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Conserved domains on  [gi|1907177089|ref|XP_036008523|]
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C-terminal-binding protein 2 isoform X2 [Mus musculus]

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 2.13e-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: 423.46  E-value: 2.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  85 NVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1907177089 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 2.13e-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: 423.46  E-value: 2.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  85 NVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1907177089 325 PES 327
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
11-334 5.78e-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: 290.07  E-value: 5.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDI 88
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  89 KAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRTGQ 168
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 169 AVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 249 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPesl 328
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1907177089 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 7.35e-84

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 259.14  E-value: 7.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  90 AAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQA 169
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 170 VAVRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 1907177089 325 PeslRNCVN 333
Cdd:pfam00389 306 P---ANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
64-335 2.89e-55

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 185.77  E-value: 2.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQI 143
Cdd:PRK13243   59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAW 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 144 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEH 223
Cdd:PRK13243  139 HPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESDFVSLHVPLTKE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 224 NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWYSEQ 303
Cdd:PRK13243  218 TYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVVLAPHIGSATFE 295
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907177089 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 2.13e-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: 423.46  E-value: 2.13e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089   9 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYD 84
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  85 NVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 164
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 165 RTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1907177089 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 1.07e-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: 309.56  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGRDCTVEMPILKDL-ATVAFCDAQSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:cd05198     2 VLVLEPLFPPEALEALEATgFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  90 AAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRvqsveqIREVASGAARIRGETLGLIGFGRTGQA 169
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 170 VAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGG 249
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907177089 250 LVDEKALAQALKEGRIRGAALDVHESEPFSFAqGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRR 318
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
11-334 5.78e-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: 290.07  E-value: 5.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDI 88
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  89 KAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRTGQ 168
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 169 AVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 249 GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPesl 328
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1907177089 329 RNCVNK 334
Cdd:COG1052   311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
30-333 3.04e-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: 3.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  30 ATVAFCDAQSTQEIHEKvLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEET 109
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 110 ADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQ 189
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 190 DGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAA 269
Cdd:COG0111   175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907177089 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 1.80e-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: 1.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  39 STQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHIL 118
Cdd:cd12172    37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 119 NLYRRNTWLYQALREG--TRVQSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSL 196
Cdd:cd12172   115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 197 GVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE 276
Cdd:cd12172   184 GVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907177089 277 PFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 319
Cdd:cd12172   263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
63-323 5.62e-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: 264.28  E-value: 5.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  63 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGT----RVQ 138
Cdd:cd12173    53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 139 SVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHC 218
Cdd:cd12173   133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGGVELV-SLDELLAEADFISLHT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 219 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:cd12173   201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                         250       260
                  ....*....|....*....|....*
gi 1907177089 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 7.35e-84

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 259.14  E-value: 7.35e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGAMMYHTIT-LTREDLEKFKALRVIVRIGSGYDNVDIK 89
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  90 AAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRTGQA 169
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 170 VAVRAKAFGFSVIFYDPYLQDgiERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 244
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 245 AARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 324
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 1907177089 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 5.51e-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: 5.51e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  59 TITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGtrvq 138
Cdd:cd12175    52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 139 svEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLH 217
Cdd:cd12175   128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 218 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHT 297
Cdd:cd12175   205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLP-PDDPLLRLDNVILTPHI 283
                         250       260
                  ....*....|....*....|....*...
gi 1907177089 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 3.77e-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: 238.89  E-value: 3.77e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12162    55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 Q------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIerslGVQRVyTLQDLLYQSDCVS 215
Cdd:cd12162   135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYV-SLDELLAQSDVIS 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL-KDAPNLICT 294
Cdd:cd12162   203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPR-ADNPLlKAAPNLIIT 281
                         250
                  ....*....|....*.
gi 1907177089 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 3.72e-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: 234.44  E-value: 3.72e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  63 TREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRntwlyqaLREGTRvqsveQ 142
Cdd:cd12178    56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR-------IAEGDR-----L 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 143 IRE-VASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDC 213
Cdd:cd12178   124 MRRgGFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDF 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGpLKDAPNLIC 293
Cdd:cd12178   203 VSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVIL 280
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907177089 294 TPHTAWYSEQASLEMREAAATEIRRAITGRIPeslRNCVN 333
Cdd:cd12178   281 TPHIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
23-322 3.19e-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: 226.51  E-value: 3.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  23 MPILKDLATVAFCD---AQSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVC 99
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 100 NIPSAAVEETADSTVCHILNLYRRntwlyqaLREGtrvqsveqIREVASGA-----------ARIRGETLGLIGFGRTGQ 168
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARR-------VVEG--------DRFVRAGEwkgwsptlllgTDLHGKTLGIVGMGRIGQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 169 AVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARG 248
Cdd:cd05301   158 AVARRAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARG 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907177089 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 5.36e-71

