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Conserved domains on  [gi|4557497|ref|NP_001319|]
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C-terminal-binding protein 1 isoform 1 [Homo sapiens]

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 ...
28-346 7.90e-145

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: 415.37  E-value: 7.90e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299   1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  104 NIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299  78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  184 RVGQAVALRAKAFGFNVLFYDPYLSDGVERALGlQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVN 263
Cdd:cd05299 152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGG-VRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  264 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299 231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                ...
gi 4557497  344 PDS 346
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 ...
28-346 7.90e-145

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: 415.37  E-value: 7.90e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299   1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  104 NIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299  78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  184 RVGQAVALRAKAFGFNVLFYDPYLSDGVERALGlQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVN 263
Cdd:cd05299 152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGG-VRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  264 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299 231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                ...
gi 4557497  344 PDS 346
Cdd:cd05299 310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 9.81e-97

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: 292.76  E-value: 9.81e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDI 107
Cdd:COG1052   3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  108 KSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 187
Cdd:COG1052  83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  188 AVALRAKAFGFNVLFYDPYLSDGVErALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARG 267
Cdd:COG1052 157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  268 GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 347
Cdd:COG1052 235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                ....*.
gi 4557497  348 KNCVNK 353
Cdd:COG1052 311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 9.90e-82

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: 254.14  E-value: 9.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497     30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    109 SAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    189 VALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLF---HSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    266 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 4557497    346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
80-352 1.38e-68

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: 226.82  E-value: 1.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497     80 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtrvqsv 159
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    160 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDgvERA--LGLQRVSTLQDLLFHSDCVTLHC 237
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    238 GLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAA 317
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 4557497    318 WYSEQASIEMREEAAREIRRAITGripDSLKNCVN 352
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVN 311
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 2.90e-58

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 193.66  E-value: 2.90e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    30 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLTREDLEKFKALRIIVRIGSGFDNID 106
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   107 IKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSvEQIREVASGAARIRGETLGIIGLGRVG 186
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   187 QAVALRAKAFGFNVLFYDPylsDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTAR 266
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557497   267 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfSQGPL---KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
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 ...
28-346 7.90e-145

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: 415.37  E-value: 7.90e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299   1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  104 NIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299  78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  184 RVGQAVALRAKAFGFNVLFYDPYLSDGVERALGlQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVN 263
Cdd:cd05299 152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGG-VRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  264 TARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299 231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                ...
gi 4557497  344 PDS 346
Cdd:cd05299 310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
30-337 1.88e-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: 1.88e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   30 VALLDGRDCTVEMPILKD-VATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:cd05198   2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  109 SAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRvqsveqIREVASGAARIRGETLGIIGLGRVGQA 188
Cdd:cd05198  81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  189 VALRAKAFGFNVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGG 268
Cdd:cd05198 155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVVS-LDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557497  269 LVDEKALAQALKEGRIRGAALDVHESEPFSFSqGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 337
Cdd:cd05198 234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 9.81e-97

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: 292.76  E-value: 9.81e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDI 107
Cdd:COG1052   3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  108 KSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 187
Cdd:COG1052  83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  188 AVALRAKAFGFNVLFYDPYLSDGVErALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARG 267
Cdd:COG1052 157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  268 GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 347
Cdd:COG1052 235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                ....*.
gi 4557497  348 KNCVNK 353
Cdd:COG1052 311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
49-352 9.05e-93

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: 282.85  E-value: 9.05e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   49 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEET 128
Cdd:COG0111  23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  129 ADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLS 208
Cdd:COG0111 102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  209 DGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAA 288
Cdd:COG0111 175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557497  289 LDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRipdSLKNCVN 352
Cdd:COG0111 255 LDVFEPEPLPADS-PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
58-338 4.55e-86

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


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 265.12  E-value: 4.55e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   58 STQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHIL 137
Cdd:cd12172  37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  138 NLYRRATWLHQALREG--TRVQSVEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERAL 215
Cdd:cd12172 115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  216 GLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE 295
Cdd:cd12172 184 GVEFVS-LEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 4557497  296 PFSfSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 338
Cdd:cd12172 263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
82-342 1.36e-85

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: 263.89  E-value: 1.36e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   82 TREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGT----RVQ 157
Cdd:cd12173  53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  158 SVEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGlQRVSTLQDLLFHSDCVTLHC 237
Cdd:cd12173 133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISLHT 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  238 GLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAA 317
Cdd:cd12173 201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                       250       260
                ....*....|....*....|....*
gi 4557497  318 WYSEQASIEMREEAAREIRRAITGR 342
Cdd:cd12173 280 ASTEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 9.90e-82

