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Conserved domains on  [gi|697821559|ref|XP_009647160|]
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C-terminal-binding protein 1 isoform X2 [Egretta garzetta]

Protein Classification

C-terminal binding protein( domain architecture ID 10143094)

C-terminal binding protein (CtBP) functions as a transcriptional regulator by tethering chromatin remodeling proteins, such as histone deacetylases, histone methyl transferases, and histone demethylases, to DNA-bound transcription factors; CtBP may also have NAD-dependent dehydrogenase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 3.94e-147

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: 421.15  E-value: 3.94e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  34 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 110 NIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 190 RVGQAVALRAKAFGFSVIFYDPYLSDGmERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDG-VAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 270 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 697821559 350 PDS 352
Cdd:cd05299  310 PRN 312
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 3.94e-147

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: 421.15  E-value: 3.94e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  34 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 110 NIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 190 RVGQAVALRAKAFGFSVIFYDPYLSDGmERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDG-VAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 270 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 697821559 350 PDS 352
Cdd:cd05299  310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
36-359 1.19e-98

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: 297.77  E-value: 1.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDI 113
Cdd:COG1052    3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 114 KSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 193
Cdd:COG1052   83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 194 AVALRAKAFGFSVIFYDPYLSDGMErALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 273
Cdd:COG1052  157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 274 GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 353
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                 ....*.
gi 697821559 354 KNCVNK 359
Cdd:COG1052  311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
36-358 6.71e-84

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: 259.91  E-value: 6.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559   36 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIVRIGSGFDNIDIK 114
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  115 SAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 194
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  195 VALRAKAFGFSVIFYDPYLSDGMERALGLQRVSTLQDLLF---HSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTA 271
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  272 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 351
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 697821559  352 slKNCVN 358
Cdd:pfam00389 307 --ANAVN 311
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
86-358 5.14e-69

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: 227.98  E-value: 5.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559   86 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvqsv 165
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  166 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDgmERA--LGLQRVSTLQDLLFHSDCVTLHC 243
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  244 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAA 323
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 697821559  324 WYSEQASIEMREEAAREIRRAITGripDSLKNCVN 358
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVN 311
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
36-347 2.58e-58

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 194.05  E-value: 2.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLTREDLEKFKALRIIVRIGSGFDNID 112
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 113 IKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSvEQIREVASGAARIRGETLGIIGLGRVG 192
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 193 QAVALRAKAFGFSVIFYDPylsDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTAR 272
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697821559 273 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfSQGPL---KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:PRK08410 234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
34-352 3.94e-147

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: 421.15  E-value: 3.94e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  34 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 109
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 110 NIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 189
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 190 RVGQAVALRAKAFGFSVIFYDPYLSDGmERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVN 269
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDG-VAALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 270 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 349
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 697821559 350 PDS 352
Cdd:cd05299  310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
36-343 1.79e-107

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: 319.96  E-value: 1.79e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGRDCTVEMPILKD-VATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIK 114
Cdd:cd05198    2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 115 SAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRvqsveqIREVASGAARIRGETLGIIGLGRVGQA 194
Cdd:cd05198   81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 195 VALRAKAFGFSVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGG 274
Cdd:cd05198  155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVVS-LDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697821559 275 LVDEKALAQALKEGRIRGAALDVHESEPFSFSqGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 343
Cdd:cd05198  234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
36-359 1.19e-98

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: 297.77  E-value: 1.19e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDI 113
Cdd:COG1052    3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 114 KSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 193
Cdd:COG1052   83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 194 AVALRAKAFGFSVIFYDPYLSDGMErALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 273
Cdd:COG1052  157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 274 GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 353
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                 ....*.
gi 697821559 354 KNCVNK 359
Cdd:COG1052  311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
55-358 3.62e-94

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: 286.32  E-value: 3.62e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  55 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEET 134
Cdd:COG0111   23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 135 ADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLS 214
Cdd:COG0111  102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 215 DGMERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAA 294
Cdd:COG0111  175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697821559 295 LDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRipdSLKNCVN 358
Cdd:COG0111  255 LDVFEPEPLPADS-PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
64-344 3.23e-88

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: 270.90  E-value: 3.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  64 STQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHIL 143
Cdd:cd12172   37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 144 NLYRRTTWLHQALREG--TRVQSVEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERAL 221
Cdd:cd12172  115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 222 GLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE 301
Cdd:cd12172  184 GVEFVS-LEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 697821559 302 PFSfSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 344
Cdd:cd12172  263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
88-348 1.49e-86

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: 266.59  E-value: 1.49e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  88 TREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGT----RVQ 163
Cdd:cd12173   53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 164 SVEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGlQRVSTLQDLLFHSDCVTLHC 243
Cdd:cd12173  133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISLHT 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 244 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAA 323
Cdd:cd12173  201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                        250       260
                 ....*....|....*....|....*
gi 697821559 324 WYSEQASIEMREEAAREIRRAITGR 348
Cdd:cd12173  280 ASTEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
36-358 6.71e-84

