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Conserved domains on  [gi|767961795|ref|XP_011537660|]
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C-terminal-binding protein 2 isoform X2 [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 ...
9-327 1.89e-148

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: 423.85  E-value: 1.89e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  85 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961795 325 PES 327
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 ...
9-327 1.89e-148

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: 423.85  E-value: 1.89e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  85 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961795 325 PES 327
Cdd:cd05299  310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
11-334 9.52e-96

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: 289.68  E-value: 9.52e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  11 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDI 88
Cdd:COG1052    3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  89 KAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRTGQ 168
Cdd:COG1052   83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 169 AVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:COG1052  157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 249 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPesl 328
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                 ....*.
gi 767961795 329 RNCVNK 334
Cdd:COG1052  311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
11-333 9.02e-84

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 258.76  E-value: 9.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   11 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   90 AAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQA 169
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  170 VAVRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 767961795  325 PeslRNCVN 333
Cdd:pfam00389 306 P---ANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
64-335 2.39e-55

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 186.15  E-value: 2.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQI 143
Cdd:PRK13243  59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAW 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 144 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEH 223
Cdd:PRK13243 139 HPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESDFVSLHVPLTKE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 224 NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWYSEQ 303
Cdd:PRK13243 218 TYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVVLAPHIGSATFE 295
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767961795 304 ASLEMREAAATEIRRAITGRIPESLrncVNKE 335
Cdd:PRK13243 296 AREGMAELVAENLIAFKRGEVPPTL---VNRE 324
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
9-327 1.89e-148

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: 423.85  E-value: 1.89e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299    1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  85 NVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299   78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299  152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299  231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                 ...
gi 767961795 325 PES 327
Cdd:cd05299  310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
11-318 1.32e-103

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: 309.17  E-value: 1.32e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  11 VALLDGRDCTVEMPILKDL-ATVAFCDAQSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:cd05198    2 VLVLEPLFPPEALEALEATgFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  90 AAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRvqsveqIREVASGAARIRGETLGLIGFGRTGQA 169
Cdd:cd05198   81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 170 VAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGG 249
Cdd:cd05198  155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961795 250 LVDEKALAQALKEGRIRGAALDVHESEPFSFAqGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRR 318
Cdd:cd05198  234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
11-334 9.52e-96

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: 289.68  E-value: 9.52e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  11 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDI 88
Cdd:COG1052    3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  89 KAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRTGQ 168
Cdd:COG1052   83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 169 AVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:COG1052  157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 249 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPesl 328
Cdd:COG1052  235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                 ....*.
gi 767961795 329 RNCVNK 334
Cdd:COG1052  311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
30-333 3.18e-95

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: 288.25  E-value: 3.18e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  30 ATVAFCDAQSTQEIHEKvLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEET 109
Cdd:COG0111   23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 110 ADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQ 189
Cdd:COG0111  102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 190 DGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAA 269
Cdd:COG0111  175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961795 270 LDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGripESLRNCVN 333
Cdd:COG0111  255 LDVFEPEPLP-ADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAG---EPLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
39-319 1.90e-89

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: 273.21  E-value: 1.90e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  39 STQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHIL 118
Cdd:cd12172   37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 119 NLYRRNTWLYQALREG--TRVQSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSL 196
Cdd:cd12172  115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 197 GVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE 276
Cdd:cd12172  184 GVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767961795 277 PFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 319
Cdd:cd12172  263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
63-323 2.72e-86

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


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 265.05  E-value: 2.72e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  63 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGT----RVQ 138
Cdd:cd12173   53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 139 SVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHC 218
Cdd:cd12173  133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGGVELV-SLDELLAEADFISLHT 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 219 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:cd12173  201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                        250       260
                 ....*....|....*....|....*
gi 767961795 299 WYSEQASLEMREAAATEIRRAITGR 323
Cdd:cd12173  280 ASTEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
11-333 9.02e-84

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 258.76  E-value: 9.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   11 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795   90 AAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQA 169
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  170 VAVRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 767961795  325 PeslRNCVN 333
Cdd:pfam00389 306 P---ANAVN 311
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
59-325 5.39e-80

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


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 249.03  E-value: 5.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  59 TITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvq 138
Cdd:cd12175   52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 139 svEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLH 217
Cdd:cd12175  128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLH 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 218 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHT 297
Cdd:cd12175  205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLP-PDDPLLRLDNVILTPHI 283
                        250       260
                 ....*....|....*....|....*...
gi 767961795 298 AWYSEQASLEMREAAATEIRRAITGRIP 325
Cdd:cd12175  284 AGVTDESYQRMAAIVAENIARLLRGEPP 311
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
62-310 1.63e-76

