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Conserved domains on  [gi|1838075539|ref|XP_033948962|]
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C-terminal-binding protein 1 [Pseudochaenichthys georgianus]

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 ...
46-364 2.39e-149

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: 427.70  E-value: 2.39e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  46 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKGLRIIVRIGSGYD 121
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 122 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 201
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 202 RVGQAVALRAKAFGFNVIFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 281
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 282 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRI 361
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1838075539 362 PDS 364
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 ...
46-364 2.39e-149

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: 427.70  E-value: 2.39e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  46 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKGLRIIVRIGSGYD 121
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 122 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 201
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 202 RVGQAVALRAKAFGFNVIFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 281
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 282 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRI 361
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1838075539 362 PDS 364
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
48-371 3.78e-98

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 297.39  E-value: 3.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDI 125
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 126 KSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGLIGLGRVGQ 205
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 206 AVALRAKAFGFNVIFYDPYLADGVERsLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 285
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 286 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPdsl 365
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1838075539 366 KNCVNK 371
Cdd:COG1052   311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
48-370 4.73e-83

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 258.37  E-value: 4.73e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKGLRIIVRIGSGYDNIDIK 126
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 127 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGLIGLGRVGQA 206
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 207 VALRAKAFGFNVIFYDPYLADGVERSLGLQRVTTLQDLLF---HSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 283
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 284 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPd 363
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1838075539 364 slKNCVN 370
Cdd:pfam00389 307 --ANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
78-374 4.04e-58

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 194.63  E-value: 4.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  78 QEIHEKVLNEAV---GALmyhtITLM-----REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADS 149
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLseridCEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 150 TLCHILTLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGV 229
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 230 ERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 309
Cdd:PRK13243  188 EKELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838075539 310 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPDSLkncVNKEFL 374
Cdd:PRK13243  267 FEEEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNREVV 326
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
46-364 2.39e-149

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: 427.70  E-value: 2.39e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  46 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKGLRIIVRIGSGYD 121
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 122 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 201
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 202 RVGQAVALRAKAFGFNVIFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 281
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 282 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRI 361
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1838075539 362 PDS 364
Cdd:cd05299   310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
48-355 1.50e-108

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: 323.43  E-value: 1.50e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRDCTVEMPILKD-VATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIK 126
Cdd:cd05198     2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 127 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRvqsveqIREVASGAARIRGETLGLIGLGRVGQA 206
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 207 VALRAKAFGFNVIFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGG 286
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVVS-LDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838075539 287 LVDEKALAQALKEGRIRGAALDVHETEPFSFSqGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRR 355
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
48-371 3.78e-98

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 297.39  E-value: 3.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDI 125
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 126 KSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGLIGLGRVGQ 205
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 206 AVALRAKAFGFNVIFYDPYLADGVERsLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 285
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 286 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPdsl 365
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1838075539 366 KNCVNK 371
Cdd:COG1052   311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
67-370 1.42e-96

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: 293.25  E-value: 1.42e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  67 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEET 146
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 147 ADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLA 226
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 227 DGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAA 306
Cdd:COG0111   175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838075539 307 LDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRipdSLKNCVN 370
Cdd:COG0111   255 LDVFEPEPLPADS-PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
76-356 2.94e-88

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


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 271.67  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  76 STQEIHEKvLNEAVGAL-MYHTITlmREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHI 154
Cdd:cd12172    37 TEEELIEL-LKDADGVIaGLDPIT--EEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 155 LTLYRRTTWLHQALREG--TRVQSVEqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERS 232
Cdd:cd12172   114 LALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 233 LGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 312
Cdd:cd12172   183 HGVEFVS-LEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEE 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1838075539 313 EPFSfSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRA 356
Cdd:cd12172   262 EPPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
101-360 4.70e-88

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: 270.83  E-value: 4.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGT----RVQS 176
Cdd:cd12173    54 AEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFMG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 177 VEqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERSLGlQRVTTLQDLLFHSDCVSLHCS 256
Cdd:cd12173   134 VE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISLHTP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 257 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAW 336
Cdd:cd12173   202 LTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLGA 280
                         250       260
                  ....*....|....*....|....
gi 1838075539 337 YSEQASLEMREEAAREIRRAITGR 360
Cdd:cd12173   281 STEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
48-370 4.73e-83