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: 259.91  E-value: 6.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559   36 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIVRIGSGFDNIDIK 114
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  115 SAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 194
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  195 VALRAKAFGFSVIFYDPYLSDGMERALGLQRVSTLQDLLF---HSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTA 271
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  272 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 351
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 697821559  352 slKNCVN 358
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
88-358 5.05e-78

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: 245.22  E-value: 5.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  88 TREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvqsveq 167
Cdd:cd12178   56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRG-------- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 168 ireVASGAAR-------IRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALGLQRVStLQDLLFHSDCV 239
Cdd:cd12178  128 ---GFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD-LDELLKESDFV 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 240 TLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGpLKDAPNLICT 319
Cdd:cd12178  204 SLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVILT 281
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 697821559 320 PHAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVN 358
Cdd:cd12178  282 PHIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
84-350 3.10e-76

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: 240.17  E-value: 3.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  84 TITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvq 163
Cdd:cd12175   52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 164 svEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALGLQRVStLQDLLFHSDCVTLH 242
Cdd:cd12175  128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYVE-LDELLAESDVVSLH 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 243 CNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHA 322
Cdd:cd12175  205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDD-PLLRLDNVILTPHI 283
                        250       260
                 ....*....|....*....|....*...
gi 697821559 323 AWYSEQASIEMREEAAREIRRAITGRIP 350
Cdd:cd12175  284 AGVTDESYQRMAAIVAENIARLLRGEPP 311
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
98-347 4.03e-74

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: 235.13  E-value: 4.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  98 LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEqirevASGAAR 177
Cdd:cd12168   77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 178 IRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALGLqRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDF 256
Cdd:cd12168  152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALAT-YYVSLDELLAQSDVVSLNCPLTAATRHLINKK 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 257 TIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFsFSQGpLKDAPNLICTPHAAWYSEQASIEMREE 336
Cdd:cd12168  231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPE-VNPG-LLKMPNVTLLPHMGTLTVETQEKMEEL 308
                        250
                 ....*....|.
gi 697821559 337 AAREIRRAITG 347
Cdd:cd12168  309 VLENIEAFLET 319
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
87-335 1.28e-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: 233.50  E-value: 1.28e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVE 166
Cdd:cd12162   55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 167 Q------IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGmeraLGLQRVStLQDLLFHSDCVT 240
Cdd:cd12162  135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPP----LREGYVS-LDELLAQSDVIS 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsqgP------LKDAP 314
Cdd:cd12162  203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplLKAAP 276
                        250       260
                 ....*....|....*....|.
gi 697821559 315 NLICTPHAAWyseqASIEMRE 335
Cdd:cd12162  277 NLIITPHIAW----ASREARQ 293
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
36-348 2.35e-72

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: 230.65  E-value: 2.35e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGRDctVEMPILKDVA-----TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDN 110
Cdd:cd01619    3 VLIYDYRD--DELEIEKEILkaggvDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 111 IDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGR 190
Cdd:cd01619   81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRE-------LEDQTVGVVGTGK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 191 VGQAVALRAKAFGFSVIFYDPYLSDGMErALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNT 270
Cdd:cd01619  154 IGRAVAQRAKGFGMKVIAYDPFRNPELE-DKGVKYVS-LEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 271 ARGGLVDEKALAQALKEGRIRGAALDVHESE-----------PFSFSQGP-LKDAPNLICTPHAAWYSEQASIEMREEAA 338
Cdd:cd01619  232 ARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISC 311
                        330
                 ....*....|
gi 697821559 339 REIRRAITGR 348
Cdd:cd01619  312 ENIVDFLEGE 321
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
48-347 2.08e-71

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: 227.66  E-value: 2.08e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  48 MPILKDVATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVC 124
Cdd:cd05301   14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 125 NVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvqSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGF 204
Cdd:cd05301   93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAG----EWKGWSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 205 SVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 284
Cdd:cd05301  169 KILYHNRSRKPEAEEELGARYVS-LDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEA 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697821559 285 LKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:cd05301  248 LKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
86-358 5.14e-69

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: 227.98  E-value: 5.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559   86 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvqsv 165
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  166 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDgmERA--LGLQRVSTLQDLLFHSDCVTLHC 243
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  244 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAA 323
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 697821559  324 WYSEQASIEMREEAAREIRRAITGripDSLKNCVN 358
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVN 311
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
139-323 9.39e-68

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: 213.51  E-value: 9.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  139 MCHILNLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGM 217
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  218 ERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 297
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 697821559  298 HESEPFSFSQgPLKDAPNLICTPHAA 323
Cdd:pfam02826 154 FEPEPLPADH-PLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
86-321 3.02e-67

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: 216.64  E-value: 3.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrvqsv 165
Cdd:cd05303   52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 166 eQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNL 245
Cdd:cd05303  126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTVS-LEELLKNSDFISLHVPL 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697821559 246 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgpLKDAPNLICTPH 321
Cdd:cd05303  204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
67-343 6.94e-66

