRGFLDLTLahDPRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEEL 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 183 SASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVF 262
Cdd:cd12168 193 EKALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVF 272
                       250       260       270
                ....*....|....*....|....*....|..
gi 33990002 263 VEEPPRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12168 273 ENEPEVNPGLLKMPNVTLLPHMGTLTVETQEK 304
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
8-300 5.32e-77

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: 244.41  E-value: 5.32e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVV-TEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVD 86
Cdd:cd12176   2 KILLLENIHPSADELFRAGGIEVeRLKGALDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  87 AATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQS 166
Cdd:cd12176  82 AAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 167 FGMKTIGYDPITPPEVSASWGVEqmTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALL 246
Cdd:cd12176 162 LGMRVIFYDIAEKLPLGNARQVS--SLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALA 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33990002 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 ...
30-294 2.89e-73

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: 235.04  E-value: 2.89e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  30 VTEKQQMTKEELIAEIQNYDGLIVrSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAEL 109
Cdd:cd12162  27 LTVYDRTSPEEVVERIKDADIVIT-NKVVLDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQH 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 110 TCALVMSLSRHIPQAVISMKDGKWDRKK---FMG---SELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVs 183
Cdd:cd12162 106 TFALLLALARLVAYHNDVVKAGEWQKSPdfcFWDypiIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL- 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 184 aswGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFV 263
Cdd:cd12162 185 ---REGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLS 261
                       250       260       270
                ....*....|....*....|....*....|...
gi 33990002 264 EEPPRE--RALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12162 262 QEPPRAdnPLLKAAPNLIITPHIAWASREARQR 294
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
112-285 6.19e-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: 226.99  E-value: 6.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   112 ALVMSLSRHIPQAVISMKDGKWD-RKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSAS-WGVE 189
Cdd:pfam02826   2 ALLLALARRIPEADRQVRAGRWAsPDALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEeLGAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   190 QMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PR 268
Cdd:pfam02826  82 YVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEPlPA 161
                         170
                  ....*....|....*..
gi 33990002   269 ERALVNHPNVISCPHLG 285
Cdd:pfam02826 162 DHPLLDLPNVILTPHIA 178
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
37-310 4.96e-70

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: 227.18  E-value: 4.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  37 TKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:cd01619  35 NDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPEYSPNAVAEHTIALILA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 117 LSRHipQAVISMKDGKWDR--KKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVsASWGVEQMTLD 194
Cdd:cd01619 115 LLRN--RKYIDERDKNQDLqdAGVIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNPEL-EDKGVKYVSLE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 195 QLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEE--------- 265
Cdd:cd01619 192 ELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdle 271
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 33990002 266 -----PPRERALVNHPNVISCPHLGASTKEAQARCgKDIALQ-IVDMASGK 310
Cdd:cd01619 272 geifkDALNALLGRRPNVIITPHTAFYTDDALKNM-VEISCEnIVDFLEGE 321
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
38-291 2.48e-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: 224.70  E-value: 2.48e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  38 KEELIAEIQNYDGLIV-RSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTlSAAELTCALVMS 116
Cdd:cd12169  37 EDALAERLAPFDAIVLmRERTPFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCGTGGGPT-ATAELTWALILA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 117 LSRHIPQAVISMKDGKWDRKkfMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQM-TLDQ 195
Cdd:cd12169 116 LARNLPEEDAALRAGGWQTT--LGTGLAGKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLTAERAAAAGVEAAvSKEE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 196 LWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVN 274
Cdd:cd12169 194 LFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEPlPADHPLRG 273
                       250
                ....*....|....*..
gi 33990002 275 HPNVISCPHLGASTKEA 291
Cdd:cd12169 274 LPNVLLTPHIGYVTEEA 290
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
8-305 2.64e-68

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: 222.17  E-value: 2.64e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   8 RVLISESVDPCCKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDA 87
Cdd:cd12179   1 KILIIDKNHPSLTELLEALGFEVDYDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  88 ATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:cd12179  81 AKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGIIGYGNMGKAFAKRLSGF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 168 GMKTIGYDPItppEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:cd12179 161 GCKVIAYDKY---KNFGDAYAEQVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVK 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33990002 248 ALESGQCGGAGLDVFVEE----------PPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVD 305
Cdd:cd12179 238 ALKSGKILGACLDVLEYEkasfesifnqPEAFEYLIKSPKVILTPHIAGWTFESYEKIAEVLVDKIKA 305
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
7-309 1.90e-67