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: 254.14  E-value: 9.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497     30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    109 SAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    189 VALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLF---HSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    266 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 4557497    346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
82-352 1.99e-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: 245.99  E-value: 1.99e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   82 TREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRatwlhqaLREGTRvqsveQ 161
Cdd:cd12178  56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR-------IAEGDR-----L 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  162 IRE-VASGAAR-------IRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALGLQRVStLQDLLFHSDC 232
Cdd:cd12178 124 MRRgGFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD-LDELLKESDF 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  233 VTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGpLKDAPNLIC 312
Cdd:cd12178 203 VSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVIL 280
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4557497  313 TPHAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVN 352
Cdd:cd12178 281 TPHIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
78-344 2.12e-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: 240.55  E-value: 2.12e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   78 TITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtrvq 157
Cdd:cd12175  52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  158 svEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALGLQRVStLQDLLFHSDCVTLH 236
Cdd:cd12175 128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYVE-LDELLAESDVVSLH 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  237 CGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHA 316
Cdd:cd12175 205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDD-PLLRLDNVILTPHI 283
                       250       260
                ....*....|....*....|....*...
gi 4557497  317 AWYSEQASIEMREEAAREIRRAITGRIP 344
Cdd:cd12175 284 AGVTDESYQRMAAIVAENIARLLRGEPP 311
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
92-341 6.62e-73

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: 232.05  E-value: 6.62e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   92 LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEqirevASGAAR 171
Cdd:cd12168  77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  172 IRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALGLqRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDF 250
Cdd:cd12168 152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALAT-YYVSLDELLAQSDVVSLNCPLTAATRHLINKK 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  251 TVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFsFSQGpLKDAPNLICTPHAAWYSEQASIEMREE 330
Cdd:cd12168 231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPE-VNPG-LLKMPNVTLLPHMGTLTVETQEKMEEL 308
                       250
                ....*....|.
gi 4557497  331 AAREIRRAITG 341
Cdd:cd12168 309 VLENIEAFLET 319
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
81-329 1.24e-72

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: 230.80  E-value: 1.24e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   81 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVE 160
Cdd:cd12162  55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  161 Q------IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVeralGLQRVStLQDLLFHSDCVT 234
Cdd:cd12162 135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYVS-LDELLAQSDVIS 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  235 LHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsqgP------LKDAP 308
Cdd:cd12162 203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplLKAAP 276
                       250       260
                ....*....|....*....|.
gi 4557497  309 NLICTPHAAWyseqASIEMRE 329
Cdd:cd12162 277 NLIITPHIAW----ASREARQ 293
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
42-341 1.02e-70

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: 225.74  E-value: 1.02e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   42 MPILKDVATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVC 118
Cdd:cd05301  14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  119 NVPAASVEETADSTLCHILNLYRRATWLHQALREGtrvqSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGF 198
Cdd:cd05301  93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAG----EWKGWSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  199 NVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQA 278
Cdd:cd05301 169 KILYHNRSRKPEAEEELGARYVS-LDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEA 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557497  279 LKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd05301 248 LKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
30-342 1.20e-69

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: 223.72  E-value: 1.20e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   30 VALLDGRDctVEMPILKDVA-----TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDN 104
Cdd:cd01619   3 VLIYDYRD--DELEIEKEILkaggvDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  105 IDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRatwlhqalREGTRVQSVEQIREVAS-GAARIRGETLGIIGLG 183
Cdd:cd01619  81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRN--------RKYIDERDKNQDLQDAGvIGRELEDQTVGVVGTG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  184 RVGQAVALRAKAFGFNVLFYDPYLSDGVErALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVN 263
Cdd:cd01619 153 KIGRAVAQRAKGFGMKVIAYDPFRNPELE-DKGVKYVS-LEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIIN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  264 TARGGLVDEKALAQALKEGRIRGAALDVHESE-----------PFSFSQGP-LKDAPNLICTPHAAWYSEQASIEMREEA 331
Cdd:cd01619 231 TARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEIS 310
                       330
                ....*....|.
gi 4557497  332 AREIRRAITGR 342
Cdd:cd01619 311 CENIVDFLEGE 321
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
80-352 1.38e-68

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: 226.82  E-value: 1.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497     80 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtrvqsv 159
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    160 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDgvERA--LGLQRVSTLQDLLFHSDCVTLHC 237
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    238 GLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSqgPLKDAPNLICTPHAA 317
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 4557497    318 WYSEQASIEMREEAAREIRRAITGripDSLKNCVN 352
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVN 311
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
80-315 1.89e-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: 217.02  E-value: 1.89e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtrvqsv 159
Cdd:cd05303  52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  160 eQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGL 239
Cdd:cd05303 126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTVS-LEELLKNSDFISLHVPL 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557497  240 NEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgpLKDAPNLICTPH 315
Cdd:cd05303 204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
133-317 2.68e-66

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: 209.66  E-value: 2.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    133 LCHILNLYRRATWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGV 211
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    212 ERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 4557497    292 HESEPFSFSQgPLKDAPNLICTPHAA 317
Cdd:pfam02826 154 FEPEPLPADH-PLLDLPNVILTPHIA 178
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
31-349 8.41e-65

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: 211.03  E-value: 8.41e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   31 ALLDGRDCTVEMPILKDVATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLTREDLEKFKALRIIVRIGSGFDN 104
Cdd:cd12177   7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  105 IDIKSAGDLGIAVCNVPAA----SVEETAdstLCHILNLYRRATWLHQALREGtrvqsveQIREVASGAAR-IRGETLGI 179
Cdd:cd12177  83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  180 IGLGRVGQAVA-LRAKAFGFNVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQG 258
Cdd:cd12177 153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPVS-LEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  259 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 338
Cdd:cd12177 232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADH-PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                       330
                ....*....|.
gi 4557497  339 ITGRIPDSLKN 349
Cdd:cd12177 311 LAGKEPKGILN 321
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
83-352 3.29e-64