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: 226.43  E-value: 5.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  12 ALLDGRDCTVEMPILKDLATVAFCDAQSTqeIHEKVLNEAVgaMMYHTI------TLTREDLEKFKALRVIVRIGSGYDN 85
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKL--KGYDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  86 VDIKAAGELGIAVCNIPSA----AVEETAdstVCHILNLYRRNTWLYQALREGtrvqsveQIREVASGAAR-IRGETLGL 160
Cdd:cd12177    83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 161 IGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQG 239
Cdd:cd12177   153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 240 AFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 319
Cdd:cd12177   232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIK-ADHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                         330
                  ....*....|.
gi 1907177089 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 2.81e-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: 224.35  E-value: 2.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  73 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEqirevASGAAR 152
Cdd:cd12168    77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 153 IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDF 231
Cdd:cd12168   152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALATYYV-SLDELLAQSDVVSLNCPLTAATRHLINKK 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 232 TIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAWYSEQASLEMREA 311
Cdd:cd12168   231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEP--EVNPGLLKMPNVTLLPHMGTLTVETQEKMEEL 308
                         250
                  ....*....|.
gi 1907177089 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 5.92e-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: 223.72  E-value: 5.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  25 ILKDL-ATVAFCDAQSTQEIHEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPS 103
Cdd:cd01619    19 ILKAGgVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 104 AAVEETADSTVCHILNLYRRntwlyqalREGTRVQSVEQIREVAS-GAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVI 182
Cdd:cd01619    99 YSPNAVAEHTIALILALLRN--------RKYIDERDKNQDLQDAGvIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 183 FYDPYLQDGIERSlGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKE 262
Cdd:cd01619   171 AYDPFRNPELEDK-GVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDS 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907177089 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 1.01e-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: 210.43  E-value: 1.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 114 VCHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGI 192
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 193 ERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV 272
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 1907177089 273 HESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:pfam02826 154 FEPEPLP-ADHPLLDLPNVILTPHIA 178
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
58-298 1.28e-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: 212.01  E-value: 1.28e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  58 HTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGtrv 137
Cdd:cd12171    53 HFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDG--- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 138 qsveQIREVASGAAR----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDC 213
Cdd:cd12171   130 ----EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEADGVKKV-SLEELLKRSDV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 293
Cdd:cd12171   205 VSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLP-ADHPLLKLDNVTL 283

                  ....*
gi 1907177089 294 TPHTA 298
Cdd:cd12171   284 TPHIA 288
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
61-296 5.61e-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: 210.09  E-value: 5.61e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGtrvqsv 140
Cdd:cd05303    52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 141 eQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNL 220
Cdd:cd05303   126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLHVPL 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907177089 221 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQgpLKDAPNLICTPH 296
Cdd:cd05303   204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
64-333 9.69e-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: 199.32  E-value: 9.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETAdstVCHILNLYRRntwLYQALREGTRVQSV 140
Cdd:cd12174    42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGAnanAVAELV---IAMMLALSRN---IIQAIKWVTNGDGD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 141 EQIREVASGAAR-----IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLG--VQRVYTLQDLLYQSDC 213
Cdd:cd12174   116 DISKGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSveVQRVTSLEELLATADY 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEpfsfaqgPLKDAPNLIC 293
Cdd:cd12174   196 ITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIA 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907177089 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 9.09e-59