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: 220.24  E-value: 1.90e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   7 KRVLISESVDPCCKTVLQENGIVVTEKQQ--MTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd12157   2 PKVVITHKVHPEVLELLKPHCEVISNQTDepLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  85 VDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWD--RKKFMGSELYGKVLGIVGLGRIGKEVAT 162
Cdd:cd12157  82 VEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGDRFVRSGKFGgwRPKFYGTGLDGKTVGILGMGALGRAIAR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 163 RMQSFGMKTIGYDPIT-PPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIID 241
Cdd:cd12157 162 RLSGFGATLLYYDPHPlDQAEEQALNLRRVELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVD 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33990002 242 EAALLRALESGQCGGAGLDVF----VEEPPRERA-----LVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASG 309
Cdd:cd12157 242 EAAVAEALKSGHLGGYAADVFemedWARPDRPRSipqelLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
34-294 3.89e-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: 219.84  E-value: 3.89e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  34 QQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCAL 113
Cdd:cd12187  28 SQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFAL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 114 VMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTL 193
Cdd:cd12187 108 LLALSRKLREAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYVSL 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 194 DQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP------P 267
Cdd:cd12187 188 EELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaE 267
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 33990002 268 RER---------------ALVNHPNVISCPHLGASTKEAQAR 294
Cdd:cd12187 268 LFRedvspedlkklladhALLRKPNVIITPHVAYNTKEALER 309
PRK13243 PRK13243
glyoxylate reductase; Reviewed
25-321 1.65e-66

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 218.12  E-value: 1.65e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   25 ENGI----------VVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGII 94
Cdd:PRK13243  13 ENGIemleehfeveVWEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   95 VMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKK-------FMGSELYGKVLGIVGLGRIGKEVATRMQSF 167
Cdd:PRK13243  93 VTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGIIGFGRIGQAVARRAKGF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  168 GMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLR 247
Cdd:PRK13243 173 GMRILYYSRTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVK 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33990002  248 ALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNAQVL 321
Cdd:PRK13243 253 ALKEGWIAGAGLDVFEEEPYYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVNREVV 326
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
39-291 2.54e-65

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: 214.39  E-value: 2.54e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  39 EELIAEIQNYDGLIVrSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLS 118
Cdd:cd12161  40 AELIERSKDADIVMI-ANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 119 RHIPQAVISMKDGKwDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPiTPPEVSASWGVEQMTLDQLWP 198
Cdd:cd12161 119 RNIVPCDAAVRAGG-TKAGLIGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSR-SEKEEAKALGIEYVSLDELLA 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 199 QCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPP--RERALVNHP 276
Cdd:cd12161 197 ESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPlpADYPLLHAP 276
                       250
                ....*....|....*
gi 33990002 277 NVISCPHLGASTKEA 291
Cdd:cd12161 277 NTILTPHVAFATEEA 291
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
1-317 1.79e-64

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 215.43  E-value: 1.79e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002    1 MAPISVK----RVLISESVDPCCKTVLQENGI--VVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIG 74
Cdd:PRK11790   1 MAKVSLPkdkiKFLLLEGVHQSAVEVLRAAGYtnIEYHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAEKLVAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   75 RAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDrKKFMGS-ELYGKVLGIVGL 153
Cdd:PRK11790  81 CFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWN-KSAAGSfEVRGKTLGIVGY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  154 GRIGKEVATRMQSFGMKTIGYDPITP-PEVSAswgvEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKV 231
Cdd:PRK11790 160 GHIGTQLSVLAESLGMRVYFYDIEDKlPLGNA----RQVgSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAIL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  232 VNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-----PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDM 306
Cdd:PRK11790 236 INASRGTVVDIDALADALKSGHLAGAAIDVFPVEPksngdPFESPLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKY 315
                        330
                 ....*....|.
gi 33990002  307 ASGKALVGAVN 317
Cdd:PRK11790 316 SDNGSTLSAVN 326
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
24-291 3.82e-63