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 258.37  E-value: 4.73e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKGLRIIVRIGSGYDNIDIK 126
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 127 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGLIGLGRVGQA 206
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 207 VALRAKAFGFNVIFYDPYLADGVERSLGLQRVTTLQDLLF---HSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 283
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 284 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPd 363
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1838075539 364 slKNCVN 370
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
99-362 4.16e-79

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: 248.26  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  99 LMREDLEK-FKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqsv 177
Cdd:cd12175    54 VIDAELLAaAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG------ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 178 EQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY-LADGVERSLGLQRVTtLQDLLFHSDCVSLHCS 256
Cdd:cd12175   128 RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYVE-LDELLAESDVVSLHVP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 257 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAW 336
Cdd:cd12175   207 LTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDD-PLLRLDNVILTPHIAG 285
                         250       260
                  ....*....|....*....|....*.
gi 1838075539 337 YSEQASLEMREEAAREIRRAITGRIP 362
Cdd:cd12175   286 VTDESYQRMAAIVAENIARLLRGEPP 311
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
101-370 1.27e-77

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: 244.45  E-value: 1.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqsveqi 180
Cdd:cd12178    57 KEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRG--------- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 181 reVASGAAR-------IRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY-LADGVERSLGLQRVTtLQDLLFHSDCVS 252
Cdd:cd12178   128 --GFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD-LDELLKESDFVS 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 253 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGpLKDAPNLICTP 332
Cdd:cd12178   205 LHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVILTP 282
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1838075539 333 HAAWYSEQASLEMREEAAREIRRAITGRIPdslKNCVN 370
Cdd:cd12178   283 HIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
107-359 9.73e-74

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


Pssm-ID: 240645 [Multi-domain]  Cd Length: 321  Bit Score: 234.75  E-value: 9.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 107 FKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEqirevASG 186
Cdd:cd12168    74 PPSLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 187 AARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY-LADGVERSLGLqRVTTLQDLLFHSDCVSLHCSLNEHNHHLI 265
Cdd:cd12168   149 AHDPRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALAT-YYVSLDELLAQSDVVSLNCPLTAATRHLI 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 266 NDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFsFSQGpLKDAPNLICTPHAAWYSEQASLEM 345
Cdd:cd12168   228 NKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPE-VNPG-LLKMPNVTLLPHMGTLTVETQEKM 305
                         250
                  ....*....|....
gi 1838075539 346 REEAAREIRRAITG 359
Cdd:cd12168   306 EELVLENIEAFLET 319
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
48-360 3.87e-72

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


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 230.65  E-value: 3.87e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGRDctVEMPILKDVA-----TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDN 122
Cdd:cd01619     3 VLIYDYRD--DELEIEKEILkaggvDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 123 IDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGR 202
Cdd:cd01619    81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRE-------LEDQTVGVVGTGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 203 VGQAVALRAKAFGFNVIFYDPYLADGVERSLGlqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNT 282
Cdd:cd01619   154 IGRAVAQRAKGFGMKVIAYDPFRNPELEDKGV--KYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 283 ARGGLVDEKALAQALKEGRIRGAALDVHETE-----------PFSFSQGP-LKDAPNLICTPHAAWYSEQASLEMREEAA 350
Cdd:cd01619   232 ARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISC 311
                         330
                  ....*....|
gi 1838075539 351 REIRRAITGR 360
Cdd:cd01619   312 ENIVDFLEGE 321
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
101-347 6.76e-72

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


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 229.26  E-value: 6.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQ- 179
Cdd:cd12162    57 AEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPDFc 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 180 -----IREVAsgaarirGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVerslGLQRVTtLQDLLFHSDCVSLH 254
Cdd:cd12162   137 fwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYVS-LDELLAQSDVISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 255 CSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsqgP------LKDAPNL 328
Cdd:cd12162   205 CPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplLKAAPNL 278
                         250
                  ....*....|....*....
gi 1838075539 329 ICTPHAAWyseqASLEMRE 347
Cdd:cd12162   279 IITPHIAW----ASREARQ 293
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
60-359 1.17e-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: 228.82  E-value: 1.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  60 MPILKDVATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVC 136
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 137 NMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGF 216
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAG----EWKGWSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 217 NVIFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 296
Cdd:cd05301   169 KILYHNRSRKPEAEEELGARYVS-LDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEA 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 297 LKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITG 359
Cdd:cd05301   248 LKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
101-333 1.78e-69