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: 213.55  E-value: 6.94e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  67 EIHEKVLNEAVGA--LMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILN 144
Cdd:cd12171   35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 145 LYRRTTWLHQALREGtrvqsveQIREVASGAAR----IRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERA 220
Cdd:cd12171  115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 221 LGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHES 300
Cdd:cd12171  188 DGVKKVS-LEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 697821559 301 EPFSfSQGPLKDAPNLICTPHAAWYSEQA---SIEMreeAAREIRR 343
Cdd:cd12171  267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
37-355 8.16e-66

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 213.72  E-value: 8.16e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  37 ALLDGRDCTVEMPILKDVATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLTREDLEKFKALRIIVRIGSGFDN 110
Cdd:cd12177    7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 111 IDIKSAGDLGIAVCNVPAA----SVEETAdstMCHILNLYRRTTWLHQALREGtrvqsveQIREVASGAAR-IRGETLGI 185
Cdd:cd12177   83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 186 IGLGRVGQAVA-LRAKAFGFSVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQG 264
Cdd:cd12177  153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPVS-LEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 265 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 344
Cdd:cd12177  232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADH-PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                        330
                 ....*....|.
gi 697821559 345 ITGRIPDSLKN 355
Cdd:cd12177  311 LAGKEPKGILN 321
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
89-358 8.52e-65

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: 210.49  E-value: 8.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  89 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRttwLHQALREGTRVQSVEQI 168
Cdd:cd12174   42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRN---IIQAIKWVTNGDGDDIS 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 169 REVASGAAR-----IRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDgmERALGL----QRVSTLQDLLFHSDCV 239
Cdd:cd12174  119 KGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSV--EAAWKLsvevQRVTSLEELLATADYI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 240 TLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEpfsfsqgPLKDAPNLICT 319
Cdd:cd12174  197 TLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIAT 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 697821559 320 PHAAWYSEQASIEMREEAAREIRRAI-TGRIPdslkNCVN 358
Cdd:cd12174  270 PHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
64-347 5.67e-60

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: 198.91  E-value: 5.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  64 STQEIHEKVLNEAVGA---LMYHTITLTREDLEKFKAL---RIIVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADS 137
Cdd:cd12186   30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEYgikQIALRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 138 TMCHILNLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDG 216
Cdd:cd12186  109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 217 MErALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALD 296
Cdd:cd12186  182 LE-KFLLYYDS-LEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697821559 297 VHESE----PFSFSQGPLKDA--------PNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:cd12186  260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEG 322
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
87-348 2.31e-58

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: 194.42  E-value: 2.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVE 166
Cdd:cd12187   53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 167 QIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNLN 246
Cdd:cd12187  133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYVS-LEELLQESDIISLHVPYT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 247 EHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPF----------SFSQGPLKDA--- 313
Cdd:cd12187  205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVlreeaelfreDVSPEDLKKLlad 284
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 697821559 314 ------PNLICTPHAAWYSEQASIEMREEAAREIRRAITGR 348
Cdd:cd12187  285 hallrkPNVIITPHVAYNTKEALERILDTTVENIKAFAAGQ 325
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
36-347 2.58e-58

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 194.05  E-value: 2.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  36 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLTREDLEKFKALRIIVRIGSGFDNID 112
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 113 IKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSvEQIREVASGAARIRGETLGIIGLGRVG 192
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 193 QAVALRAKAFGFSVIFYDPylsDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTAR 272
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697821559 273 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfSQGPL---KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:PRK08410 234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
PRK13243 PRK13243
glyoxylate reductase; Reviewed
66-355 1.75e-56

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 189.62  E-value: 1.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  66 QEIHEKVLNEAV---GALMyhTITLTREDLEKFKA---LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTM 139
Cdd:PRK13243  32 REIPREVLLEKVrdvDALV--TMLSERIDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAW 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 140 CHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMER 219
Cdd:PRK13243 110 ALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEK 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 220 ALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHE 299
Cdd:PRK13243 190 ELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFE 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 697821559 300 SEPfsFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKN 355
Cdd:PRK13243 269 EEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVN 322
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
49-347 1.84e-56

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: 188.87  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  49 PILKDVATV-AFCD-AQSTQEIHEKVLN-EAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCN 125
Cdd:cd12169   19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 126 VPAaSVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVeqirevasgAARIRGETLGIIGLGRVGQAVALRAKAFGFS 205
Cdd:cd12169   98 TGG-GPTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 206 VIFYDPYLSDGMERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQAL 285
Cdd:cd12169  168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 697821559 286 KEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:cd12169  248 RAGRIAGAALDVFDVEPLPADH-PLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
79-338 3.44e-56

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: 188.58  E-value: 3.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  79 ALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALRE 158
Cdd:cd12161   51 IVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 159 GTRVQSVEQiREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMErALGLQRVStLQDLLFHSDC 238
Cdd:cd12161  131 GGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK-ALGIEYVS-LDELLAESDI 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 239 VTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLIC 318
Cdd:cd12161  201 VSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTIL 280
                        250       260
                 ....*....|....*....|
gi 697821559 319 TPHAAWYSEQAsIEMREEAA 338
Cdd:cd12161  281 TPHVAFATEEA-MEKRAEIV 299
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
86-329 4.15e-55