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


Pssm-ID: 240662  Cd Length: 329  Bit Score: 194.68  E-value: 9.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  39 STQEIHEKVLNEAVGA---MMYHTITLTREDLEKFKA--LRVI-VRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADS 112
Cdd:cd12186    30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEygIKQIaLRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 113 TVCHILNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12186   109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 192 IErSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 271
Cdd:cd12186   182 LE-KFLLYYD-SLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907177089 272 VHESE----PFSFAQGPLKDA--------PNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPES 327
Cdd:cd12186   260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEGGTSEN 327
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
24-322 1.24e-55

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


Pssm-ID: 240646 [Multi-domain]  Cd Length: 308  Bit Score: 186.18  E-value: 1.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  24 PILKDLATV-AFCD-AQSTQEIHEKVLN-EAVGAMMYHTiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN 100
Cdd:cd12169    19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 101 IPSAaVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVeqirevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFS 180
Cdd:cd12169    98 TGGG-PTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 181 VIFYDPYLQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQAL 260
Cdd:cd12169   168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907177089 261 KEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:cd12169   248 RAGRIAGAALDVFDVEPLP-ADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
62-309 2.05e-55

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


Pssm-ID: 240638 [Multi-domain]  Cd Length: 315  Bit Score: 185.50  E-value: 2.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12161    59 LPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 QiREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIErSLGVQRVyTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12161   139 G-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK-ALGIEYV-SLDELLAESDIVSLHLPLN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNLICTPHTAWYS 301
Cdd:cd12161   209 DETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFAT 288

                  ....*...
gi 1907177089 302 EQAsLEMR 309
Cdd:cd12161   289 EEA-MEKR 295
PRK13243 PRK13243
glyoxylate reductase; Reviewed
64-335 2.89e-55

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 185.77  E-value: 2.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQI 143
Cdd:PRK13243   59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAW 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 144 REVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEH 223
Cdd:PRK13243  139 HPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESDFVSLHVPLTKE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 224 NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfaQGPLKDAPNLICTPHTAWYSEQ 303
Cdd:PRK13243  218 TYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVVLAPHIGSATFE 295
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907177089 304 ASLEMREAAATEIRRAITGRIPESLrncVNKE 335
Cdd:PRK13243  296 AREGMAELVAENLIAFKRGEVPPTL---VNRE 324
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
11-322 4.40e-55

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 184.80  E-value: 4.40e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  11 VALLDGR---DCTVEmpILKDLATVAFCDAQSTQEIHEKVLNEAVgaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVD 87
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  88 IKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSvEQIREVASGAARIRGETLGLIGFGRTG 167
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 168 QAVAVRAKAFGFSVIFYDPylqDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAAR 247
Cdd:PRK08410  158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907177089 248 GGLVDEKALAQALKEGRIrGAALDVHESEPFSfAQGPL---KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:PRK08410  234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
36-323 2.61e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 182.98  E-value: 2.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  36 DAQSTQEIHEKvLNEAVGAMMyHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVC 115
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 116 HILNLYRRNTWLYQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpyL 188
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 189 QDGIERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGA 268
Cdd:PRK06487  177 GQLPGRPARPDRL-PLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907177089 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 4.54e-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: 182.48  E-value: 4.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12187    53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 QIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqRVYTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12187   133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYT 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEP--------FSFAQGPLKDA----- 288
Cdd:cd12187   205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelFREDVSPEDLKkllad 284
                         250       260
                  ....*....|....*....|..
gi 1907177089 289 ------PNLICTPHTAWYSEQA 304
Cdd:cd12187   285 hallrkPNVIITPHVAYNTKEA 306
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
61-317 8.50e-52