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: 208.95  E-value: 3.29e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   83 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRatwLHQALREGTRVQSVEQI 162
Cdd:cd12174  42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRN---IIQAIKWVTNGDGDDIS 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  163 REVASGAAR-----IRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSdgVERALGL----QRVSTLQDLLFHSDCV 233
Cdd:cd12174 119 KGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLS--VEAAWKLsvevQRVTSLEELLATADYI 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  234 TLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEpfsfsqgPLKDAPNLICT 313
Cdd:cd12174 197 TLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIAT 269
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4557497  314 PHAAWYSEQASIEMREEAAREIRRAI-TGRIPdslkNCVN 352
Cdd:cd12174 270 PHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-337 4.45e-64

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: 208.55  E-value: 4.45e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   61 EIHEKVLNEAVGA--LMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILN 138
Cdd:cd12171  35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  139 LYRRATWLHQALREGtrvqsveQIREVASGAAR----IRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERA 214
Cdd:cd12171 115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEA 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  215 LGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHES 294
Cdd:cd12171 188 DGVKKVS-LEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 4557497  295 EPFSfSQGPLKDAPNLICTPHAAWYSEQA---SIEMreeAAREIRR 337
Cdd:cd12171 267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
58-341 1.59e-58

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: 194.68  E-value: 1.59e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   58 STQEIHEKVLNEAVGA---LMYHTITLTREDLEKFKAL---RIIVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADS 131
Cdd:cd12186  30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEYgikQIALRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  132 TLCHILNLYRRATWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDG 210
Cdd:cd12186 109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  211 VErALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALD 290
Cdd:cd12186 182 LE-KFLLYYDS-LEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557497  291 VHESE----PFSFSQGPLKDA--------PNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12186 260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEG 322
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 2.90e-58

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 193.66  E-value: 2.90e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    30 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLTREDLEKFKALRIIVRIGSGFDNID 106
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   107 IKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSvEQIREVASGAARIRGETLGIIGLGRVG 186
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   187 QAVALRAKAFGFNVLFYDPylsDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTAR 266
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557497   267 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfSQGPL---KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:PRK08410 234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
81-342 4.80e-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: 193.65  E-value: 4.80e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   81 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVE 160
Cdd:cd12187  53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  161 QIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGLN 240
Cdd:cd12187 133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYVS-LEELLQESDIISLHVPYT 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  241 EHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPF----------SFSQGPLKDA--- 307
Cdd:cd12187 205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVlreeaelfreDVSPEDLKKLlad 284
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 4557497  308 ------PNLICTPHAAWYSEQASIEMREEAAREIRRAITGR 342
Cdd:cd12187 285 hallrkPNVIITPHVAYNTKEALERILDTTVENIKAFAAGQ 325
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-349 2.84e-57

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 191.55  E-value: 2.84e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    60 QEIHEKVLNEAV---GALMyhTITLTREDLEKFKA---LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTL 133
Cdd:PRK13243  32 REIPREVLLEKVrdvDALV--TMLSERIDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAW 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   134 CHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVER 213
Cdd:PRK13243 110 ALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEK 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   214 ALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHE 293
Cdd:PRK13243 190 ELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFE 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557497   294 SEPfsFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKN 349
Cdd:PRK13243 269 EEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTLVN 322
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
73-332 2.07e-55

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: 186.27  E-value: 2.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   73 ALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALRE 152
Cdd:cd12161  51 IVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  153 GTRVQSVEQiREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVErALGLQRVStLQDLLFHSDC 232
Cdd:cd12161 131 GGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK-ALGIEYVS-LDELLAESDI 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  233 VTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLIC 312
Cdd:cd12161 201 VSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTIL 280
                       250       260
                ....*....|....*....|
gi 4557497  313 TPHAAWYSEQAsIEMREEAA 332
Cdd:cd12161 281 TPHVAFATEEA-MEKRAEIV 299
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
43-341 5.98e-55

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: 184.64  E-value: 5.98e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   43 PILKDVATV-AFCD-AQSTQEIHEKVLN-EAVGALMYHTiTLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCN 119
Cdd:cd12169  19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  120 VPAaSVEETADSTLCHILNLYRRATWLHQALREGTRVQSVeqirevasgAARIRGETLGIIGLGRVGQAVALRAKAFGFN 199
Cdd:cd12169  98 TGG-GPTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  200 VLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQAL 279
Cdd:cd12169 168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557497  280 KEGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12169 248 RAGRIAGAALDVFDVEPLPADH-PLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
80-323 1.63e-54