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: 186.11  E-value: 4.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKAL--RIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTtwlHQALregtrvq 163
Cdd:cd12183   55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKI---HRAY------- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 164 sveqirevasgaARIR---------------GETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMErALGLQRVSt 228
Cdd:cd12183  125 ------------NRVRegnfsldgllgfdlhGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELA-KLGVEYVD- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 229 LQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSF--- 305
Cdd:cd12183  191 LDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFfed 270
                        250       260       270
                 ....*....|....*....|....*....|...
gi 697821559 306 -SQGPLKDA--------PNLICTPHAAWYSEQA 329
Cdd:cd12183  271 hSDEIIQDDvlarllsfPNVLITGHQAFFTKEA 303
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
61-348 4.34e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 182.98  E-value: 4.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  61 DAQSTQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMC 140
Cdd:PRK06487  32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 141 HILNLYRRTTWLHQALREGtRVQSVEQ-------IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFSVIfydpyL 213
Cdd:PRK06487 110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 214 SDGMERALGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGA 293
Cdd:PRK06487 177 GQLPGRPARPDRLP-LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 697821559 294 ALDVHESEPfSFSQGPL--KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGR 348
Cdd:PRK06487 256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
57-342 9.37e-51

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: 174.32  E-value: 9.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  57 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLTREDLEKFKAL-------RIIvrigsGFDNIDIKSAGDLGIAVCNVPA 128
Cdd:cd12185   27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVTY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 129 aSVEETADSTMCHILNLYRRTTW-LHQALREGTRVQSVeQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVI 207
Cdd:cd12185  100 -SPNSVADYTVMLMLMALRKYKQiMKRAEVNDYSLGGL-QGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCKIL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 208 FYDPYLSDGMERalGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKE 287
Cdd:cd12185  171 AYDPYPNEEVKK--YAEYVD-LDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLES 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697821559 288 GRIRGAALDVHESEPFSFSQ------------GPLKDAPNLICTPHAAWYSEQASIEMREEAAREIR 342
Cdd:cd12185  248 GKIGGAALDVIEGEDGIYYNdrkgdilsnrelAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLV 314
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
82-321 1.56e-47

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: 166.73  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  82 YHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTR 161
Cdd:cd05302   69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 162 vqsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALGLQRVSTLQDLLFHSDCVT 240
Cdd:cd05302  149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGPLKDAPNLICTP 320
Cdd:cd05302  224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302

                 .
gi 697821559 321 H 321
Cdd:cd05302  303 H 303
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
86-343 4.96e-47

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: 163.90  E-value: 4.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKALriiVRIGS---GFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtrv 162
Cdd:cd12176   53 QLTEEVLEAAPKL---LAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG--- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 163 qsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPylsdgmERALGL---QRVSTLQDLLFHSDCV 239
Cdd:cd12176  127 ----IWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYDI------AEKLPLgnaRQVSSLEELLAEADFV 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 240 TLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFS----FSQgPLKDAPN 315
Cdd:cd12176  197 TLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngepFSS-PLQGLPN 275
                        250       260
                 ....*....|....*....|....*...
gi 697821559 316 LICTPHAAWYSEQASIEMREEAAREIRR 343
Cdd:cd12176  276 VILTPHIGGSTEEAQENIGLEVAGKLVK 303
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
86-366 1.63e-46

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: 163.50  E-value: 1.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQsv 165
Cdd:cd12167   61 PLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG-- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 166 eqiREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGLQRVStLQDLLFHSDCVTLHCNL 245
Cdd:cd12167  139 ---WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVS-LDELLARSDVVSLHAPL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 246 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHESEPFSFSQgPLKDAPNLICTPHAAWY 325
Cdd:cd12167  215 TPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLPPDS-PLRTLPNVLLTPHIAGS 292
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 697821559 326 SEQASIEMREEAAREIRRAITGRIPdslKNCVNKDHLTAAT 366
Cdd:cd12167  293 TGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
87-341 1.91e-46

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 162.66  E-value: 1.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNL-YRRTTWLHQALreGTRVQSV 165
Cdd:PRK06932  55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALkHSLMGWYRDQL--SDRWATC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 166 EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDpylsdgmERALGLQRVSTL--QDLLFHSDCVTLHC 243
Cdd:PRK06932 133 KQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREGYTpfEEVLKQADIVTLHC 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 244 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPL----KDAPNLICT 319
Cdd:PRK06932 206 PLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLPNLLIT 284
                        250       260
                 ....*....|....*....|..
gi 697821559 320 PHAAWYSEQASIEMREEAAREI 341
Cdd:PRK06932 285 PHIAWASDSAVTTLVNKVAQNI 306
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
75-335 2.73e-46

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: 161.87  E-value: 2.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  75 EAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQ 154
Cdd:cd12156   42 RIRAVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADR 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 155 ALREGtrvqsvEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGmeraLGLQRVSTLQDLLF 234
Cdd:cd12156  122 FVRAG------RWPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPD----VPYRYYASLLELAA 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 235 HSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsQGP--LKD 312
Cdd:cd12156  192 ESDVLVVACPGGPATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLD 267
                        250       260
                 ....*....|....*....|...
gi 697821559 313 APNLICTPHAAWYSEQASIEMRE 335
Cdd:cd12156  268 LDNVVLTPHIASATVETRRAMGD 290
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
64-347 9.02e-46