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: 176.48  E-value: 8.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREG---- 134
Cdd:cd12183    55 DLDAPVLEKLAELgvKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGnfsl 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 135 ---TRVQsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERsLGVQRVyTLQDLLYQS 211
Cdd:cd12183   135 dglLGFD--------------LHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAK-LGVEYV-DLDELLAES 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 212 DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG----PLKD 287
Cdd:cd12183   199 DIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDhsdeIIQD 278
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907177089 288 A--------PNLICTPHTAWYSEQAsleMREAAATEIR 317
Cdd:cd12183   279 DvlarllsfPNVLITGHQAFFTKEA---LTNIAETTLE 313
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
58-310 2.23e-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: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  58 HTITLTREDLEKFKAL--RVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAvEETADSTVCHILNLYRRntwlYQALREGT 135
Cdd:cd12185    52 GKSKISAELLEKLKEAgvKYISTRSIGYDHIDLDAAKELGIKVSNVTYSP-NSVADYTVMLMLMALRK----YKQIMKRA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 136 RVQ--SVEQIRevasgAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslGVQRVyTLQDLLYQSDC 213
Cdd:cd12185   127 EVNdySLGGLQ-----GRELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNEEVKK--YAEYV-DLDTLYKESDI 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 214 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQ----------- 282
Cdd:cd12185   199 ITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEDGIYYNdrkgdilsnre 278
                         250       260
                  ....*....|....*....|....*....
gi 1907177089 283 -GPLKDAPNLICTPHTAWYSEQASLEMRE 310
Cdd:cd12185   279 lAILRSFPNVILTPHMAFYTDQAVSDMVE 307
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-341 5.65e-49

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: 169.28  E-value: 5.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKALRVIVRI-GSGYDNVDiKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQs 139
Cdd:cd12167    61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 140 veqiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVQRVyTLQDLLYQSDCVSLHCN 219
Cdd:cd12167   139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSLHAP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 220 LNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLICTPHTAW 299
Cdd:cd12167   214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLP-PDSPLRTLPNVLLTPHIAG 291
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907177089 300 YSEQASLEMREAAATEIRRAITGRIPeslRNCVNKEFFVTSA 341
Cdd:cd12167   292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
61-296 6.93e-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: 165.44  E-value: 6.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRntwLYQALREGTRvqsv 140
Cdd:cd12176    53 QLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARR---LPDRNAAAHR---- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 141 EQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIE--RSLGVQR-VYTLQDLLYQSDCVSLH 217
Cdd:cd12176   126 GIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD------IAekLPLGNARqVSSLEELLAEADFVTLH 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 218 CNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLICT 294
Cdd:cd12176   200 VPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGEPfssPLQGLPNVILT 279

                  ..
gi 1907177089 295 PH 296
Cdd:cd12176   280 PH 281
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
57-314 2.09e-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: 162.88  E-value: 2.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  57 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTR 136
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 137 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVS 215
Cdd:cd05302   149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTP 295
Cdd:cd05302   224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302
                         250
                  ....*....|....*....
gi 1907177089 296 HTAWYSEQAslEMREAAAT 314
Cdd:cd05302   303 HISGTTLDA--QARYAAGT 319
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
62-304 2.96e-46

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 161.51  E-value: 2.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIP---SAAVEEtadstvcHILNL-----YRRNTWLYQALre 133
Cdd:PRK06932   55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTgysSTTVPE-------HVLGMifalkHSLMGWYRDQL-- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 134 GTRVQSVEQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgiERSLGVQRV-YT-LQDLLYQS 211
Cdd:PRK06932  126 SDRWATCKQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREgYTpFEEVLKQA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 212 DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPL----KD 287
Cdd:PRK06932  199 DIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKR 277
                         250
                  ....*....|....*..
gi 1907177089 288 APNLICTPHTAWYSEQA 304
Cdd:PRK06932  278 LPNLLITPHIAWASDSA 294
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
62-313 4.92e-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: 155.32  E-value: 4.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGtrvqsvE 141
Cdd:cd12156    54 LSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------R 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgvQRVYTLQDLLYQSDCVSLHCNLN 221
Cdd:cd12156   128 WPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPY----RYYASLLELAAESDVLVVACPGG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 222 EHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGP--LKDAPNLICTPHTAw 299
Cdd:cd12156   204 PATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIA- 278
                         250
                  ....*....|....
gi 1907177089 300 yseQASLEMREAAA 313
Cdd:cd12156   279 ---SATVETRRAMG 289
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
39-322 7.25e-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: 7.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  39 STQEIHEKVLNeAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHIL 118
Cdd:cd12157    34 SREELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 119 NLYRRntwlyqaLREGTRVqsveqIREVASGAAR-------IRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12157   113 GLGRH-------ILAGDRF-----VRSGKFGGWRpkfygtgLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQ 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 192 I-ERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAAL 270
Cdd:cd12157   181 AeEQALNLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAA 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907177089 271 DVHESE-------PFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 322
Cdd:cd12157   260 DVFEMEdwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
62-296 3.15e-43