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: 240.05  E-value: 1.63e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12162   55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 Q------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIerslGVQRVyTLQDLLYQSDCVS 215
Cdd:cd12162  135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYV-SLDELLAQSDVIS 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL-KDAPNLICT 294
Cdd:cd12162  203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPR-ADNPLlKAAPNLIIT 281
                        250
                 ....*....|....*.
gi 767961795 295 PHTAWyseqASLEMRE 310
Cdd:cd12162  282 PHIAW----ASREARQ 293
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
63-333 6.37e-74

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: 233.67  E-value: 6.37e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  63 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlyqaLREGTRvqsveQ 142
Cdd:cd12178   56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR-------IAEGDR-----L 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 143 IRE-VASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDC 213
Cdd:cd12178  124 MRRgGFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDF 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGpLKDAPNLIC 293
Cdd:cd12178  203 VSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVIL 280
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767961795 294 TPHTAWYSEQASLEMREAAATEIRRAITGRIPeslRNCVN 333
Cdd:cd12178  281 TPHIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
23-322 5.69e-71

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240626 [Multi-domain]  Cd Length: 309  Bit Score: 225.74  E-value: 5.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  23 MPILKDLATVAFCD---AQSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVC 99
Cdd:cd05301   14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 100 NIPSAAVEETADSTICHILNLYRRntwlyqaLREGtrvqsveqIREVASGA-----------ARIRGETLGLIGFGRTGQ 168
Cdd:cd05301   93 NTPDVLTDATADLAFALLLAAARR-------VVEG--------DRFVRAGEwkgwsptlllgTDLHGKTLGIVGMGRIGQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 169 AVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:cd05301  158 AVARRAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961795 249 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:cd05301  237 GVVDEDALVEALKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
12-330 1.24e-70

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: 225.28  E-value: 1.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  12 ALLDGRDCTVEMPILKDLATVAFCDAQSTqeIHEKVLNEAVgaMMYHTI------TLTREDLEKFKALRVIVRIGSGYDN 85
Cdd:cd12177    7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKL--KGYDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  86 VDIKAAGELGIAVCNIPSA----AVEETAdstICHILNLYRRNTWLYQALREGtrvqsveQIREVASGAAR-IRGETLGL 160
Cdd:cd12177   83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 161 IGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQG 239
Cdd:cd12177  153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 240 AFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 319
Cdd:cd12177  232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIK-ADHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                        330
                 ....*....|.
gi 767961795 320 ITGRIPESLRN 330
Cdd:cd12177  311 LAGKEPKGILN 321
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
73-322 1.73e-70

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


Pssm-ID: 240645 [Multi-domain]  Cd Length: 321  Bit Score: 225.12  E-value: 1.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  73 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEqirevASGAAR 152
Cdd:cd12168   77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 153 IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDF 231
Cdd:cd12168  152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALATYYV-SLDELLAQSDVVSLNCPLTAATRHLINKK 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 232 TIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAWYSEQASLEMREA 311
Cdd:cd12168  231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEP--EVNPGLLKMPNVTLLPHMGTLTVETQEKMEEL 308
                        250
                 ....*....|.
gi 767961795 312 AATEIRRAITG 322
Cdd:cd12168  309 VLENIEAFLET 319
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
25-323 3.18e-70

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 224.49  E-value: 3.18e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  25 ILKDL-ATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPS 103
Cdd:cd01619   19 ILKAGgVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 104 AAVEETADSTICHILNLYRRntwlyqalREGTRVQSVEQIREVAS-GAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVI 182
Cdd:cd01619   99 YSPNAVAEHTIALILALLRN--------RKYIDERDKNQDLQDAGvIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 183 FYDPYLQDGIERSlGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKE 262
Cdd:cd01619  171 AYDPFRNPELEDK-GVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDS 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961795 263 GRIRGAALDVHESE-----------PFSFAQGP-LKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 323
Cdd:cd01619  249 GKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEGE 321
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
114-298 1.05e-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: 210.05  E-value: 1.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  114 ICHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGI 192
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  193 ERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV 272
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 767961795  273 HESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:pfam02826 154 FEPEPLP-ADHPLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
61-296 1.86e-65