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: 160.92  E-value: 9.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  64 STQEIHEKVLNeAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHIL 143
Cdd:cd12157   34 SREELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 144 NLYRRTTWLHQALREGTRvqsvEQIREVASGAArIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALG 222
Cdd:cd12157  113 GLGRHILAGDRFVRSGKF----GGWRPKFYGTG-LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHpLDQAEEQALN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 223 LQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE- 301
Cdd:cd12157  188 LRRVE-LDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEMEd 266
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 697821559 302 ------PFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 347
Cdd:cd12157  267 warpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
89-327 1.31e-43

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: 155.14  E-value: 1.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  89 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLyrrttwLHQALREGTRVQSVEQI 168
Cdd:cd12179   54 KEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLAL------FNKLNRADQEVRNGIWD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 169 REVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERAlglQRVStLQDLLFHSDCVTLHCNLNEH 248
Cdd:cd12179  128 REGNRGV-ELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAYA---EQVS-LETLFKEADILSLHIPLTPE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 249 NHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSF---SQGP-----LKDAPNLICTP 320
Cdd:cd12179  203 TRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFesiFNQPeafeyLIKSPKVILTP 282

                 ....*...
gi 697821559 321 H-AAWYSE 327
Cdd:cd12179  283 HiAGWTFE 290
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
86-335 3.69e-43

(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: 154.37  E-value: 3.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKALRI---IVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTT-WLHQALREGTR 161
Cdd:cd12184   55 FADKENLEIYKEYGIkyvFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAyTASRTANKNFK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 162 VQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGLQrvsTLQDLLFHSDCVTL 241
Cdd:cd12184  134 VDPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVVTFV---SLDELLKKSDIISL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 242 HC-NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--HESEPF--SFSQGPLKDA--- 313
Cdd:cd12184  204 HVpYIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvve 283
                        250       260
                 ....*....|....*....|....*...
gi 697821559 314 ------PNLICTPHAAWYSEQASIEMRE 335
Cdd:cd12184  284 klldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
87-341 3.73e-43

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 155.99  E-value: 3.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRvqsve 166
Cdd:PRK07574 104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 167 QIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPY-LSDGMERALGLQRVSTLQDLLFHSDCVTLHCNL 245
Cdd:PRK07574 179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 246 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHesepfsFSQGPLKD-----APNLICTP 320
Cdd:PRK07574 259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVW------FPQPAPADhpwrtMPRNGMTP 332
                        250       260
                 ....*....|....*....|...
gi 697821559 321 HAAW--YSEQASIemrEEAAREI 341
Cdd:PRK07574 333 HISGttLSAQARY---AAGTREI 352
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
70-351 1.17e-40

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: 147.39  E-value: 1.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  70 EKVLNEAvGALMYHTITLtREDLEKFKALRIIVRIGSGFDNIDIKSAGDlGIAVCNVPAASvEETADSTMCHILNLYRRT 149
Cdd:cd12165   35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHGNS-PAVAEHALALILALAKRI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 150 TWLHQALREGTRVQSVEQIREVASgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYD--PYLSDGMERALGlqrVS 227
Cdd:cd12165  111 VEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGT---LS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 228 TLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--------HE 299
Cdd:cd12165  184 DLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDP 263
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 697821559 300 SEPFSFsqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD 351
Cdd:cd12165  264 VAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
87-321 2.20e-40

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 149.17  E-value: 2.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALriiVRIGS---GFDNIDIKSAGDLGIAVCNVPAA---SVEETAdstMCHILNLYRRTTWLHQALREGT 160
Cdd:PRK11790  65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSntrSVAELV---IGEIILLLRGIPEKNAKAHRGG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 161 RVQSveqirevASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPylsdgMER-ALG-LQRVSTLQDLLFHSDC 238
Cdd:PRK11790 139 WNKS-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYDI-----EDKlPLGnARQVGSLEELLAQSDV 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 239 VTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQG---PLKDAPN 315
Cdd:PRK11790 207 VSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDN 286

                 ....*.
gi 697821559 316 LICTPH 321
Cdd:PRK11790 287 VILTPH 292
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
98-329 7.92e-38

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 140.26  E-value: 7.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  98 LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREgtrvqsvEQIREVASGAAR 177
Cdd:PRK08605  70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVRE-------HDFRWEPPILSR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 178 -IRGETLGIIGLGRVGQAVA-LRAKAFGFSVIFYDPYLSDGMerALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLIND 255
Cdd:PRK08605 143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKA--ATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 256 FTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFSQGPLKDA--------PNLICTPHAA 323
Cdd:PRK08605 221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                 ....*.
gi 697821559 324 WYSEQA 329
Cdd:PRK08605 301 FYTDAA 306
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
65-358 2.86e-37