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 156.11  E-value: 3.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALrviVRIGS---GYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQ 138
Cdd:PRK11790   65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 139 SveqirevASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDpylqdgIER--SLG-VQRVYTLQDLLYQSDCVS 215
Cdd:PRK11790  142 S-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDklPLGnARQVGSLEELLAQSDVVS 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQG---PLKDAPNLI 292
Cdd:PRK11790  209 LHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDNVI 288

                  ....
gi 1907177089 293 CTPH 296
Cdd:PRK11790  289 LTPH 292
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
38-302 8.13e-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: 152.45  E-value: 8.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  38 QSTQEIhEKVLNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSA---AVEETADSTV 114
Cdd:cd12179    29 ISREEI-LAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGnrdAVGEHALGML 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 115 CHILNLYRRNTWLYQA---LREGTRvqSVEqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG 191
Cdd:cd12179   108 LALFNKLNRADQEVRNgiwDREGNR--GVE-----------LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 192 IERslgVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALD 271
Cdd:cd12179   175 DAY---AEQV-SLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLD 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907177089 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 1.04e-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: 152.40  E-value: 1.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGElGIAVCNIP--SAAVEETAdstVCHILNLYRRNTWLYQALREGTRVQSVE 141
Cdd:cd12165    52 EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHgnSPAVAEHA---LALILALAKRIVEYDNDLRRGIWHGRAG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 QIREVASgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCV 214
Cdd:cd12165   128 EEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVI--------GVSRSpkedEGADFVGTLSDLdeaLEQADVV 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 215 SLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--------HESEPFSFaqgPLK 286
Cdd:cd12165   196 VVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDPVAPSRY---PFH 272
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907177089 287 DAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 325
Cdd:cd12165   273 ELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPL 311
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
62-315 1.23e-41

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 151.36  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  62 LTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRvqsve 141
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 142 QIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPY-LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNL 220
Cdd:PRK07574  179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 221 NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDAPNLICTPHTAWY 300
Cdd:PRK07574  259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQP-APADHPWRTMPRNGMTPHISGT 337
                         250
                  ....*....|....*
gi 1907177089 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 6.51e-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: 144.59  E-value: 6.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  64 REDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCN---IPSAAVeetADSTVCHILNLYRRnTWLYQALREGTRVQSV 140
Cdd:cd05300    51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNargIFGPPI---AEYVLGYMLAFARK-LPRYARNQAERRWQRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 141 EQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL-----GVQRVYT---LQDLLYQSD 212
Cdd:cd05300   127 GPVRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEAD 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 213 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLI 292
Cdd:cd05300   192 YVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVI 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907177089 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 7.65e-40

(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: 145.13  E-value: 7.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKAL---RVIVRIgSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRR-NTWLYQALREGTR 136
Cdd:cd12184    55 FADKENLEIYKEYgikYVFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHtAYTASRTANKNFK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 137 VQSVEQIREvasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSL 216
Cdd:cd12184   134 VDPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKD---VVTFVSLDELLKKSDIISL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 217 HC-NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDV--HESEPF--SFAQGPLKDA--- 288
Cdd:cd12184   204 HVpYIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvve 283
                         250       260
                  ....*....|....*....|....*...
gi 1907177089 289 ------PNLICTPHTAWYSEQASLEMRE 310
Cdd:cd12184   284 klldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
40-333 9.12e-39