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: 209.31  E-value: 3.82e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  24 QENGI-VVTEKQQMTKEElIAEIQNYDGLIVRSATKVTADVIN--AGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPS 100
Cdd:cd12186  21 KEHPVeVDTTTELLTPET-VDLAKGYDGVVVQQTLPYDEEVYEklAEYGIKQIALRSAGVDMIDLDLAKENGLKITNVPA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 101 GNTLSAAELTCALVMSLSRHIPQAVISMKDG--KWDrKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPIT 178
Cdd:cd12186 100 YSPRAIAEFAVTQALNLLRNTPEIDRRVAKGdfRWA-PGLIGREIRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYP 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 179 PPEVsASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAG 258
Cdd:cd12186 179 NPEL-EKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAA 257
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 33990002 259 LDVF--------------VEEPPRERALVNHPNVISCPHLGASTKEA 291
Cdd:cd12186 258 LDTYenetgyfnkdwsgkEIEDEVLKELIAMPNVLITPHIAFYTDTA 304
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
59-322 1.33e-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: 207.80  E-value: 1.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  59 VTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWD--RK 136
Cdd:cd12167  62 LDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWgwPT 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 137 KFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGL 216
Cdd:cd12167 142 RRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVSLDELLARSDVVSLHAPLTPETRGM 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 217 LNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQcGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARC 295
Cdd:cd12167 222 IDARLLALMRDGATFINTARGALVDEAALLAELRSGR-LRAALDVTDPEPlPPDSPLRTLPNVLLTPHIAGSTGDERRRL 300
                       250       260
                ....*....|....*....|....*..
gi 33990002 296 GKDIALQIVDMASGKALVGAVNAQVLA 322
Cdd:cd12167 301 GDYALDELERFLAGEPLLHEVTPERLA 327
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
46-316 1.78e-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: 199.59  E-value: 1.78e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  46 QNYDGLIVRSATKVTADVINAGSSL--KIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQ 123
Cdd:cd12183  43 KGFDAVCVFVNDDLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHR 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 124 AVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVsASWGVEQMTLDQLWPQCDYI 203
Cdd:cd12183 123 AYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPEL-AKLGVEYVDLDELLAESDII 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 204 TVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPR--------------- 268
Cdd:cd12183 202 SLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLffedhsdeiiqddvl 281
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 33990002 269 ERaLVNHPNVISCPHLGASTKEAQarcgKDIALQ----IVDMASGKALVGAV 316
Cdd:cd12183 282 AR-LLSFPNVLITGHQAFFTKEAL----TNIAETtlenLDDFEAGKPLKNEV 328
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
50-291 8.02e-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: 194.22  E-value: 8.02e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  50 GLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMK 129
Cdd:cd12156  45 AVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 130 DGKWDRKKF-MGSELYGKVLGIVGLGRIGKEVATRMQSFGMkTIGY-DPITPPEVsaSWGVEQmTLDQLWPQCDYITVHT 207
Cdd:cd12156 125 AGRWPKGAFpLTRKVSGKRVGIVGLGRIGRAIARRLEAFGM-EIAYhGRRPKPDV--PYRYYA-SLLELAAESDVLVVAC 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 208 PLMASTTGLLNdASFAKC--KKGVkVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHPNVISCPHLG 285
Cdd:cd12156 201 PGGPATRHLVN-AEVLEAlgPDGV-LVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEPNVPAALLDLDNVVLTPHIA 278

                ....*.
gi 33990002 286 ASTKEA 291
Cdd:cd12156 279 SATVET 284
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-312 7.86e-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: 189.76  E-value: 7.86e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  61 ADVINAGSSLKIIGRAGTGVDNVDVDAATKrGIIVMNTpSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDR---KK 137
Cdd:cd12165  52 EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANN-HGNSPAVAEHALALILALAKRIVEYDNDLRRGIWHGragEE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 138 FMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTG 215
Cdd:cd12165 130 PESKELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGTLSD--LDEALEQADVVVVALPLTKQTRG 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 216 LLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERA-------LVNHPNVISCPHLGAST 288
Cdd:cd12165 208 LIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVWWRYPSRGDPvapsrypFHELPNVIMSPHNAGWT 287
                       250       260
                ....*....|....*....|....
gi 33990002 289 KEAQARCGKDIALQIVDMASGKAL 312
Cdd:cd12165 288 EETFRRRIDEAAENIRRYLRGEPL 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
19-291 6.22e-55

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: 187.42  E-value: 6.22e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  19 CKTVLQENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSL--KIIGRAGTGVDNVDVDAATKRGIIVM 96
Cdd:cd12185  16 FEKFAKEYNVEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAgvKYISTRSIGYDHIDLDAAKELGIKVS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  97 NTP-SGNtlSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12185  96 NVTySPN--SVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 176 PITPPEVSAswGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCG 255
Cdd:cd12185 174 PYPNEEVKK--YAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIG 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 33990002 256 GAGLDVFVEE-------------PPRERALVN-HPNVISCPHLGASTKEA 291
Cdd:cd12185 252 GAALDVIEGEdgiyyndrkgdilSNRELAILRsFPNVILTPHMAFYTDQA 301
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
7-317 8.91e-54