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 138.35  E-value: 2.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  65 TQEIHEKVLNEAVGaLMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILN 144
Cdd:PRK15409  35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 145 LYRRttwlhqALREGTRVQSVEQIREVASG--AARIRGETLGIIGLGRVGQAVALRAKaFGFS--VIFYDPYLSDGMERA 220
Cdd:PRK15409 114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNmpILYNARRHHKEAEER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 221 LGLQRVStLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHES 300
Cdd:PRK15409 187 FNARYCD-LDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 697821559 301 EPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVN 358
Cdd:PRK15409 266 EPLSVDS-PLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVN 319
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
86-326 4.93e-36

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: 135.74  E-value: 4.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  86 TLTREDLEKFKALriIVR-----------------IGS---GFDNIDIKSAGDLGIAVCNVP---AASVeetADSTMCHI 142
Cdd:cd12158   28 EITAEDLKDADVL--LVRsvtkvneallegskvkfVGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSAL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 143 LNLYRRTTWLhqalregtrvqsveqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLsdgmERALG 222
Cdd:cd12158  103 LVLAQRQGFS-------------------------LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPR----AEAEG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 223 LQRVSTLQDLLFHSDCVTLHCNLNEH----NHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVH 298
Cdd:cd12158  154 DPGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233
                        250       260
                 ....*....|....*....|....*...
gi 697821559 299 ESEPfSFSQGPLKDApnLICTPHAAWYS 326
Cdd:cd12158  234 ENEP-EIDLELLDKV--DIATPHIAGYS 258
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
89-361 5.47e-35

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: 131.88  E-value: 5.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  89 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGtRVQSVEQI 168
Cdd:cd05300   51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAER-RWQRRGPV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 169 REvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIfydpylsdGMER-----ALGLQRVST---LQDLLFHSDCVT 240
Cdd:cd05300  130 RE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRsgrpaPPVVDEVYTpdeLDELLPEADYVV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 241 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTP 320
Cdd:cd05300  195 NALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVIITP 273
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 697821559 321 HAAWYSEqasiEMREEAA----REIRRAITGRipdSLKNCVNKDH 361
Cdd:cd05300  274 HISGDSP----SYPERVVeiflENLRRYLAGE---PLLNVVDKDR 311
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
91-328 2.42e-33

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: 127.70  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  91 DLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRttwLHQALRegtrvQSVEQIRE 170
Cdd:cd12155   54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKG---LKKAYK-----NQKEKKWK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 171 VASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIfydpylsdGMER----ALGLQRVSTLQDL---LFHSDCVTLHC 243
Cdd:cd12155  126 MDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTsgrdVEYFDKCYPLEELdevLKEADIVVNVL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 244 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAA 323
Cdd:cd12155  198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                 ....*
gi 697821559 324 WYSEQ 328
Cdd:cd12155  277 GVSEH 281
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
176-348 6.11e-32

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: 123.61  E-value: 6.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 176 ARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPylSDGMERALGLQRVSTLQDLLFHSDCVTLHCNLNEHNHHLIND 255
Cdd:cd12180  131 GSLAGSTLGIVGFGAIGQALARRALALGMRVLALRR--SGRPSDVPGVEAAADLAELFARSDHLVLAAPLTPETRHLINA 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 256 FTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAAWYSEQASIEMRE 335
Cdd:cd12180  209 DVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDGRRNLAD 287
                        170
                 ....*....|...
gi 697821559 336 EAAREIRRAITGR 348
Cdd:cd12180  288 RFLENLARYRAGQ 300
PLN02928 PLN02928
oxidoreductase family protein
87-354 1.93e-31

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 123.25  E-value: 1.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  87 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAasvEET--ADSTMCH----ILNLYRRttwlHQALRegt 160
Cdd:PLN02928  72 LDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPS---EGTgnAASCAEMaiylMLGLLRK----QNEMQ--- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 161 rvQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERALGLQRVST------------ 228
Cdd:PLN02928 142 --ISLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVddlvdekgghed 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 229 LQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQg 308
Cdd:PLN02928 220 IYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDD- 298
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 697821559 309 PLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLK 354
Cdd:PLN02928 299 PILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIE 344
PLN02306 PLN02306
hydroxypyruvate reductase
107-347 8.88e-31

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 122.27  E-value: 8.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 107 GFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgAARIRGETLGII 186
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 187 GLGRVGQAVA-LRAKAFGFSVIFYDPYLSDGME----------RALGLQ-----RVSTLQDLLFHSDCVTLHCNLNEHNH 250
Cdd:PLN02306 172 GAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEkfvtaygqflKANGEQpvtwkRASSMEEVLREADVISLHPVLDKTTY 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 251 HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFSQGPLKDAPNLICTPHAAWYSEQAS 330
Cdd:PLN02306 252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIASASKWTR 329
                        250
                 ....*....|....*..
gi 697821559 331 IEMREEAAREIRRAITG 347
Cdd:PLN02306 330 EGMATLAALNVLGKLKG 346
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
92-329 1.56e-28