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 142.20  E-value: 9.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  40 TQEIHEKVLNEAVGaMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILN 119
Cdd:PRK15409   35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 120 LYRRntwlyqALREGTRVQSVEQIREVASG--AARIRGETLGLIGFGRTGQAVAVRAKaFGFSV-IFYDPYLQ-DGIERS 195
Cdd:PRK15409  114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 196 LGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHES 275
Cdd:PRK15409  187 FNARYC-DLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907177089 276 EPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPEslrNCVN 333
Cdd:PRK15409  266 EPLS-VDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEK---NCVN 319
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
73-304 1.44e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 136.41  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  73 LRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRntwlYQALREGTRVQSveqIREVASGAAR 152
Cdd:PRK08605   70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRH----FNQIQTKVREHD---FRWEPPILSR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 153 -IRGETLGLIGFGRTGQAVA-VRAKAFGFSVIFYDPYLQDGIERSlgVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLIND 230
Cdd:PRK08605  143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATY--VDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 231 FTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESE----PFSFAQGPLKDA--------PNLICTPHTA 298
Cdd:PRK08605  221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                  ....*.
gi 1907177089 299 WYSEQA 304
Cdd:PRK08605  301 FYTDAA 306
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
61-320 1.75e-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: 136.51  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  61 TLTREDLEKFKALrvIVR-----------------IGS---GYDNVDIKAAGELGIAVCNIP---SAAVeetADSTVCHI 117
Cdd:cd12158    28 EITAEDLKDADVL--LVRsvtkvneallegskvkfVGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSAL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 118 LNLYRRNTWLyqalregtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQdgiERSLG 197
Cdd:cd12158   103 LVLAQRQGFS-------------------------LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAEGD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 198 VQRVyTLQDLLYQSDCVSLHCNLNEH----NHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVH 273
Cdd:cd12158   155 PGFV-SLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVW 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907177089 274 ESEPfSFAQGPLKDApnLICTPHTAWYseqaSLEMREAAATEIRRAI 320
Cdd:cd12158   234 ENEP-EIDLELLDKV--DIATPHIAGY----SLEGKARGTEMIYEAL 273
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
151-333 3.12e-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: 3.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 151 ARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS------LGVQRVYTLQDLLYQSDCVSLHCNLNEHN 224
Cdd:cd12180   131 GSLAGSTLGIVGFGAIGQALARRALALGMRVL--------ALRRSgrpsdvPGVEAAADLAELFARSDHLVLAAPLTPET 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 225 HHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQA 304
Cdd:cd12180   203 RHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDG 281
                         170       180
                  ....*....|....*....|....*....
gi 1907177089 305 SLEMREAAATEIRRAITGRipeSLRNCVN 333
Cdd:cd12180   282 RRNLADRFLENLARYRAGQ---PLHDLVD 307
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
66-303 4.10e-35

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: 131.93  E-value: 4.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  66 DLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTrVQSVEQIRE 145
Cdd:cd12155    54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKK-WKMDSSLLE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 146 VAsgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVSLHC 218
Cdd:cd12155   133 LY-------GKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 219 NLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:cd12155   198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                  ....*
gi 1907177089 299 WYSEQ 303
Cdd:cd12155   277 GVSEH 281
PLN02928 PLN02928
oxidoreductase family protein
51-325 4.01e-34