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: 184.26  E-value: 8.91e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   7 KRVLISESVDPCCKTVLQEN--GIVVTEKqqmTKEELIAEIQNYDGLIvrsATKVTADVINAGSSLKIIGRAGTGVDNVD 84
Cdd:cd05300   1 MKILVLSPLDDEHLERLRAAapGAELRVV---TAEELTEELADADVLL---GNPPLPELLPAAPRLRWIQSTSAGVDALL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  85 VDAATKRGIIVMNTpSG-NTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGsELYGKVLGIVGLGRIGKEVATR 163
Cdd:cd05300  75 FPELLERDVVLTNA-RGiFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQRRGPVR-ELAGKTVLIVGLGDIGREIARR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 164 MQSFGMKTIGYD---PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGII 240
Cdd:cd05300 153 AKAFGMRVIGVRrsgRPAPPVVDEVYTPDE--LDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVV 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33990002 241 DEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVN 317
Cdd:cd05300 231 DEDALIEALESGRIAGAALDVFEEEPlPADSPLWDLPNVIITPHISGDSPSYPERVVEIFLENLRRYLAGEPLLNVVD 308
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
37-294 1.93e-52

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 180.67  E-value: 1.93e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   37 TKEELIAEIQnydGLIVRSATKV--TADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALV 114
Cdd:PRK06487  35 TPEQVAERLR---GAQVAISNKValDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  115 MSLSRHIPQAVISMKDGKWDRKK------FMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKT-IGYDPITPPevsaswG 187
Cdd:PRK06487 112 LALATRLPDYQQAVAAGRWQQSSqfclldFPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVlIGQLPGRPA------R 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  188 VEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPP 267
Cdd:PRK06487 186 PDRLPLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVEPP 265
                        250       260       270
                 ....*....|....*....|....*....|
gi 33990002  268 RE-RALV--NHPNVISCPHLGASTKEAQAR 294
Cdd:PRK06487 266 VNgNPLLapDIPRLIVTPHSAWGSREARQR 295
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
37-310 4.57e-51

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 176.71  E-value: 4.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   37 TKEELIAEIQNYDgLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:PRK08410  32 SPEEVIERIKDAN-IIITNKVVIDKEVLSQLPNLKLICITATGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  117 LSRHIPQAVISMKDGKWDRKKF------MGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYdpiTPPEVSASWGVEQ 190
Cdd:PRK08410 111 LLGRINYYDRYVKSGEYSESPIfthisrPLGEIKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYY---STSGKNKNEEYER 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  191 MTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCgGAGLDVFVEEP-PRE 269
Cdd:PRK08410 188 VSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKEPmEKN 266
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 33990002  270 RALV---NHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGK 310
Cdd:PRK08410 267 HPLLsikNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEGG 310
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
59-294 5.30e-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: 5.30e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  59 VTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWD---- 134
Cdd:cd05302  74 MTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNvadv 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 135 -RKKFmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPIT-PPEVSASWGVEQM-TLDQLWPQCDYITVHTPLMA 211
Cdd:cd05302 154 vKRAY---DLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRlPEEVEKELGLTRHaDLEDMVSKCDVVTINCPLHP 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 212 STTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKE 290
Cdd:cd05302 231 ETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPaPKDHPWRTMPNNAMTPHISGTTLD 310

                ....
gi 33990002 291 AQAR 294
Cdd:cd05302 311 AQAR 314
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
43-275 7.10e-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: 169.25  E-value: 7.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  43 AEIQNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRhip 122
Cdd:cd12158  32 EDLKDADVLLVRSVTKVNEALL-EGSKVKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQ--- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 123 qavismkdgkwdRKKFmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPI-TPPEVSASWgveqMTLDQLWPQCD 201
Cdd:cd12158 108 ------------RQGF---SLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPrAEAEGDPGF----VSLEELLAEAD 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33990002 202 YITVHTPLMAS----TTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNH 275
Cdd:cd12158 169 IITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEIDLELLDK 246
PLN02928 PLN02928
oxidoreductase family protein
37-303 8.25e-46

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 163.70  E-value: 8.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   37 TKEELIAEIQNYDGLIVRSaTKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPS---GNTLSAAELTCAL 113
Cdd:PLN02928  51 AREDVPDVIANYDICVPKM-MRLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSegtGNAASCAEMAIYL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  114 VMSLSRHIPQAVISMKDGKWDRKkfMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGydpitppeVSASWGVEQMTL 193
Cdd:PLN02928 130 MLGLLRKQNEMQISLKARRLGEP--IGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLA--------TRRSWTSEPEDG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  194 DQLW---------------------PQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESG 252
Cdd:PLN02928 200 LLIPngdvddlvdekgghediyefaGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESG 279
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33990002  253 QCGGAGLDVFVEEP--PrERALVNHPNVISCPHLGASTKEAQARCGK---DIALQI 303
Cdd:PLN02928 280 HLGGLAIDVAWSEPfdP-DDPILKHPNVIITPHVAGVTEYSYRSMGKivgDAALQL 334
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
37-321 1.54e-45