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 114.63  E-value: 1.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  92 LEKFKALRIIVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWLHQalregtRVQSVEQIREV 171
Cdd:PRK12480  65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIER------RVQAHDFTWQA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 172 ASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERalgLQRVSTLQDLLFHSDCVTLHCNLNEHNHH 251
Cdd:PRK12480 138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 252 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFSQGPLKDA--------PNLICT 319
Cdd:PRK12480 215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayfTNDWTNKDIDDKtlleliehERILVT 294
                        250
                 ....*....|
gi 697821559 320 PHAAWYSEQA 329
Cdd:PRK12480 295 PHIAFFSDEA 304
PLN03139 PLN03139
formate dehydrogenase; Provisional
82-321 2.37e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 115.33  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  82 YHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRR--TTWlHQALREG 159
Cdd:PLN03139 106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNflPGY-HQVVSGE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 160 TRVQsveqirEVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDG-MERALGLQRVSTLQDLLFHSDC 238
Cdd:PLN03139 185 WNVA------GIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDV 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 239 VTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLIC 318
Cdd:PLN03139 259 VVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAM 337

                 ...
gi 697821559 319 TPH 321
Cdd:PLN03139 338 TPH 340
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
90-345 3.51e-24

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: 101.80  E-value: 3.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  90 EDLEKFKALRIIVRIGSGFDNIDiKSAGDLGIAVCNVpaasVEETADSTMC-----HILNLYRRTTwlhqALREGTRVQS 164
Cdd:cd12164   51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRL----VDPGLAQGMAeyvlaAVLRLHRDMD----RYAAQQRRGV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 165 VEQIREVASGAARIrgetlGIIGLGRVGQAVALRAKAFGFSVI--------------FYdpylsdGMERalglqrvstLQ 230
Cdd:cd12164  122 WKPLPQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVSgwsrspkdiegvtcFH------GEEG---------LD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 231 DLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPL 310
Cdd:cd12164  182 AFLAQTDILVCLLPLTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPL 260
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 697821559 311 KDAPNLICTPHAawyseqASIEMREEAAREIRRAI 345
Cdd:cd12164  261 WRHPRVTVTPHI------AAITDPDSAAAQVAENI 289
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
79-346 3.01e-22

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 97.80  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  79 ALMYHTIT-LTREDLEKFKaLRIIVRIGSGFDNIDIKSAGDLGIAVCNVP---AASVeetADSTMCHILNLyrrttwlhq 154
Cdd:PRK00257  40 VLLVRSVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPgcnARGV---VDYVLGSLLTL--------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 155 ALREGtrvqsveqirevasgaARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDgmerALGLQRVSTLQDLLF 234
Cdd:PRK00257 107 AEREG----------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQE----AEGDGDFVSLERILE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 235 HSDCVTLHCNLN-EHNH---HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsQGPL 310
Cdd:PRK00257 167 ECDVISLHTPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDL 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 697821559 311 KDAPN-LICTPHAAWYseqaSIEMREEAAREIRRAIT 346
Cdd:PRK00257 243 ELADLcTIATPHIAGY----SLDGKARGTAQIYQALC 275
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
120-323 1.14e-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: 240636  Cd Length: 303  Bit Score: 91.94  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 120 GIAVCNVPAASVEETADSTMCHILNLYRRttwLHQALREGTRVQSveqirEVASGAARIRGETLGIIGLGRVGQAVALRA 199
Cdd:cd12159   73 GRRWTNAAGAYAETVAEHALALLLAGLRQ---LPARARATTWDPA-----EEDDLVTLLRGSTVAIVGAGGIGRALIPLL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 200 KAFGFSVIFYD--PYLSDGMERALglqRVSTLQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVD 277
Cdd:cd12159  145 APFGAKVIAVNrsGRPVEGADETV---PADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVD 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 697821559 278 EKALAQALKEGRIRGAALDVHESEPfsFSQG-PLKDAPNLICTPHAA 323
Cdd:cd12159  222 TDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
88-353 2.23e-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: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 91.11  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  88 TREDLEKFKALRIIVRIGSGFDNIDikSAGDLGIAVCN---VPAASveeTADSTMCHILNLYRRttwLHQALREGTRVQ- 163
Cdd:cd12166   51 VLEALRALPRLRVVQTLSAGYDGVL--PLLPEGVTLCNargVHDAS---TAELAVALILASLRG---LPRFVRAQARGRw 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 164 SVEQIREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFSVIfydpylsdgmeralglqRVST-------------LQ 230
Cdd:cd12166  123 EPRRTPSLA-------DRRVLIVGYGSIGRAIERRLAPFEVRVT-----------------RVARtarpgeqvhgideLP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 231 DLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHESEPfsFSQG-P 309
Cdd:cd12166  179 ALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEP--LPPGhP 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 697821559 310 LKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSL 353
Cdd:cd12166  256 LWSAPGVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
135-348 7.76e-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: 240637  Cd Length: 310  Bit Score: 89.74  E-value: 7.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 135 ADSTMCHILNLYRRTTWLHQALREGTRVQSV--EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIfydPY 212
Cdd:cd12160   96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT---GV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 213 LSDGMERAlGLQRVST--LQDLLFHSDCVTLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRI 290
Cdd:cd12160  173 ARSAGERA-GFPVVAEdeLPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRL 251
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 697821559 291 RGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMreeAAREIRRAITGR 348
Cdd:cd12160  252 GGAALDVTATEPLPASS-PLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
179-327 2.33e-17