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: 184.18  E-value: 1.63e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKAL--RIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRatwLHQAlregtrvq 157
Cdd:cd12183  55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRK---IHRA-------- 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  158 sveqirevasgAARIR---------------GETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVErALGLQRVSt 222
Cdd:cd12183 124 -----------YNRVRegnfsldgllgfdlhGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELA-KLGVEYVD- 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  223 LQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSF--- 299
Cdd:cd12183 191 LDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFfed 270
                       250       260       270
                ....*....|....*....|....*....|...
gi 4557497  300 -SQGPLKDA--------PNLICTPHAAWYSEQA 323
Cdd:cd12183 271 hSDEIIQDDvlarllsfPNVLITGHQAFFTKEA 303
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
55-342 2.77e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 183.36  E-value: 2.77e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    55 DAQSTQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLC 134
Cdd:PRK06487  32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   135 HILNLYRRATWLHQALREGtRVQSVEQ-------IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFNVLfydpyL 207
Cdd:PRK06487 110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   208 SDGVERALGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGA 287
Cdd:PRK06487 177 GQLPGRPARPDRLP-LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557497   288 ALDVHESEPfSFSQGPL--KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGR 342
Cdd:PRK06487 256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
51-336 1.11e-50

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: 173.93  E-value: 1.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   51 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLTREDLEKFKAL-------RIIvrigsGFDNIDIKSAGDLGIAVCNVPA 122
Cdd:cd12185  27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVTY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  123 aSVEETADSTLCHILNLYRRATW-LHQALREGTRVQSVeQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVL 201
Cdd:cd12185 100 -SPNSVADYTVMLMLMALRKYKQiMKRAEVNDYSLGGL-QGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCKIL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  202 FYDPYLSDGVERalGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKE 281
Cdd:cd12185 171 AYDPYPNEEVKK--YAEYVD-LDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLES 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557497  282 GRIRGAALDVHESEPFSFSQ------------GPLKDAPNLICTPHAAWYSEQASIEMREEAAREIR 336
Cdd:cd12185 248 GKIGGAALDVIEGEDGIYYNdrkgdilsnrelAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLV 314
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
80-360 2.14e-48

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: 168.12  E-value: 2.14e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQsv 159
Cdd:cd12167  61 PLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG-- 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  160 eqiREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVStLQDLLFHSDCVTLHCGL 239
Cdd:cd12167 139 ---WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVS-LDELLARSDVVSLHAPL 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  240 NEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHESEPFSFSQgPLKDAPNLICTPHAAWY 319
Cdd:cd12167 215 TPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLPPDS-PLRTLPNVLLTPHIAGS 292
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 4557497  320 SEQASIEMREEAAREIRRAITGRIPdslKNCVNKDHLTAAT 360
Cdd:cd12167 293 TGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
76-315 2.16e-48

NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of a formate anion to carbon dioxide coupled with the reduction of NAD+ to NADH. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family have 2 highly similar subdomains of the alpha/beta form, with NAD binding occurring in the cleft between subdomains. NAD contacts are primarily to the Rossmann-fold NAD-binding domain which is inserted within the linear sequence of the more diverse flavodoxin-like catalytic subdomain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production from C1 compounds such as methanol, and in the stress responses of plants. NAD-dependent FDH is useful in cofactor regeneration in asymmetrical biocatalytic reduction processes, where FDH irreversibly oxidizes formate to carbon dioxide, while reducing the oxidized form of the cofactor to the reduced form.


Pssm-ID: 240627  Cd Length: 348  Bit Score: 168.66  E-value: 2.16e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   76 YHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTR 155
Cdd:cd05302  69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  156 vqsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALGLQRVSTLQDLLFHSDCVT 234
Cdd:cd05302 149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  235 LHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGPLKDAPNLICTP 314
Cdd:cd05302 224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302

                .
gi 4557497  315 H 315
Cdd:cd05302 303 H 303
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
81-335 1.19e-47

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 165.74  E-value: 1.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    81 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNL-YRRATWLHQALreGTRVQSV 159
Cdd:PRK06932  55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALkHSLMGWYRDQL--SDRWATC 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   160 EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDpylsdgvERALGLQRVSTL--QDLLFHSDCVTLHC 237
Cdd:PRK06932 133 KQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREGYTpfEEVLKQADIVTLHC 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   238 GLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPL----KDAPNLICT 313
Cdd:PRK06932 206 PLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLPNLLIT 284
                        250       260
                 ....*....|....*....|..
gi 4557497   314 PHAAWYSEQASIEMREEAAREI 335
Cdd:PRK06932 285 PHIAWASDSAVTTLVNKVAQNI 306
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
80-337 4.57e-46

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: 161.21  E-value: 4.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKALriiVRIGS---GFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtrv 156
Cdd:cd12176  53 QLTEEVLEAAPKL---LAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG--- 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  157 qsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDpylsdgVERALGL---QRVSTLQDLLFHSDCV 233
Cdd:cd12176 127 ----IWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD------IAEKLPLgnaRQVSSLEELLAEADFV 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  234 TLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFS----FSQgPLKDAPN 309
Cdd:cd12176 197 TLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngepFSS-PLQGLPN 275
                       250       260
                ....*....|....*....|....*...
gi 4557497  310 LICTPHAAWYSEQASIEMREEAAREIRR 337
Cdd:cd12176 276 VILTPHIGGSTEEAQENIGLEVAGKLVK 303
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
58-341 7.78e-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: 161.30  E-value: 7.78e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   58 STQEIHEKVLNeAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHIL 137
Cdd:cd12157  34 SREELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLI 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  138 NLYRRATWLHQALREGTRvqsvEQIREVASGAArIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALG 216
Cdd:cd12157 113 GLGRHILAGDRFVRSGKF----GGWRPKFYGTG-LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHpLDQAEEQALN 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  217 LQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE- 295
Cdd:cd12157 188 LRRVE-LDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEMEd 266
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4557497  296 ------PFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12157 267 warpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
69-329 3.34e-45