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 162.61  E-value: 1.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   37 TKEELIAEIQNYDGLIvRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMS 116
Cdd:PRK15409  35 TVEQHAAAFAEAEGLL-GSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  117 LSRHIPQAVISMKDGKWDRK---KFMGSELYGKVLGIVGLGRIGKEVATRMQ-SFGMKTIGYDPITPPEVSASWGVEQMT 192
Cdd:PRK15409 114 TARRVVEVAERVKAGEWTASigpDWFGTDVHHKTLGIVGMGRIGMALAQRAHfGFNMPILYNARRHHKEAEERFNARYCD 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  193 LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERA 271
Cdd:PRK15409 194 LDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPlSVDSP 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 33990002  272 LVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNAQVL 321
Cdd:PRK15409 274 LLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEKNCVNPQVA 323
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
20-294 1.19e-44

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 161.77  E-value: 1.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   20 KTVLQENG--IVVTEKQQMTKEELIAEIQNYDglIVRSA----TKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGI 93
Cdd:PRK07574  61 RKFLEERGheLVVTSDKDGPDSDFEKELPDAD--VVISQpfwpAYLTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   94 IVMNTPSGNTLSAAELTCALVMSLSR-HIPQAVISMKdGKWDRKKFMGS--ELYGKVLGIVGLGRIGKEVATRMQSFGMK 170
Cdd:PRK07574 139 TVAEVTGSNSISVAEHVVMMILALVRnYEPSHRQAVE-GGWNIADCVSRsyDLEGMTVGIVGAGRIGLAVLRRLKPFDVK 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  171 TIGYDPI-TPPEVSASWGVE-QMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRA 248
Cdd:PRK07574 218 LHYTDRHrLPEEVEQELGLTyHVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRA 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 33990002  249 LESGQCGGAGLDV-FVEEPPRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:PRK07574 298 LESGHLAGYAGDVwFPQPAPADHPWRTMPRNGMTPHISGTTLSAQAR 344
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
63-294 1.27e-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: 1.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  63 VINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMgSE 142
Cdd:cd12155  54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMDSSL-LE 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 143 LYGKVLGIVGLGRIGKEVATRMQSFGMKTIGydpitppeVSASwG--VEQM----TLDQL---WPQCDYITVHTPLMAST 213
Cdd:cd12155 133 LYGKTILFLGTGSIGQEIAKRLKAFGMKVIG--------VNTS-GrdVEYFdkcyPLEELdevLKEADIVVNVLPLTEET 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 214 TGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQ 292
Cdd:cd12155 204 HHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPlPKDSPLWDLDNVLITPHISGVSEHFN 283

                ..
gi 33990002 293 AR 294
Cdd:cd12155 284 ER 285
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
40-291 3.95e-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: 150.91  E-value: 3.95e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  40 ELIAEIQNYDGLIVRSATKVTADVinagssLKIIGRAG--------TGVDNVDVDAATKRGIIVMNTPSGNTLSAAELTC 111
Cdd:cd12184  37 ENVHLAKGHDAVIVRGNCFADKEN------LEIYKEYGikyvftrtVGFNHIDLEAAKELGFKMARVPSYSPNAIAELAF 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 112 ALVMSLSRHIPQAVISMKDGKWDRKKFMGS-ELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPItpPEVSASWGVEQ 190
Cdd:cd12184 111 TLAMTLSRHTAYTASRTANKNFKVDPFMFSkEIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIY--PSDAAKDVVTF 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 191 MTLDQLWPQCDYITVHTPLMASTTG-LLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP--- 266
Cdd:cd12184 189 VSLDELLKKSDIISLHVPYIKGKNDkLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNEKeif 268
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 33990002 267 -----------PRERALVN-HPNVISCPHLGASTKEA 291
Cdd:cd12184 269 fkdfdgdkiedPVVEKLLDlYPRVLLTPHIGSYTDEA 305
PLN03139 PLN03139
formate dehydrogenase; Provisional
29-294 4.47e-40