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 130.19  E-value: 4.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  51 AVGAMMyhtiTLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAV---EETADSTVCHILNLYRRNTWL 127
Cdd:PLN02928   65 CVPKMM----RLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTgnaASCAEMAIYLMLGLLRKQNEM 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 128 YQALRegtrvqsveqirevasgaARIRGETLG---------LIGFGRTGQAVAVRAKAFGFSVIFY------DPYLQDGI 192
Cdd:PLN02928  141 QISLK------------------ARRLGEPIGdtlfgktvfILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLI 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 193 ERSLGVQRVY------TLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIR 266
Cdd:PLN02928  203 PNGDVDDLVDekggheDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLG 282
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907177089 267 GAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIP 325
Cdd:PLN02928  283 GLAIDVAWSEPFD-PDDPILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPL 340
PLN02306 PLN02306
hydroxypyruvate reductase
82-324 1.43e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.51  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  82 GYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTRVQSVEQIREvasgAARIRGETLGLI 161
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 162 GFGRTGQAVA-VRAKAFGFSVIFYDPY---------------LQDGIERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNH 225
Cdd:PLN02306  172 GAGRIGSAYArMMVEGFKMNLIYYDLYqstrlekfvtaygqfLKANGEQPVTWKRASSMEEVLREADVISLHPVLDKTTY 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 226 HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQGPLKDAPNLICTPHTAwyseQAS 305
Cdd:PLN02306  252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SAS 325
                         250
                  ....*....|....*....
gi 1907177089 306 LEMREAAATEIRRAITGRI 324
Cdd:PLN02306  326 KWTREGMATLAALNVLGKL 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
57-315 3.32e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 114.56  E-value: 3.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  57 YHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWLYQALREGTR 136
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 137 vqsveQIREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVS 215
Cdd:PLN03139  186 -----NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVVV 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTP 295
Cdd:PLN03139  261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMTP 339
                         250       260
                  ....*....|....*....|
gi 1907177089 296 HTAWYSEQASLemREAAATE 315
Cdd:PLN03139  340 HISGTTIDAQL--RYAAGVK 357
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
67-304 1.35e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 111.93  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  67 LEKFkALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRntwlYQALREgtRVQSVEQIREV 146
Cdd:PRK12480   65 LESY-GIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRR----FPDIER--RVQAHDFTWQA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 147 ASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERslgVQRVYTLQDLLYQSDCVSLHCNLNEHNHH 226
Cdd:PRK12480  138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 227 LINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFA---QGPLKDAP---------NLICT 294
Cdd:PRK12480  215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAYFTndwTNKDIDDKtllelieheRILVT 294
                         250
                  ....*....|
gi 1907177089 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 1.35e-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: 99.88  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  65 EDLEKFKALRVIVRIGSGYDNVDiKAAGELGIAVCNIPSAAVEET-ADSTVCHILNLYRRntwlYQALREGTRVQSVEQI 143
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRD----MDRYAAQQRRGVWKPL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 144 REVASGAARIrgetlGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSL----GVQRVY---TLQDLLYQSDCVsl 216
Cdd:cd12164   126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkdieGVTCFHgeeGLDAFLAQTDIL-- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 217 hCNL---NEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLIC 293
Cdd:cd12164   191 -VCLlplTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTV 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907177089 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 1.36e-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: 99.97  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  63 TREDLEKFKALRVIVRIGSGYDNVdIKAAGElGIAVCNipSAAVEE--TADSTVCHILNLYRRNTWLYQALREG----TR 136
Cdd:cd12166    51 VLEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGLPRFVRAQARGrwepRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 137 VQSVEqirevasgaarirGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDLLYQSD 212
Cdd:cd12166   127 TPSLA-------------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEAD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 213 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRgAALDVHESEPFSfAQGPLKDAPNLI 292
Cdd:cd12166   186 VVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEPLP-PGHPLWSAPGVL 263
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907177089 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 7.57e-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: 7.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 143 IREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIfydpylqdGIERS----LGVQRVYTLQDL---LYQSDCVS 215
Cdd:cd12159   113 PAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVV 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 216 LHCNLNEHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsFAQG-PLKDAPNLICT 294
Cdd:cd12159   185 LAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALIT 262

                  ....
gi 1907177089 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 2.84e-20

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 90.51  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 162 GFGRTGQAVAVRAKAFGFSVIfydpylqdGIERSLGVQ---RVYT---LQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQ 235
Cdd:cd12160   150 GFGSIGQRLAPLLTALGARVT--------GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAA 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 236 MRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMreaAATE 315
Cdd:cd12160   222 LPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLP-ASSPLWDAPNLILTPHAAGGRPQGAEEL---IAEN 297
                         170
                  ....*....|....*
gi 1907177089 316 IRRAITGRipeSLRN 330
Cdd:cd12160   298 LRAFLAGG---PLRN 309
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
59-301 5.73e-20

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 90.87  E-value: 5.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  59 TIT-LTREDLEKFKaLRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLyrrntwlyqALREGtrv 137
Cdd:PRK00257   45 SVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTL---------AEREG--- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 138 qsveqirevasgaARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGIERSLGVqrvyTLQDLLYQSDCVSLH 217
Cdd:PRK00257  112 -------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFV----SLERILEECDVISLH 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 218 CNLN-EHNH---HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfsfaQGPLKDAPN-LI 292
Cdd:PRK00257  175 TPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTI 250