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: 158.79  E-value: 3.34e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   69 EAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQ 148
Cdd:cd12156  42 RIRAVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADR 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  149 ALREGtrvqsvEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVeralGLQRVSTLQDLLF 228
Cdd:cd12156 122 FVRAG------RWPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDV----PYRYYASLLELAA 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  229 HSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsQGP--LKD 306
Cdd:cd12156 192 ESDVLVVACPGGPATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLD 267
                       250       260
                ....*....|....*....|...
gi 4557497  307 APNLICTPHAAWYSEQASIEMRE 329
Cdd:cd12156 268 LDNVVLTPHIASATVETRRAMGD 290
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
81-335 4.21e-44

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 158.30  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    81 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRvqsve 160
Cdd:PRK07574 104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   161 QIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPY-LSDGVERALGLQRVSTLQDLLFHSDCVTLHCGL 239
Cdd:PRK07574 179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   240 NEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHesepfsFSQGPLKD-----APNLICTP 314
Cdd:PRK07574 259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVW------FPQPAPADhpwrtMPRNGMTP 332
                        250       260
                 ....*....|....*....|...
gi 4557497   315 HAAW--YSEQASIemrEEAAREI 335
Cdd:PRK07574 333 HISGttLSAQARY---AAGTREI 352
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
83-321 3.96e-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: 153.60  E-value: 3.96e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   83 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLyrratwLHQALREGTRVQSVEQI 162
Cdd:cd12179  54 KEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLAL------FNKLNRADQEVRNGIWD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  163 REVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERAlglQRVStLQDLLFHSDCVTLHCGLNEH 242
Cdd:cd12179 128 REGNRGV-ELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAYA---EQVS-LETLFKEADILSLHIPLTPE 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  243 NHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSF---SQGP-----LKDAPNLICTP 314
Cdd:cd12179 203 TRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFesiFNQPeafeyLIKSPKVILTP 282

                ....*...
gi 4557497  315 H-AAWYSE 321
Cdd:cd12179 283 HiAGWTFE 290
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
80-329 1.18e-42

(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: 153.22  E-value: 1.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKALRI---IVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRR-ATWLHQALREGTR 155
Cdd:cd12184  55 FADKENLEIYKEYGIkyvFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHtAYTASRTANKNFK 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  156 VQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQrvsTLQDLLFHSDCVTL 235
Cdd:cd12184 134 VDPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVVTFV---SLDELLKKSDIISL 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  236 HCG-LNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--HESEPF--SFSQGPLKDA--- 307
Cdd:cd12184 204 HVPyIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvve 283
                       250       260
                ....*....|....*....|....*...
gi 4557497  308 ------PNLICTPHAAWYSEQASIEMRE 329
Cdd:cd12184 284 klldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
81-315 1.08e-39

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 146.86  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    81 LTREDLEKFKALriiVRIGS---GFDNIDIKSAGDLGIAVCNVPAA---SVEETAdstLCHILNLYRRATWLHQALREGT 154
Cdd:PRK11790  65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSntrSVAELV---IGEIILLLRGIPEKNAKAHRGG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   155 RVQSveqirevASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDpylsdgVERALGL---QRVSTLQDLLFHSD 231
Cdd:PRK11790 139 WNKS-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDKLPLgnaRQVGSLEELLAQSD 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   232 CVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQG---PLKDAP 308
Cdd:PRK11790 206 VVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLD 285

                 ....*..
gi 4557497   309 NLICTPH 315
Cdd:PRK11790 286 NVILTPH 292
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
64-345 1.99e-39

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: 143.92  E-value: 1.99e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   64 EKVLNEAvGALMYHTITLtREDLEKFKALRIIVRIGSGFDNIDIKSAGDlGIAVCNVPAASvEETADSTLCHILNLYRRA 143
Cdd:cd12165  35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHGNS-PAVAEHALALILALAKRI 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  144 TWLHQALREGTRVQSVEQIREVASgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYD--PYLSDGVERALGlqrVS 221
Cdd:cd12165 111 VEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGT---LS 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  222 TLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--------HE 293
Cdd:cd12165 184 DLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDP 263
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4557497  294 SEPFSFsqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD 345
Cdd:cd12165 264 VAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
92-323 1.44e-38

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 142.19  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    92 LRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREgtrvqsvEQIREVASGAAR 171
Cdd:PRK08605  70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVRE-------HDFRWEPPILSR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   172 -IRGETLGIIGLGRVGQAVA-LRAKAFGFNVLFYDPYLSDGVerALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLIND 249
Cdd:PRK08605 143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKA--ATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   250 FTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFSQGPLKDA--------PNLICTPHAA 317
Cdd:PRK08605 221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                 ....*.
gi 4557497   318 WYSEQA 323
Cdd:PRK08605 301 FYTDAA 306
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
59-352 2.61e-37