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: 211.24  E-value: 1.86e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsv 140
Cdd:cd05303   52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 141 eQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNL 220
Cdd:cd05303  126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLHVPL 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961795 221 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgpLKDAPNLICTPH 296
Cdd:cd05303  204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
58-298 2.28e-65

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: 211.24  E-value: 2.28e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  58 HTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrv 137
Cdd:cd12171   53 HFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDG--- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 138 qsveQIREVASGAAR----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDC 213
Cdd:cd12171  130 ----EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGVKKV-SLEELLKRSDV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 293
Cdd:cd12171  205 VSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLP-ADHPLLKLDNVTL 283

                 ....*
gi 767961795 294 TPHTA 298
Cdd:cd12171  284 TPHIA 288
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
64-333 5.80e-61

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: 199.71  E-value: 5.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETAdstICHILNLYRRntwLYQALREGTRVQSV 140
Cdd:cd12174   42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGAnanAVAELV---IAMMLALSRN---IIQAIKWVTNGDGD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 141 EQIREVASGAAR-----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLG--VQRVYTLQDLLYQSDC 213
Cdd:cd12174  116 DISKGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSveVQRVTSLEELLATADY 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEpfsfaqgPLKDAPNLIC 293
Cdd:cd12174  196 ITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIA 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767961795 294 TPHTAWYSEQASLEMREAAATEIRRAI-TGRIPeslrNCVN 333
Cdd:cd12174  269 TPHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
39-327 4.25e-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: 193.14  E-value: 4.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  39 STQEIHEKVLNEAVGA---MMYHTITLTREDLEKFKA--LRVI-VRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADS 112
Cdd:cd12186   30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEygIKQIaLRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 113 TICHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12186  109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 192 IErSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 271
Cdd:cd12186  182 LE-KFLLYYD-SLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961795 272 VHESE----PFSFAQGPLKDA--------PNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPES 327
Cdd:cd12186  260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEGGTSEN 327
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
62-309 3.74e-56

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


Pssm-ID: 240638 [Multi-domain]  Cd Length: 315  Bit Score: 187.43  E-value: 3.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12161   59 LPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 QiREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIErSLGVQRVyTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12161  139 G-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK-ALGIEYV-SLDELLAESDIVSLHLPLN 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYS 301
Cdd:cd12161  209 DETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFAT 288

                 ....*...
gi 767961795 302 EQAsLEMR 309
Cdd:cd12161  289 EEA-MEKR 295
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
24-322 5.31e-56

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


Pssm-ID: 240646 [Multi-domain]  Cd Length: 308  Bit Score: 186.95  E-value: 5.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  24 PILKDLATV-AFCD-AQSTQEIHEKVLN-EAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN 100
Cdd:cd12169   19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 101 IPSAaVEETADSTICHILNLYRRNTWLYQALREGTRVQSVeqirevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFS 180
Cdd:cd12169   98 TGGG-PTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 181 VIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQAL 260
Cdd:cd12169  168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961795 261 KEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:cd12169  248 RAGRIAGAALDVFDVEPLP-ADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
PRK13243 PRK13243
glyoxylate reductase; Reviewed
64-335 2.39e-55

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 186.15  E-value: 2.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQI 143
Cdd:PRK13243  59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAW 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 144 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEH 223
Cdd:PRK13243 139 HPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESDFVSLHVPLTKE 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 224 NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWYSEQ 303
Cdd:PRK13243 218 TYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVVLAPHIGSATFE 295
                        250       260       270
                 ....*....|....*....|....*....|..
gi 767961795 304 ASLEMREAAATEIRRAITGRIPESLrncVNKE 335
Cdd:PRK13243 296 AREGMAELVAENLIAFKRGEVPPTL---VNRE 324
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
11-322 3.37e-55

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 185.19  E-value: 3.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  11 VALLDGR---DCTVEmpILKDLATVAFCDAQSTQEIHEKVLNEAVgaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVD 87
Cdd:PRK08410   3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  88 IKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSvEQIREVASGAARIRGETLGLIGFGRTG 167
Cdd:PRK08410  79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 168 QAVAVRAKAFGFSVIFYDPylqDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAAR 247
Cdd:PRK08410 158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961795 248 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfAQGPL---KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:PRK08410 234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
36-323 1.38e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 183.75  E-value: 1.38e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  36 DAQSTQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTIC 115
Cdd:PRK06487  32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 116 HILNLYRRNTWLYQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpyL 188
Cdd:PRK06487 110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 189 QDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGA 268
Cdd:PRK06487 177 GQLPGRPARPDRL-PLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767961795 269 ALDVHESEPfSFAQGPL--KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 323
Cdd:PRK06487 256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
62-304 2.16e-54