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: 222.80  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqsveQI 180
Cdd:cd05303    55 KEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG-------KW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 181 REVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEH 260
Cdd:cd05303   128 NKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTVS-LEELLKNSDFISLHVPLTPE 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 261 NHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgpLKDAPNLICTPH 333
Cdd:cd05303   207 TKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
151-335 8.40e-68

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 214.28  E-value: 8.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 151 LCHILTLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGV 229
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 230 ERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 309
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 1838075539 310 HETEPFSFSQgPLKDAPNLICTPHAA 335
Cdd:pfam02826 154 FEPEPLPADH-PLLDLPNVILTPHIA 178
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
49-367 8.04e-67

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: 216.80  E-value: 8.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  49 ALLDGRDCTVEMPILKDVATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLMREDLEKFKGLRIIVRIGSGYDN 122
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 123 IDIKSAGELGIAVCNMPAA----SVEETAdstLCHILTLYRRTTWLHQALREGtrvqsveQIREVASGAAR-IRGETLGL 197
Cdd:cd12177    83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 198 IGLGRVGQAVA-LRAKAFGFNVIFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQG 276
Cdd:cd12177   153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPVS-LEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 277 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRA 356
Cdd:cd12177   232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADH-PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                         330
                  ....*....|.
gi 1838075539 357 ITGRIPDSLKN 367
Cdd:cd12177   311 LAGKEPKGILN 321
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
79-355 8.39e-66

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


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 213.94  E-value: 8.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  79 EIHEKVLNEAVGA--LMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILT 156
Cdd:cd12171    35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 157 LYRRTTWLHQALREGtrvqsveQIREVASGAAR----IRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYlADGVERS 232
Cdd:cd12171   115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPY-VDPEKIE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 233 LGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 312
Cdd:cd12171   187 ADGVKKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1838075539 313 EPFSfSQGPLKDAPNLICTPHAAWYSEQA---SLEMreeAAREIRR 355
Cdd:cd12171   267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
101-370 6.77e-65

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


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 211.27  E-value: 6.77e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRttwLHQALREGTRVQSVEQI 180
Cdd:cd12174    42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRN---IIQAIKWVTNGDGDDIS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 181 REVASGAAR-----IRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLAdgVERSLGL----QRVTTLQDLLFHSDCV 251
Cdd:cd12174   119 KGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLS--VEAAWKLsvevQRVTSLEELLATADYI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 252 SLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEpfsfsqgPLKDAPNLICT 331
Cdd:cd12174   197 TLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIAT 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1838075539 332 PHAAWYSEQASLEMREEAAREIRRAI-TGRIPdslkNCVN 370
Cdd:cd12174   270 PHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
PRK13243 PRK13243
glyoxylate reductase; Reviewed
78-374 4.04e-58

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 194.63  E-value: 4.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  78 QEIHEKVLNEAV---GALmyhtITLM-----REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADS 149
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLseridCEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 150 TLCHILTLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGV 229
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 230 ERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 309
Cdd:PRK13243  188 EKELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838075539 310 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPDSLkncVNKEFL 374
Cdd:PRK13243  267 FEEEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNREVV 326
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
57-360 4.56e-58

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


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 194.42  E-value: 4.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  57 TVEMPILKDVATVaFCDAqstqeihekvlnEAVGALMYHTITlmREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVC 136
Cdd:cd12187    26 FTSQELLDDNVEE-FKDA------------EVISVFVYSRLD--AEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 137 NMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGF 216
Cdd:cd12187    91 NVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFE-------LAGKTLGVVGTGRIGRRVARIARGFGM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 217 NVIFYDPYLADGVERSLGLqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 296
Cdd:cd12187   164 KVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 297 LKEGRIRGAALDVHETEPF----------SFSQGPLKDA---------PNLICTPHAAWYSEQASLEMREEAAREIRRAI 357
Cdd:cd12187   243 LKEGKLAGAGLDVLEQEEVlreeaelfreDVSPEDLKKLladhallrkPNVIITPHVAYNTKEALERILDTTVENIKAFA 322