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 138.35  E-value: 2.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    59 TQEIHEKVLNEAVGaLMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILN 138
Cdd:PRK15409  35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   139 LYRRATWLHQalregtRVQSVEQIREVASG--AARIRGETLGIIGLGRVGQAVALRAKaFGFN--VLFYDPYLSDGVERA 214
Cdd:PRK15409 114 TARRVVEVAE------RVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNmpILYNARRHHKEAEER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   215 LGLQRVStLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHES 294
Cdd:PRK15409 187 FNARYCD-LDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557497   295 EPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVN 352
Cdd:PRK15409 266 EPLSVDS-PLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVN 319
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
80-320 8.72e-37

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: 137.66  E-value: 8.72e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   80 TLTREDLEKFKALriIVR-----------------IGS---GFDNIDIKSAGDLGIAVCNVP---AASVeetADSTLCHI 136
Cdd:cd12158  28 EITAEDLKDADVL--LVRsvtkvneallegskvkfVGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSAL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  137 LNLYRRATWLhqalregtrvqsveqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLsdgvERALG 216
Cdd:cd12158 103 LVLAQRQGFS-------------------------LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPR----AEAEG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  217 LQRVSTLQDLLFHSDCVTLHCGLNEH----NHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVH 292
Cdd:cd12158 154 DPGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233
                       250       260
                ....*....|....*....|....*...
gi 4557497  293 ESEPfSFSQGPLKDApnLICTPHAAWYS 320
Cdd:cd12158 234 ENEP-EIDLELLDKV--DIATPHIAGYS 258
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
83-355 2.26e-34

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: 130.33  E-value: 2.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   83 REDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGtRVQSVEQI 162
Cdd:cd05300  51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAER-RWQRRGPV 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  163 REvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLfydpylsdGVER-----ALGLQRVST---LQDLLFHSDCVT 234
Cdd:cd05300 130 RE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRsgrpaPPVVDEVYTpdeLDELLPEADYVV 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  235 LHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTP 314
Cdd:cd05300 195 NALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVIITP 273
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4557497  315 HAAWYSEqasiEMREEAA----REIRRAITGRipdSLKNCVNKDH 355
Cdd:cd05300 274 HISGDSP----SYPERVVeiflENLRRYLAGE---PLLNVVDKDR 311
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
85-322 4.71e-34

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: 129.62  E-value: 4.71e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   85 DLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRatwLHQALRegtrvQSVEQIRE 164
Cdd:cd12155  54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKG---LKKAYK-----NQKEKKWK 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  165 VASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLfydpylsdGVER----ALGLQRVSTLQDL---LFHSDCVTLHC 237
Cdd:cd12155 126 MDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTsgrdVEYFDKCYPLEELdevLKEADIVVNVL 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  238 GLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAA 317
Cdd:cd12155 198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                ....*
gi 4557497  318 WYSEQ 322
Cdd:cd12155 277 GVSEH 281
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
170-342 1.71e-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: 125.15  E-value: 1.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  170 ARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYD----PYLSDGVERAlglqrvSTLQDLLFHSDCVTLHCGLNEHNHH 245
Cdd:cd12180 131 GSLAGSTLGIVGFGAIGQALARRALALGMRVLALRrsgrPSDVPGVEAA------ADLAELFARSDHLVLAAPLTPETRH 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  246 LINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAAWYSEQASI 325
Cdd:cd12180 205 LINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDGRR 283
                       170
                ....*....|....*..
gi 4557497  326 EMREEAAREIRRAITGR 342
Cdd:cd12180 284 NLADRFLENLARYRAGQ 300
PLN02928 PLN02928
oxidoreductase family protein
81-348 4.01e-30

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 119.40  E-value: 4.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    81 LTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAA---SVEETADSTLCHILNLYRRatwlHQALRegtrvQ 157
Cdd:PLN02928  72 LDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRK----QNEMQ-----I 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   158 SVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVST------------LQD 225
Cdd:PLN02928 143 SLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVddlvdekgghedIYE 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   226 LLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQgPLK 305
Cdd:PLN02928 223 FAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDD-PIL 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 4557497   306 DAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLK 348
Cdd:PLN02928 302 KHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIE 344
PLN02306 PLN02306
hydroxypyruvate reductase
101-341 7.93e-30

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 119.58  E-value: 7.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   101 GFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREvasgAARIRGETLGII 180
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   181 GLGRVGQAVA-LRAKAFGFNVLFYDPYLSDGVE----------RALGLQ-----RVSTLQDLLFHSDCVTLHCGLNEHNH 244
Cdd:PLN02306 172 GAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEkfvtaygqflKANGEQpvtwkRASSMEEVLREADVISLHPVLDKTTY 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   245 HLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFSQGPLKDAPNLICTPHAAWYSEQAS 324
Cdd:PLN02306 252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIASASKWTR 329
                        250
                 ....*....|....*..
gi 4557497   325 IEMREEAAREIRRAITG 341
Cdd:PLN02306 330 EGMATLAALNVLGKLKG 346
PLN03139 PLN03139
formate dehydrogenase; Provisional
76-315 9.44e-30