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: 183.63  E-value: 2.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12187   53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 QIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12187  133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEP--------FSFAQGPLKDA----- 288
Cdd:cd12187  205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelFREDVSPEDLKkllad 284
                        250       260
                 ....*....|....*....|..
gi 767961795 289 ------PNLICTPHTAWYSEQA 304
Cdd:cd12187  285 hallrkPNVIITPHVAYNTKEA 306
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
58-310 2.11e-51

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 175.47  E-value: 2.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  58 HTITLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAvEETADSTICHILNLYRRntwlYQALREGT 135
Cdd:cd12185   52 GKSKISAELLEKLKEAgvKYISTRSIGYDHIDLDAAKELGIKVSNVTYSP-NSVADYTVMLMLMALRK----YKQIMKRA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 136 RVQ--SVEQIRevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslGVQRVyTLQDLLYQSDC 213
Cdd:cd12185  127 EVNdySLGGLQ-----GRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNEEVKK--YAEYV-DLDTLYKESDI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQ----------- 282
Cdd:cd12185  199 ITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEDGIYYNdrkgdilsnre 278
                        250       260
                 ....*....|....*....|....*....
gi 767961795 283 -GPLKDAPNLICTPHTAWYSEQASLEMRE 310
Cdd:cd12185  279 lAILRSFPNVILTPHMAFYTDQAVSDMVE 307
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
61-317 3.12e-51

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: 174.94  E-value: 3.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREG---- 134
Cdd:cd12183   55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGnfsl 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 135 ---TRVQsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQS 211
Cdd:cd12183  135 dglLGFD--------------LHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAK-LGVEYV-DLDELLAES 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 212 DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG----PLKD 287
Cdd:cd12183  199 DIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDhsdeIIQD 278
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767961795 288 A--------PNLICTPHTAWYSEQAsleMREAAATEIR 317
Cdd:cd12183  279 DvlarllsfPNVLITGHQAFFTKEA---LTNIAETTLE 313
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
61-296 1.31e-48

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: 167.37  E-value: 1.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwLYQALREGTRvqsv 140
Cdd:cd12176   53 QLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARR---LPDRNAAAHR---- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 141 EQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIE--RSLGVQR-VYTLQDLLYQSDCVSLH 217
Cdd:cd12176  126 GIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD------IAekLPLGNARqVSSLEELLAEADFVTLH 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 218 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLICT 294
Cdd:cd12176  200 VPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGEPfssPLQGLPNVILT 279

                 ..
gi 767961795 295 PH 296
Cdd:cd12176  280 PH 281
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-341 1.37e-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: 1.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKALRVIVRI-GSGYDNVDiKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQs 139
Cdd:cd12167   61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 140 veqiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCN 219
Cdd:cd12167  139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSLHAP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 220 LNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLICTPHTAW 299
Cdd:cd12167  214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLP-PDSPLRTLPNVLLTPHIAG 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767961795 300 YSEQASLEMREAAATEIRRAITGRIPeslRNCVNKEFFVTSA 341
Cdd:cd12167  292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
62-304 1.24e-46

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 162.66  E-value: 1.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIP---SAAVEETADSTIC---HILNLYRRNtwlyqalREGT 135
Cdd:PRK06932  55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTgysSTTVPEHVLGMIFalkHSLMGWYRD-------QLSD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 136 RVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgiERSLGVQRV-YT-LQDLLYQSDC 213
Cdd:PRK06932 128 RWATCKQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREgYTpFEEVLKQADI 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL----KDAP 289
Cdd:PRK06932 201 VTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLP 279
                        250
                 ....*....|....*
gi 767961795 290 NLICTPHTAWYSEQA 304
Cdd:PRK06932 280 NLLITPHIAWASDSA 294
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
57-314 8.32e-46

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: 161.34  E-value: 8.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  57 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTR 136
Cdd:cd05302   69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 137 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVS 215
Cdd:cd05302  149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTP 295
Cdd:cd05302  224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302
                        250
                 ....*....|....*....
gi 767961795 296 HTAWYSEQAslEMREAAAT 314
Cdd:cd05302  303 HISGTTLDA--QARYAAGT 319
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
62-313 6.39e-44