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 149.23  E-value: 4.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   29 VVTEKQQMTKEELIAEIQNYDGLIVRS--ATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSA 106
Cdd:PLN03139  79 IVTDDKEGPDCELEKHIPDLHVLITTPfhPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  107 AELTCALVMSLSRHIPQAVISMKDGKWDRKK--FMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPIT-PPEVS 183
Cdd:PLN03139 159 AEDELMRILILLRNFLPGYHQVVSGEWNVAGiaYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKmDPELE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  184 ASWGVEQMT-LDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVF 262
Cdd:PLN03139 239 KETGAKFEEdLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVW 318
                        250       260       270
                 ....*....|....*....|....*....|...
gi 33990002  263 VEEP-PRERALVNHPNVISCPHLGASTKEAQAR 294
Cdd:PLN03139 319 YPQPaPKDHPWRYMPNHAMTPHISGTTIDAQLR 351
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
70-319 1.03e-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: 143.41  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  70 LKIIGRAGTGVDNVDVDAATKRGIIV-MNTPsGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFMGSELYgKVl 148
Cdd:cd12164  59 LKAIFSLGAGVDHLLADPDLPDVPIVrLVDP-GLAQGMAEYVLAAVLRLHRDMDRYAAQQRRGVWKPLPQRPAAER-RV- 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 149 GIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCK 226
Cdd:cd12164 136 GVLGLGELGAAVARRLAALGFPVSGWSrsPKDIEGVTCFHGEEG--LDAFLAQTDILVCLLPLTPETRGILNAELLARLP 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 227 KGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQArcGKDIALQIVD 305
Cdd:cd12164 214 RGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPlPADHPLWRHPRVTVTPHIAAITDPDSA--AAQVAENIRR 291
                       250
                ....*....|....
gi 33990002 306 MASGKALVGAVNAQ 319
Cdd:cd12164 292 LEAGEPLPNLVDRA 305
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
31-284 2.61e-38

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 142.63  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   31 TEKQQMTKEELIAEIQNYDgLIVRSATKVTADVINAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELT 110
Cdd:PRK06932  28 IEYDHTSAEQTIERAKDAD-IVITSKVLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  111 CALVMSLSRHIPQAVISMKDGKW-DRKKFMG-----SELYGKVLGIVGLGRIGKEVATRMQSFGMKTI------------ 172
Cdd:PRK06932 107 LGMIFALKHSLMGWYRDQLSDRWaTCKQFCYfdypiTDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLyaehkgasvcre 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  173 GYDPitppevsaswgveqmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESG 252
Cdd:PRK06932 187 GYTP----------------FEEVLKQADIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENG 250
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 33990002  253 QCGGAGLDVFVEEPPRE-----RALVNHPNVISCPHL 284
Cdd:PRK06932 251 KIAGAALDVLVKEPPEKdnpliQAAKRLPNLLITPHI 287
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
24-291 9.58e-35

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 133.33  E-value: 9.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   24 QENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKI--IGRAGTGVDNVDVDAATKRGIIVMNTPSG 101
Cdd:PRK08605  22 EKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIkqIAQRSAGFDTYDLELATKYNLIISNVPSY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  102 NTLSAAELTCALVMSLSRHIP--QAVISMKDGKWdrkkfmGSELYGKVLG-----IVGLGRIGKEVATRM-QSFGMKTIG 173
Cdd:PRK08605 102 SPESIAEFTVTQAINLVRHFNqiQTKVREHDFRW------EPPILSRSIKdlkvaVIGTGRIGLAVAKIFaKGYGSDVVA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  174 YDPItPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQ 253
Cdd:PRK08605 176 YDPF-PNAKAATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGL 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 33990002  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 5.13e-34

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: 130.54  E-value: 5.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 107 AELTCALVMSLSRHIPQAVISmKDGKWDRKKfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGY-DPITPPEVSas 185
Cdd:cd12180 100 AEFVLAAILAAAKRLPEIWVK-GAEQWRREP--LGSLAGSTLGIVGFGAIGQALARRALALGMRVLALrRSGRPSDVP-- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 186 wGVEQM-TLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVE 264
Cdd:cd12180 175 -GVEAAaDLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDP 253
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33990002 265 EP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNA 318
Cdd:cd12180 254 EPlPEGHPLYTHPRVRLSPHTSAIAPDGRRNLADRFLENLARYRAGQPLHDLVDP 308
PLN02306 PLN02306
hydroxypyruvate reductase
79-289 7.46e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.51  E-value: 7.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   79 GVDNVDVDAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGK---WDRKKFMGSELYGKVLGIVGLGR 155
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLyegWLPHLFVGNLLKGQTVGVIGAGR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  156 IGKEVATRM-QSFGMKTIGYDPI-----------------TPPEVSASWGvEQMTLDQLWPQCDYITVHTPLMASTTGLL 217
Cdd:PLN02306 176 IGSAYARMMvEGFKMNLIYYDLYqstrlekfvtaygqflkANGEQPVTWK-RASSMEEVLREADVISLHPVLDKTTYHLI 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33990002  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 5.86e-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: 121.93  E-value: 5.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  78 TGVDNVDvdAATKRGIIVMNTPSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKkFMGSeLYGKVLGIVGLGRIG 157
Cdd:cd12166  69 AGYDGVL--PLLPEGVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPR-RTPS-LADRRVLIVGYGSIG 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 158 KEVATRMQSFGMKT--IGYDPITPPEVSaswGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCA 235
Cdd:cd12166 145 RAIERRLAPFEVRVtrVARTARPGEQVH---GIDE--LPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVA 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 236 RGGIIDEAALLRALESGQCgGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVG 314
Cdd:cd12166 220 RGPVVDTDALVAELASGRL-RAALDVTDPEPlPPGHPLWSAPGVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLEN 298