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 119.18  E-value: 9.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    76 YHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRR-ATWLHQALREGT 154
Cdd:PLN03139 106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNfLPGYHQVVSGEW 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   155 RVQsveqirEVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDG-VERALGLQRVSTLQDLLFHSDCV 233
Cdd:PLN03139 186 NVA------GIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVV 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   234 TLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICT 313
Cdd:PLN03139 260 VINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMT 338

                 ..
gi 4557497   314 PH 315
Cdd:PLN03139 339 PH 340
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
86-323 5.82e-28

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 113.08  E-value: 5.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    86 LEKFKALRIIVRIgSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQalregtRVQSVEQIREV 165
Cdd:PRK12480  65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIER------RVQAHDFTWQA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   166 ASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERalgLQRVSTLQDLLFHSDCVTLHCGLNEHNHH 245
Cdd:PRK12480 138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   246 LINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFSQGPLKDA--------PNLICT 313
Cdd:PRK12480 215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayfTNDWTNKDIDDKtlleliehERILVT 294
                        250
                 ....*....|
gi 4557497   314 PHAAWYSEQA 323
Cdd:PRK12480 295 PHIAFFSDEA 304
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
84-339 1.10e-23

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: 100.65  E-value: 1.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   84 EDLEKFKALRIIVRIGSGFDNIDiKSAGDLGIAVCNVPAASVEET-ADSTLCHILNLYRRatwlHQALREGTRVQSVEQI 162
Cdd:cd12164  51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRD----MDRYAAQQRRGVWKPL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  163 REVASGAARIrgetlGIIGLGRVGQAVALRAKAFGFNVLFYD--PYLSDGVERALGLQRvstLQDLLFHSDCVTLHCGLN 240
Cdd:cd12164 126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVSGWSrsPKDIEGVTCFHGEEG---LDAFLAQTDILVCLLPLT 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  241 EHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAawys 320
Cdd:cd12164 198 PETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTVTPHI---- 272
                       250
                ....*....|....*....
gi 4557497  321 eqASIEMREEAAREIRRAI 339
Cdd:cd12164 273 --AAITDPDSAAAQVAENI 289
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
73-340 4.33e-23

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 100.11  E-value: 4.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    73 ALMYHTIT-LTREDLEKFKaLRIIVRIGSGFDNIDIKSAGDLGIAVCNVP---AASVeetADSTLCHILNLyrratwlhq 148
Cdd:PRK00257  40 VLLVRSVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPgcnARGV---VDYVLGSLLTL--------- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   149 ALREGtrvqsveqirevasgaARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDgverALGLQRVSTLQDLLF 228
Cdd:PRK00257 107 AEREG----------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQE----AEGDGDFVSLERILE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   229 HSDCVTLHCGLN-EHNH---HLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfsQGPL 304
Cdd:PRK00257 167 ECDVISLHTPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDL 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 4557497   305 KDAPN-LICTPHAAWYseqaSIEMREEAAREIRRAIT 340
Cdd:PRK00257 243 ELADLcTIATPHIAGY----SLDGKARGTAQIYQALC 275
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
82-347 8.52e-21

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 92.27  E-value: 8.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   82 TREDLEKFKALRIIVRIGSGFDNIDikSAGDLGIAVCN---VPAASveeTADSTLCHILNLYRRatwlhqaLREGTRVQS 158
Cdd:cd12166  51 VLEALRALPRLRVVQTLSAGYDGVL--PLLPEGVTLCNargVHDAS---TAELAVALILASLRG-------LPRFVRAQA 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  159 VEQIREVASGAarIRGETLGIIGLGRVGQAVALRAKAFGFNVLfydpylsdGVER----ALGLQRVSTLQDLLFHSDCVT 234
Cdd:cd12166 119 RGRWEPRRTPS--LADRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARtarpGEQVHGIDELPALLPEADVVV 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  235 LHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHESEPfsFSQG-PLKDAPNLICT 313
Cdd:cd12166 189 LIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEP--LPPGhPLWSAPGVLIT 265
                       250       260       270
                ....*....|....*....|....*....|....
gi 4557497  314 PHAAWYSEQASIEMREEAAREIRRAITGRIPDSL 347
Cdd:cd12166 266 PHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
114-317 1.45e-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: 91.56  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  114 GIAVCNVPAASVEETADSTLCHILNLYRRatwLHQALREGTRVQSveqirEVASGAARIRGETLGIIGLGRVGQAVALRA 193
Cdd:cd12159  73 GRRWTNAAGAYAETVAEHALALLLAGLRQ---LPARARATTWDPA-----EEDDLVTLLRGSTVAIVGAGGIGRALIPLL 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  194 KAFGFNVLFYDPYLSDgVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEK 273
Cdd:cd12159 145 APFGAKVIAVNRSGRP-VEGADETVPADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTD 223
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4557497  274 ALAQALKEGRIRGAALDVHESEPfsFSQG-PLKDAPNLICTPHAA 317
Cdd:cd12159 224 ALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
129-342 3.51e-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: 90.51  E-value: 3.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  129 ADSTLCHILNLYRRATWLHQALREGTRVQSV--EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLfydpy 206
Cdd:cd12160  96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT----- 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  207 lsdGVERALGLQ---RV---STLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALK 280
Cdd:cd12160 171 ---GVARSAGERagfPVvaeDELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALE 247
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557497  281 EGRIRGAALDVHESEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMreeAAREIRRAITGR 342
Cdd:cd12160 248 SGRLGGAALDVTATEPLPASS-PLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
135-321 6.67e-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: 81.55  E-value: 6.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  135 HILNLYRRATWLHQALREGTRVQsveqirevasgaariRGETLGIIGLGRVGQAVALRAKAFGFNVLFY----------- 203
Cdd:cd12163 109 QYIELQKEQTWGRRQEAYSVEDS---------------VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesr 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  204 --DPYLSDGVERALGLQRVStlqdlLFH-SDCVTLHCGLNEHNHHLIND----------FTVKQM----RQGAFLVNTAR 266
Cdd:cd12163 174 kdDGYIVPGTGDPDGSIPSA-----WFSgTDKASLHEFLRQDLDLLVVSlpltpatkhlLGAEEFeilaKRKTFVSNIAR 248
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4557497  267 GGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICTPHAAWYSE 321
Cdd:cd12163 249 GSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAPNVIITPHVSWQTQ 302
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
57-337 1.55e-15