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: 154.93  E-value: 6.39e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGtrvqsvE 141
Cdd:cd12156   54 LSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------R 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgvQRVYTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12156  128 WPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPY----RYYASLLELAAESDVLVVACPGG 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGP--LKDAPNLICTPHTAw 299
Cdd:cd12156  204 PATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIA- 278
                        250
                 ....*....|....
gi 767961795 300 yseQASLEMREAAA 313
Cdd:cd12156  279 ---SATVETRRAMG 289
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
62-296 6.96e-44

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 157.65  E-value: 6.96e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALrviVRIGS---GYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQ 138
Cdd:PRK11790  65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNK 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 139 SveqirevASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIER--SLG-VQRVYTLQDLLYQSDCVS 215
Cdd:PRK11790 142 S-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDklPLGnARQVGSLEELLAQSDVVS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLI 292
Cdd:PRK11790 209 LHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDNVI 288

                 ....
gi 767961795 293 CTPH 296
Cdd:PRK11790 289 LTPH 292
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
39-322 7.55e-44

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: 155.52  E-value: 7.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  39 STQEIHEKVLNeAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHIL 118
Cdd:cd12157   34 SREELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 119 NLYRRntwlyqaLREGTRVqsveqIREVASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12157  113 GLGRH-------ILAGDRF-----VRSGKFGGWRpkfygtgLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 192 I-ERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAAL 270
Cdd:cd12157  181 AeEQALNLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAA 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767961795 271 DVHESE-------PFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:cd12157  260 DVFEMEdwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
38-302 3.04e-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: 3.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  38 QSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETADSTI 114
Cdd:cd12179   29 ISREEI-LAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGnrdAVGEHALGML 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 115 CHILNLYRRNTWLYQA---LREGTRvqSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12179  108 LALFNKLNRADQEVRNgiwDREGNR--GVE-----------LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 192 IERslgVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 271
Cdd:cd12179  175 DAY---AEQV-SLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLD 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767961795 272 VHESEPFSF---AQGP-----LKDAPNLICTPHTA-WYSE 302
Cdd:cd12179  251 VLEYEKASFesiFNQPeafeyLIKSPKVILTPHIAgWTFE 290
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
64-325 2.49e-42

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: 151.24  E-value: 2.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGElGIAVCNIP--SAAVEETAdstICHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12165   52 EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHgnSPAVAEHA---LALILALAKRIVEYDNDLRRGIWHGRAG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 QIREVASgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCV 214
Cdd:cd12165  128 EEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVI--------GVSRSpkedEGADFVGTLSDLdeaLEQADVV 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 215 SLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--------HESEPFSFaqgPLK 286
Cdd:cd12165  196 VVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDPVAPSRY---PFH 272
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 767961795 287 DAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 325
Cdd:cd12165  273 ELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPL 311
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
62-315 5.89e-41

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 149.44  E-value: 5.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRvqsve 141
Cdd:PRK07574 104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 142 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNL 220
Cdd:PRK07574 179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 221 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTPHTAWY 300
Cdd:PRK07574 259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQP-APADHPWRTMPRNGMTPHISGT 337
                        250
                 ....*....|....*
gi 767961795 301 SEQAslEMREAAATE 315
Cdd:PRK07574 338 TLSA--QARYAAGTR 350
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
64-335 5.12e-40

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: 144.97  E-value: 5.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN---IPSAAVeetADSTICHILNLYRRnTWLYQALREGTRVQSV 140
Cdd:cd05300   51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNargIFGPPI---AEYVLGYMLAFARK-LPRYARNQAERRWQRR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 141 EQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL-----GVQRVYT---LQDLLYQSD 212
Cdd:cd05300  127 GPVRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEAD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 213 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLI 292
Cdd:cd05300  192 YVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVI 270
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767961795 293 CTPHTAWYSEQaslEMREAA---ATEIRRAITGripESLRNCVNKE 335
Cdd:cd05300  271 ITPHISGDSPS---YPERVVeifLENLRRYLAG---EPLLNVVDKD 310
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
61-310 1.42e-39

(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: 144.36  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKAL---RVIVRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRR-NTWLYQALREGTR 136
Cdd:cd12184   55 FADKENLEIYKEYgikYVFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHtAYTASRTANKNFK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 137 VQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSL 216
Cdd:cd12184  134 VDPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKD---VVTFVSLDELLKKSDIISL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 217 HC-NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--HESEPF--SFAQGPLKDA--- 288
Cdd:cd12184  204 HVpYIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvve 283
                        250       260
                 ....*....|....*....|....*...
gi 767961795 289 ------PNLICTPHTAWYSEQASLEMRE 310
Cdd:cd12184  284 klldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
40-333 8.39e-39