                ..
gi 33990002 315 AV 316
Cdd:cd12166 299 VV 300
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
68-317 1.97e-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: 121.23  E-value: 1.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  68 SSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSG-NTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFM--GSELY 144
Cdd:cd12163  53 PNLRLVQLFSAGADHWLGHPLYKDPEVPLCTASGiHGPQIAEWVIGTWLVLSHHFLQYIELQKEQTWGRRQEAysVEDSV 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 145 GKVLGIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPE------------------VSASW--GVEQMTLDQ-LWPQCD 201
Cdd:cd12163 133 GKRVGILGYGSIGRQTARLAQALGMEVYAYTrsPRPTPEsrkddgyivpgtgdpdgsIPSAWfsGTDKASLHEfLRQDLD 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 202 YITVHTPLMASTTGLLNDASFAKC-KKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVI 279
Cdd:cd12163 213 LLVVSLPLTPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPlPADHPLWSAPNVI 292
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 33990002 280 SCPHLGASTKEAQarcgkDIALQIVD-----MASGKALVGAVN 317
Cdd:cd12163 293 ITPHVSWQTQEYF-----DRALDVLEenlerLRKGEPLINLVD 330
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
43-294 2.18e-30

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 122.07  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   43 AEIQNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAE--LTCALVMSLSRh 120
Cdd:PRK00257  33 AAVRDADVLLVRSVTRVDRALL-EGSRVRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDyvLGSLLTLAERE- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  121 ipqavismkdgkwdrkkfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPitpPEVSASWGVEQMTLDQLWPQC 200
Cdd:PRK00257 111 -------------------GVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDP---PRQEAEGDGDFVSLERILEEC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  201 DYITVHTPLM----ASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHP 276
Cdd:PRK00257 169 DVISLHTPLTkegeHPTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQIDLELADLC 248
                        250
                 ....*....|....*...
gi 33990002  277 nVISCPHLGASTKEAQAR 294
Cdd:PRK00257 249 -TIATPHIAGYSLDGKAR 265
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
42-294 2.58e-30

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 121.94  E-value: 2.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   42 IAEIQNYDGLIVRSATKVTADVInAGSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSGNTLSAAELT-CALVMSLSRH 120
Cdd:PRK15438  32 VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVfSSLLMLAERD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  121 ipqavismkdgkwdrkkfmGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPitpPEVSASWGVEQMTLDQLWPQC 200
Cdd:PRK15438 111 -------------------GFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDP---PRADRGDEGDFRSLDELVQEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  201 DYITVHTPLMAS----TTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEPPRERALVNHP 276
Cdd:PRK15438 169 DILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLKKV 248
                        250
                 ....*....|....*...
gi 33990002  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 8.29e-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: 240636  Cd Length: 303  Bit Score: 118.91  E-value: 8.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 107 AELTCALVMSLSRHIPQAVISmkdGKWDRKKFM--GSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPITPPEVSA 184
Cdd:cd12159  88 AEHALALLLAGLRQLPARARA---TTWDPAEEDdlVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNRSGRPVEGA 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 185 SWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVE 264
Cdd:cd12159 165 DETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDP 244
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33990002 265 EP-PRERALVNHPNVISCPHLGASTKEAQARCGKDIALQIVDMASGKALVGAVNA 318
Cdd:cd12159 245 EPlPDGHPLWSLPNALITPHVANTPEVIRPLLAERVAENVRAFAAGEPLLGVVDP 299
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
24-291 3.58e-28

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 114.63  E-value: 3.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002   24 QENGIVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINA--GSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTPSG 101
Cdd:PRK12480  22 KKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKleSYGIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  102 NTLSAAELTCALVMSLSRHIPQ--AVISMKDGKWdRKKFMGSELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYDPItp 179
Cdd:PRK12480 102 SPETIAEYSVSIALQLVRRFPDieRRVQAHDFTW-QAEIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAY-- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  180 PEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQCGGAGL 259
Cdd:PRK12480 179 PNKDLDFLTYKDSVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAI 258
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 33990002  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 1.22e-21