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: 76.57  E-value: 1.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   57 QSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFD----NIDIKSAGDLGIAVCNVPA---ASVEETA 129
Cdd:cd12170  35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  130 DSTLCHILNLYRRATWLHQALRegtrvqsveqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSD 209
Cdd:cd12170 114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  210 GVERALGlqRVSTLQDLLFHSDCVTLHcgLNEhNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGrirGAAL 289
Cdd:cd12170 174 DAEAKGI--RYLPLNELLKTVDVICTC--LPK-NVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 4557497  290 DVHESEPfSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 337
Cdd:cd12170 246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQAFERLSQKVLANLEE 292
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
73-320 1.77e-14

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 74.56  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    73 ALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWlhqALRE 152
Cdd:PRK15438  40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   153 gtrvqsveqirevasgaarirgETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERAlglqRVSTLQDLLFHSDC 232
Cdd:PRK15438 117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEG----DFRSLDELVQEADI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   233 VTLHCGLNEHNH----HLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFSQGPLKDAP 308
Cdd:PRK15438 171 LTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKVD 249
                        250
                 ....*....|..
gi 4557497   309 nlICTPHAAWYS 320
Cdd:PRK15438 250 --IGTPHIAGYT 259
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
90-354 1.36e-13

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 71.07  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    90 KALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEeTADSTLCHILNLYRRATWLHQALREGTRVQSVEQIrevasga 169
Cdd:PRK06436  48 KKTKMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSIS-VAEHAFALLLAWAKNICENNYNMKNGNFKQSPTKL------- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   170 arIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYD-PYLSDGVERAlglqrVSTLQDLLFHSDCVTLHCGLNEHNHHLIN 248
Cdd:PRK06436 120 --LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTrSYVNDGISSI-----YMEPEDIMKKSDFVLISLPLTDETRGMIN 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   249 DFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPlkdaPNLICTPH-AAWYSEQASIEM 327
Cdd:PRK06436 193 SKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHvAGGMSGEIMQPA 268
                        250       260
                 ....*....|....*....|....*..
gi 4557497   328 REEAAREIRRAITGRiPdslKNCVNKD 354
Cdd:PRK06436 269 VALAFENIKNFFEGK-P---KNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
85-310 5.04e-12

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: 66.48  E-value: 5.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   85 DLEKFKALRIIVRIGSGFDNIDIKSAgdLGIAvcNVPAASVEETADSTLCHILNLYRRatwlhQALREGTRVQSVeQIRE 164
Cdd:cd12154  81 ALIQKLGDRLLFTYTIGADHRDLTEA--LARA--GLTAIAVEGVELPLLTSNSIGAGE-----LSVQFIARFLEV-QQPG 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497  165 VASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYD-PYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHN 243
Cdd:cd12154 151 RLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDiNVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGKR 230
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557497  244 HHLINDFT-VKQMRQGAFLVNTARG-GLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNL 310
Cdd:cd12154 231 AGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
90-340 2.81e-10

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 61.35  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497    90 KALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETA------DSTLCHILNLYRRATwLHQALREGTRVQSVEQIR 163
Cdd:PRK15469  55 RDLKAVFALGAGVDSILSKLQAHPEMLDPSVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPEYH 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   164 evasgaariRGE-TLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSD--GVERALG-------LQRVSTLQDLLFHSdcv 233
Cdd:PRK15469 134 ---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGreelsafLSQTRVLINLLPNT--- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557497   234 tlhcglnEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfSQGPLKDAPNLICT 313
Cdd:PRK15469 202 -------PETVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAIT 273
                        250       260
                 ....*....|....*....|....*..
gi 4557497   314 PHAawyseqASIEMREEAAREIRRAIT 340
Cdd:PRK15469 274 PHV------AAVTRPAEAVEYISRTIA 294
 
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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