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 142.20  E-value: 8.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  40 TQEIHEKVLNEAVGaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILN 119
Cdd:PRK15409  35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 120 LYRRntwlyqALREGTRVQSVEQIREVASG--AARIRGETLGLIGFGRTGQAVAVRAKaFGFSV-IFYDPYLQ-DGIERS 195
Cdd:PRK15409 114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 196 LGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHES 275
Cdd:PRK15409 187 FNARYC-DLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767961795 276 EPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPEslrNCVN 333
Cdd:PRK15409 266 EPLS-VDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEK---NCVN 319
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
61-320 1.05e-36

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 136.89  E-value: 1.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  61 TLTREDLEKFKALrvIVR-----------------IGS---GYDNVDIKAAGELGIAVCNIP---SAAVeetADSTICHI 117
Cdd:cd12158   28 EITAEDLKDADVL--LVRsvtkvneallegskvkfVGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSAL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 118 LNLYRRNTWLyqalregtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQdgiERSLG 197
Cdd:cd12158  103 LVLAQRQGFS-------------------------LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAEGD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 198 VQRVyTLQDLLYQSDCVSLHCNLNEH----NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVH 273
Cdd:cd12158  155 PGFV-SLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767961795 274 ESEPfsfaqgplkdAPNL-------ICTPHTAWYseqaSLEMREAAATEIRRAI 320
Cdd:cd12158  234 ENEP----------EIDLelldkvdIATPHIAGY----SLEGKARGTEMIYEAL 273
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
73-304 5.81e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 134.87  E-value: 5.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  73 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlYQALREGTRVQSveqIREVASGAAR 152
Cdd:PRK08605  70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRH----FNQIQTKVREHD---FRWEPPILSR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 153 -IRGETLGLIGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSlgVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLIND 230
Cdd:PRK08605 143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATY--VDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 231 FTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFAQGPLKDA--------PNLICTPHTA 298
Cdd:PRK08605 221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                 ....*.
gi 767961795 299 WYSEQA 304
Cdd:PRK08605 301 FYTDAA 306
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
151-333 2.82e-35

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: 132.08  E-value: 2.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 151 ARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS------LGVQRVYTLQDLLYQSDCVSLHCNLNEHN 224
Cdd:cd12180  131 GSLAGSTLGIVGFGAIGQALARRALALGMRVL--------ALRRSgrpsdvPGVEAAADLAELFARSDHLVLAAPLTPET 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 225 HHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQA 304
Cdd:cd12180  203 RHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDG 281
                        170       180
                 ....*....|....*....|....*....
gi 767961795 305 SLEMREAAATEIRRAITGRipeSLRNCVN 333
Cdd:cd12180  282 RRNLADRFLENLARYRAGQ---PLHDLVD 307
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
66-303 1.14e-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: 130.78  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  66 DLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTrVQSVEQIRE 145
Cdd:cd12155   54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKK-WKMDSSLLE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 146 VAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVSLHC 218
Cdd:cd12155  133 LY-------GKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 219 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:cd12155  198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                 ....*
gi 767961795 299 WYSEQ 303
Cdd:cd12155  277 GVSEH 281
PLN02928 PLN02928
oxidoreductase family protein
51-325 1.91e-34