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 95.52  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  38 KEELIAEIQNYDGLIV-RSATKVTADVINAGSSLKIIGRAGTGVDNV-------DVDAATKRGIivmntpsgNTLSAAEL 109
Cdd:cd12160  27 AAPVPAEHHDAEVLVVwGNSSDNLADAARRLTRLRWVQALAAGPDAVlaagfapEVAVTSGRGL--------HDGTVAEH 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 110 TCALVMSLSRHIPQAVISMKDGKWDR----------KKFMGSELYGKVLgIVGLGRIGKEVATRMQSFGMKTIGydpitp 179
Cdd:cd12160  99 TLALILAAVRRLDEMREAQREHRWAGelgglqplrpAGRLTTLLGARVL-IWGFGSIGQRLAPLLTALGARVTG------ 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 180 peVSASWG-------VEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESG 252
Cdd:cd12160 172 --VARSAGeragfpvVAEDELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESG 249
                       250       260       270
                ....*....|....*....|....*....|..
gi 33990002 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 33990002   67 GSSLKIIGRAGTGVDNVDVDAATKRGIIVMNTpSGNTLSAAELTCALVMSLSRHIPQAVISMKDGKWDRKKFmgSELYGK 146
Cdd:PRK06436  47 GKKTKMIQSLSAGVDHIDVSGIPENVVLCSNA-GAYSISVAEHAFALLLAWAKNICENNYNMKNGNFKQSPT--KLLYNK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  147 VLGIVGLGRIGKEVATRMQSFGMKTIGYdpiTPPEVSASWGVEQMTLDQLWPQCDYITVHTPLMASTTGLLNDASFAKCK 226
Cdd:PRK06436 124 SLGILGYGGIGRRVALLAKAFGMNIYAY---TRSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFR 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  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 2.57e-20

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: 91.21  E-value: 2.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  28 IVVTEKQQMTKEELIAEIQNYDGLIVRSATKVTADVINAGSSLKIIGRAGTGVD----NVDVDAATKRGIIVMNTPSGNT 103
Cdd:cd12170  27 VVFYDDIPESDEEIIERIGDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 104 LSAAE-LTCALVMSLS-------RHIPQavismkdgkwdrkkfmgsELYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD 175
Cdd:cd12170 107 EGVVEyVISELIRLLHgfggkqwKEEPR------------------ELTGLKVGIIGLGTTGQMIADALSFFGADVYYYS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 176 PITPPEVSASwGVEQMTLDQLWPQCDYITVHTPlmaSTTGLLNDASFAKCKKGVKVVNCARGGIIDEAALLRALESGQ-- 253
Cdd:cd12170 169 RTRKPDAEAK-GIRYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKASGyn 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 33990002 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 8.63e-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: 8.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  57 TKVTADVInAGSSLKIIGRAGTGVDNVDV-DAATKRGIIVMNTP-------SGNTLSAAELtcaLVMSLSRHIPQAVISM 128
Cdd:cd12154  76 TNAEYALI-QKLGDRLLFTYTIGADHRDLtEALARAGLTAIAVEgvelpllTSNSIGAGEL---SVQFIARFLEVQQPGR 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002 129 KDGKWDrkkfmgseLYGKVLGIVGLGRIGKEVATRMQSFGMKTIGYD--PITPPEVSASWGVEQMTLDQLWPQCDYITVH 206
Cdd:cd12154 152 LGGAPD--------VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDinVEALEQLEELGGKNVEELEEALAEADVIVTT 223
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33990002 207 TPLMASTTGLLNDAS-FAKCKKGVKVVNCARG-GIIDEAALLRALESGQCGGAGLDVFVEEP 266
Cdd:cd12154 224 TLLPGKRAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGP 285
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
148-319 1.35e-16

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 80.61  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  148 LGIVGLGRIGKEVATRMQSFG--MKTIGYDPITPPEVSASWGVEQmtLDQLWPQCDYITVHTPLMASTTGLLNDASFAKC 225
Cdd:PRK15469 139 IGILGAGVLGSKVAQSLQTWGfpLRCWSRSRKSWPGVQSFAGREE--LSAFLSQTRVLINLLPNTPETVGIINQQLLEQL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33990002  226 KKGVKVVNCARGGIIDEAALLRALESGQCGGAGLDVFVEEP-PRERALVNHPNVISCPHLGASTKEAQARcgKDIALQIV 304
Cdd:PRK15469 217 PDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPlPPESPLWQHPRVAITPHVAAVTRPAEAV--EYISRTIA 294
                        170
                 ....*....|....*
gi 33990002  305 DMASGKALVGAVNAQ 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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