                  ....*....
gi 1907177089 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 1.63e-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: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 125 TWL-----YQALREGTRVQSVEQiREVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFY--------------- 184
Cdd:cd12163    99 TWLvlshhFLQYIELQKEQTWGR-RQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkddg 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 185 -------DPylqDGI--------ERSLGVQRVYTLQ-DLLyqsdCVSLhcNLNEHNHHLIN--DFTIKQMRqGAFLVNAA 246
Cdd:cd12163   178 yivpgtgDP---DGSipsawfsgTDKASLHEFLRQDlDLL----VVSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIA 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907177089 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 2.16e-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: 76.19  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  38 QSTQEIHEKVlNEAVGAMMYHTITLTREDLEKFKALRVIVRIGSGYD----NVDIKAAGELGIAVCNIPSAAVEETADST 113
Cdd:cd12170    35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 114 VCH---ILNLYRRNTWLYQALRegtrvqsveqirevasgaarIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD 190
Cdd:cd12170   114 ISElirLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 191 GIERSlGVqRVYTLQDLLYQSDCVSLHCNlneHNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGrirGAAL 270
Cdd:cd12170   174 DAEAK-GI-RYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907177089 271 DVHESEPfSFAQGPLKDAPNLICTPHTAWYSEQA 304
Cdd:cd12170   246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
54-324 1.48e-13

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 71.48  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  54 AMMYHTITLTREDLEKFKALRVIVRIGSGYDNVDIKAAGELGIAVCNIPSAAVEETADSTVCHILNLYRRNTWlyqALRE 133
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 134 gtrvqsveqirevasgaarirgETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD-GIERSLgvqrvYTLQDLLYQSD 212
Cdd:PRK15438  117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQEAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 213 CVSLHCNLNEHNH----HLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPfSFAQGPLKDA 288
Cdd:PRK15438  170 ILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKV 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907177089 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 1907177089 155 GETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDGierslGVQRVY-TLQDLLYQSDCVSLHCNLNEHNHHLINDFTI 233
Cdd:PRK06436  122 NKSLGILGYGGIGRRVALLAKAFGMNIYAYTRSYVND-----GISSIYmEPEDIMKKSDFVLISLPLTDETRGMINSKML 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 234 KQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPlkdaPNLICTPHTAwysEQASLEMREAAA 313
Cdd:PRK06436  197 SLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHVA---GGMSGEIMQPAV 269
                         170       180
                  ....*....|....*....|..
gi 1907177089 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 2.02e-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: 64.56  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  66 DLEKFKALRVIVRIGSGYDNVDIK-AAGELGIAVCNIPsaaveetadsTVCHILNLYRRNTWLYQALREGTRVQSVeQIR 144
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTeALARAGLTAIAVE----------GVELPLLTSNSIGAGELSVQFIARFLEV-QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 145 EVASGAARIRGETLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQDG-IERSLGVQRVYTLQDLLYQSDCVSLHCNLNEH 223
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALeQLEELGGKNVEELEEALAEADVIVTTTLLPGK 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 224 NHHLINDFT-IKQMRQGAFLVNAARG-GLVDEKALAQALKEGRIRGAALDVHESEPFSFAQGPLKDAPNL 291
Cdd:cd12154   230 RAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
71-321 1.27e-10

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 62.12  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089  71 KALRVIVRIGSGYDNV--DIKAAGELGIAvcNIPSAAVEETA------DSTVCHILNLYRRNTwLYQALREGTRVQSVEQ 142
Cdd:PRK15469   55 RDLKAVFALGAGVDSIlsKLQAHPEMLDP--SVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 143 IRevasgaariRGE-TLGLIGFGRTGQAVAVRAKAFGFSVIFYDPYLQD--GIERSLGVQRvytLQDLLYQSDC-VSLHC 218
Cdd:PRK15469  132 YH---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGREE---LSAFLSQTRVlINLLP 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907177089 219 NLNEhNHHLINDFTIKQMRQGAFLVNAARGGLVDEKALAQALKEGRIRGAALDVHESEPFSfAQGPLKDAPNLICTPHTA 298
Cdd:PRK15469  200 NTPE-TVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVA 277
                         250       260
                  ....*....|....*....|...
gi 1907177089 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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