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 130.96  E-value: 1.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  51 AVGAMMyhtiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAV---EETADSTICHILNLYRRNTWL 127
Cdd:PLN02928  65 CVPKMM----RLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTgnaASCAEMAIYLMLGLLRKQNEM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 128 YQALRegtrvqsveqirevasgaARIRGETLG---------LIGFGRTGQAVAVRAKAFGFSVIFY------DPYLQDGI 192
Cdd:PLN02928 141 QISLK------------------ARRLGEPIGdtlfgktvfILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 193 ERSLGVQRVY------TLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIR 266
Cdd:PLN02928 203 PNGDVDDLVDekggheDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLG 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767961795 267 GAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 325
Cdd:PLN02928 283 GLAIDVAWSEPFD-PDDPILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPL 340
PLN02306 PLN02306
hydroxypyruvate reductase
82-324 2.07e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.13  E-value: 2.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  82 GYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTRVQSVEQIREvasgAARIRGETLGLI 161
Cdd:PLN02306  96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 162 GFGRTGQAVA-VRAKAFGFSVIFYDPY---------------LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNH 225
Cdd:PLN02306 172 GAGRIGSAYArMMVEGFKMNLIYYDLYqstrlekfvtaygqfLKANGEQPVTWKRASSMEEVLREADVISLHPVLDKTTY 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 226 HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAwyseQAS 305
Cdd:PLN02306 252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SAS 325
                        250
                 ....*....|....*....
gi 767961795 306 LEMREAAATEIRRAITGRI 324
Cdd:PLN02306 326 KWTREGMATLAALNVLGKL 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
57-315 4.16e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 114.18  E-value: 4.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  57 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWLYQALREGTR 136
Cdd:PLN03139 106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 137 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVS 215
Cdd:PLN03139 186 -----NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVVV 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTP 295
Cdd:PLN03139 261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMTP 339
                        250       260
                 ....*....|....*....|
gi 767961795 296 HTAWYSEQASLemREAAATE 315
Cdd:PLN03139 340 HISGTTIDAQL--RYAAGVK 357
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
67-304 3.08e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 110.77  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  67 LEKFkALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRntwlYQALREgtRVQSVEQIREV 146
Cdd:PRK12480  65 LESY-GIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRR----FPDIER--RVQAHDFTWQA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 147 ASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSLHCNLNEHNHH 226
Cdd:PRK12480 138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 227 LINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFA---QGPLKDAP---------NLICT 294
Cdd:PRK12480 215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAYFTndwTNKDIDDKtllelieheRILVT 294
                        250
                 ....*....|
gi 767961795 295 PHTAWYSEQA 304
Cdd:PRK12480 295 PHIAFFSDEA 304
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
65-333 2.74e-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: 99.11  E-value: 2.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  65 EDLEKFKALRVIVRIGSGYDNVDiKAAGELGIAVCNIPSAAVEET-ADSTICHILNLYRRntwlYQALREGTRVQSVEQI 143
Cdd:cd12164   51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRD----MDRYAAQQRRGVWKPL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 144 REVASGAARIrgetlGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL----GVQRVY---TLQDLLYQSDCVsl 216
Cdd:cd12164  126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkdieGVTCFHgeeGLDAFLAQTDIL-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 217 hCNL---NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 293
Cdd:cd12164  191 -VCLlplTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTV 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 767961795 294 TPHTawyseqASLEMREAAATEIRRAIT-GRIPESLRNCVN 333
Cdd:cd12164  269 TPHI------AAITDPDSAAAQVAENIRrLEAGEPLPNLVD 303
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
63-328 3.51e-23

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: 98.82  E-value: 3.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  63 TREDLEKFKALRVIVRIGSGYDNVdIKAAGElGIAVCNipSAAVEE--TADSTICHILNLYRRNTWLYQALREG----TR 136
Cdd:cd12166   51 VLEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGLPRFVRAQARGrwepRR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 137 VQSVEqirevasgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDLLYQSD 212
Cdd:cd12166  127 TPSLA-------------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEAD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 213 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLI 292
Cdd:cd12166  186 VVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEPLP-PGHPLWSAPGVL 263
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767961795 293 CTPHTAWYSEQASLEMREAAATEIRRAITGRIPESL 328
Cdd:cd12166  264 ITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
143-298 7.21e-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: 240636  Cd Length: 303  Bit Score: 92.33  E-value: 7.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 143 IREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVS 215
Cdd:cd12159  113 PAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQG-PLKDAPNLICT 294
Cdd:cd12159  185 LAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALIT 262

                 ....
gi 767961795 295 PHTA 298
Cdd:cd12159  263 PHVA 266
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
162-330 2.50e-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: 90.90  E-value: 2.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 162 GFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSLGVQ---RVYT---LQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQ 235
Cdd:cd12160  150 GFGSIGQRLAPLLTALGARVT--------GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAA 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 236 MRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMreaAATE 315
Cdd:cd12160  222 LPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLP-ASSPLWDAPNLILTPHAAGGRPQGAEEL---IAEN 297
                        170
                 ....*....|....*
gi 767961795 316 IRRAITGRipeSLRN 330
Cdd:cd12160  298 LRAFLAGG---PLRN 309
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
59-301 5.11e-20

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 90.87  E-value: 5.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  59 TIT-LTREDLEKFKaLRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLyrrntwlyqALREGtrv 137
Cdd:PRK00257  45 SVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTL---------AEREG--- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 138 qsveqirevasgaARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqrvyTLQDLLYQSDCVSLH 217
Cdd:PRK00257 112 -------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFV----SLERILEECDVISLH 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 218 CNLN-EHNH---HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGPLKDAPN-LI 292
Cdd:PRK00257 175 TPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTI 250