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 82.71  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 179 RGETLGIIGLGRVGQAVALRAKAFGFSVIFY-------------DPYLSDGMERALGLQRVS--------TLQDLL-FHS 236
Cdd:cd12163  132 VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkdDGYIVPGTGDPDGSIPSAwfsgtdkaSLHEFLrQDL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 237 DCVTLHCNLNEHNHHLIN--DFTIKQMRqGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAP 314
Cdd:cd12163  212 DLLVVSLPLTPATKHLLGaeEFEILAKR-KTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAP 289
                        170
                 ....*....|...
gi 697821559 315 NLICTPHAAWYSE 327
Cdd:cd12163  290 NVIITPHVSWQTQ 302
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
79-326 1.24e-14

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 74.94  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  79 ALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTMCHILNLYRRTTWlhqALRE 158
Cdd:PRK15438  40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 159 gtrvqsveqirevasgaarirgETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSDGMERAlglqRVSTLQDLLFHSDC 238
Cdd:PRK15438 117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEG----DFRSLDELVQEADI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 239 VTLHCNLNEHNH----HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGPLKDAP 314
Cdd:PRK15438 171 LTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKVD 249
                        250
                 ....*....|..
gi 697821559 315 nlICTPHAAWYS 326
Cdd:PRK15438 250 --IGTPHIAGYT 259
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
63-343 4.54e-14

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: 72.33  E-value: 4.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  63 QSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFD----NIDIKSAGDLGIAVCNVPA---ASVEETA 135
Cdd:cd12170   35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 136 DSTMCHILNLYRRTTWLHQALRegtrvqsveqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYDPYLSD 215
Cdd:cd12170  114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 216 GMERALGlqRVSTLQDLLFHSDCVTLHCNlneHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGrirGAAL 295
Cdd:cd12170  174 DAEAKGI--RYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 697821559 296 DVHESEPfSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 343
Cdd:cd12170  246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQAFERLSQKVLANLEE 292
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
96-360 3.92e-13

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 69.91  E-value: 3.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  96 KALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAAS--VEETADSTMchiLNLYRRTTWLHQALREGTRVQSVEQIrevas 173
Cdd:PRK06436  48 KKTKMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSisVAEHAFALL---LAWAKNICENNYNMKNGNFKQSPTKL----- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 174 gaarIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYD-PYLSDGMERAlglqrVSTLQDLLFHSDCVTLHCNLNEHNHHL 252
Cdd:PRK06436 120 ----LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTrSYVNDGISSI-----YMEPEDIMKKSDFVLISLPLTDETRGM 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 253 INDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPlkdaPNLICTPH-AAWYSEQASI 331
Cdd:PRK06436 191 INSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHvAGGMSGEIMQ 266
                        250       260
                 ....*....|....*....|....*....
gi 697821559 332 EMREEAAREIRRAITGRiPdslKNCVNKD 360
Cdd:PRK06436 267 PAVALAFENIKNFFEGK-P---KNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
91-316 6.98e-11

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: 63.02  E-value: 6.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  91 DLEKFKALRIIVRIGSGFDNIDIKSAgdLGIAvcNVPAASVEETADSTMCHILNLYRRttwlhQALREGTRVQSVeQIRE 170
Cdd:cd12154   81 ALIQKLGDRLLFTYTIGADHRDLTEA--LARA--GLTAIAVEGVELPLLTSNSIGAGE-----LSVQFIARFLEV-QQPG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 171 VASGAARIRGETLGIIGLGRVGQAVALRAKAFGFSVIFYD-PYLSDGMERALGLQRVSTLQDLLFHSDCVTLHCNLNEHN 249
Cdd:cd12154  151 RLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDiNVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGKR 230
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697821559 250 HHLINDFT-IKQMRQGAFLVNTARG-GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNL 316
Cdd:cd12154  231 AGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
96-346 3.11e-10

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 60.97  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559  96 KALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETA------DSTMCHILNLYRRTTwLHQALREGTRVQSVEQIR 169
Cdd:PRK15469  55 RDLKAVFALGAGVDSILSKLQAHPEMLDPSVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPEYH 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 170 evasgaariRGE-TLGIIGLGRVGQAVALRAKAFGFSVIFYdpylSDGMERALGLQRVSTLQDL-LFHSDCVTLhCNLNE 247
Cdd:PRK15469 134 ---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCW----SRSRKSWPGVQSFAGREELsAFLSQTRVL-INLLP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697821559 248 HNHH---LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAaw 324
Cdd:PRK15469 200 NTPEtvgIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHV-- 276
                        250       260
                 ....*....|....*....|..
gi 697821559 325 yseqASIEMREEAAREIRRAIT 346
Cdd:PRK15469 277 ----AAVTRPAEAVEYISRTIA 294
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
183-233 3.40e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 39.35  E-value: 3.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 697821559 183 LGIIGLGRVGQAVALRAKAFGFSVIFYD--PYLSDGMERAlGLQRVSTLQDLL 233
Cdd:PRK09599   3 LGMIGLGRMGGNMARRLLRGGHEVVGYDrnPEAVEALAEE-GATGADSLEELV 54
 
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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