                 ....*....
gi 767961795 293 CTPHTAWYS 301
Cdd:PRK00257 251 ATPHIAGYS 259
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
125-302 1.47e-19

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 88.87  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 125 TWL-----YQALREGTRVQSVEQiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFY--------------- 184
Cdd:cd12163   99 TWLvlshhFLQYIELQKEQTWGR-RQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkddg 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 185 -------DPylqDGI--------ERSLGVQRVYTLQ-DLLyqsdCVSLhcNLNEHNHHLIN--DFTIKQMRqGAFLVNAA 246
Cdd:cd12163  178 yivpgtgDP---DGSipsawfsgTDKASLHEFLRQDlDLL----VVSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIA 247
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767961795 247 RGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSE 302
Cdd:cd12163  248 RGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAPNVIITPHVSWQTQ 302
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
38-304 1.04e-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: 76.96  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  38 QSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYD----NVDIKAAGELGIAVCNIPSAAVEETADST 113
Cdd:cd12170   35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 114 ICH---ILNLYRRNTWLYQALRegtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD 190
Cdd:cd12170  114 ISElirLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 191 GIERSlGVqRVYTLQDLLYQSDCVSLHCNlneHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGrirGAAL 270
Cdd:cd12170  174 DAEAK-GI-RYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767961795 271 DVHESEPfSFAQGPLKDAPNLICTPHTAWYSEQA 304
Cdd:cd12170  246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
54-324 1.14e-13

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 71.86  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  54 AMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTICHILNLYRRNTWlyqALRE 133
Cdd:PRK15438  40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 134 gtrvqsveqirevasgaarirgETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD-GIERSLgvqrvYTLQDLLYQSD 212
Cdd:PRK15438 117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 213 CVSLHCNLNEHNH----HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDA 288
Cdd:PRK15438 170 ILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKV 248
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767961795 289 PnlICTPHTAWYseqaSLEMREAAATEIRRAITGRI 324
Cdd:PRK15438 249 D--IGTPHIAGY----TLEGKARGTTQVFEAYSKFI 278
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
155-335 5.34e-13

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 69.14  E-value: 5.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 155 GETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGierslGVQRVY-TLQDLLYQSDCVSLHCNLNEHNHHLINDFTI 233
Cdd:PRK06436 122 NKSLGILGYGGIGRRVALLAKAFGMNIYAYTRSYVND-----GISSIYmEPEDIMKKSDFVLISLPLTDETRGMINSKML 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 234 KQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPlkdaPNLICTPHTAwysEQASLEMREAAA 313
Cdd:PRK06436 197 SLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHVA---GGMSGEIMQPAV 269
                        170       180
                 ....*....|....*....|..
gi 767961795 314 TEIRRAITGRIPESLRNCVNKE 335
Cdd:PRK06436 270 ALAFENIKNFFEGKPKNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
66-291 1.14e-11

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 65.33  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  66 DLEKFKALRVIVRIGSGYDNVDIK-AAGELGIAVCNIP-SAAVEETADSTIChilnlyrrntwLYQALREGTRVQSVeQI 143
Cdd:cd12154   81 ALIQKLGDRLLFTYTIGADHRDLTeALARAGLTAIAVEgVELPLLTSNSIGA-----------GELSVQFIARFLEV-QQ 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 144 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVSLHCNLNE 222
Cdd:cd12154  149 PGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALeQLEELGGKNVEELEEALAEADVIVTTTLLPG 228
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961795 223 HNHHLINDFT-IKQMRQGAFLVNAARG-GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNL 291
Cdd:cd12154  229 KRAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
71-321 1.91e-10

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 61.74  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795  71 KALRVIVRIGSGYDNV--DIKAAGELGIAvcNIPSAAVEETA------DSTICHILNLYRRNTwLYQALREGTRVQSVEQ 142
Cdd:PRK15469  55 RDLKAVFALGAGVDSIlsKLQAHPEMLDP--SVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 143 IRevasgaariRGE-TLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD--GIERSLGVQRvytLQDLLYQSDC-VSLHC 218
Cdd:PRK15469 132 YH---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGREE---LSAFLSQTRVlINLLP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961795 219 NLNEhNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:PRK15469 200 NTPE-TVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVA 277
                        250       260
                 ....*....|....*....|...
gi 767961795 299 WYSEQASlemreaAATEIRRAIT 321
Cdd:PRK15469 278 AVTRPAE------AVEYISRTIA 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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