                  ...
gi 1838075539 358 TGR 360
Cdd:cd12187   323 AGQ 325
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
48-359 3.55e-57

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 191.35  E-value: 3.55e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  48 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLMREDLEKFKGLRIIVRIGSGYDNID 124
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 125 IKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSvEQIREVASGAARIRGETLGLIGLGRVG 204
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 205 QAVALRAKAFGFNVIFYDPylaDGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTAR 284
Cdd:PRK08410  158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838075539 285 GGLVDEKALAQALKEGRIrGAALDVHETEPFSfSQGPL---KDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITG 359
Cdd:PRK08410  234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
76-359 8.67e-57

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: 190.82  E-value: 8.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  76 STQEIHEKVLNEAVGA---LMYHTITLMREDLEKFK--GLRII-VRIgSGYDNIDIKSAGELGIAVCNMPAASVEETADS 149
Cdd:cd12186    30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAeyGIKQIaLRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 150 TLCHILTLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADG 228
Cdd:cd12186   109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 229 VErSLGLQrVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALD 308
Cdd:cd12186   182 LE-KFLLY-YDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 309 VHETE----PFSFSQGPLKDA--------PNLICTPHAAWYSEQASLEMREEAAREIRRAITG 359
Cdd:cd12186   260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEG 322
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
61-359 5.22e-56

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


Pssm-ID: 240646 [Multi-domain]  Cd Length: 308  Bit Score: 188.10  E-value: 5.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  61 PILKDVATV-AFCDaqstqeiHEKVLNEAVGALM-YHTITLMRED-------LEKFKGLRIIVRIGSGYDNIDIKSAGEL 131
Cdd:cd12169    19 SKLDDRAEVtVFND-------HLLDEDALAERLApFDAIVLMRERtpfpaalLERLPNLKLLVTTGMRNASIDLAAAKER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 132 GIAVCNmPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVeqirevasgAARIRGETLGLIGLGRVGQAVALRA 211
Cdd:cd12169    92 GIVVCG-TGGGPTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 212 KAFGFNVIFYDPYLADGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEK 291
Cdd:cd12169   162 QAFGMRVIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEG 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838075539 292 ALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITG 359
Cdd:cd12169   242 ALLAALRAGRIAGAALDVFDVEPLPADH-PLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
60-350 1.31e-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: 187.43  E-value: 1.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  60 MPILKDVATVAFCDAQSTQEihEKVLNEAVGA--LMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCN 137
Cdd:cd12161    20 APLEEQGHEFVYYDTKTTDT--AELIERSKDAdiVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 138 MPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQiREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFN 217
Cdd:cd12161    98 AAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 218 VIFYDPYLADGVErSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQAL 297
Cdd:cd12161   170 VLAYSRSEKEEAK-ALGIEYVS-LDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADAL 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 298 KEGRIRGAALDVHETEPFSFSQGPLKDAPNLICTPHAAWYSEQAsLEMREEAA 350
Cdd:cd12161   248 NEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFATEEA-MEKRAEIV 299
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
119-341 3.33e-55

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


Pssm-ID: 240659  Cd Length: 328  Bit Score: 186.50  E-value: 3.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 119 GYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTtwlHQAlregtrvqsveqirevasgAARIR------- 191
Cdd:cd12183    78 GFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKI---HRA-------------------YNRVRegnfsld 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 192 --------GETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERSLGlqRVTTLQDLLFHSDCVSLHCSLNEHNHH 263
Cdd:cd12183   136 gllgfdlhGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAKLGV--EYVDLDELLAESDIISLHCPLTPETHH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 264 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSF----SQGPLKDA--------PNLICT 331
Cdd:cd12183   214 LINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFfedhSDEIIQDDvlarllsfPNVLIT 293
                         250
                  ....*....|
gi 1838075539 332 PHAAWYSEQA 341
Cdd:cd12183   294 GHQAFFTKEA 303
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
73-360 9.35e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 182.59  E-value: 9.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  73 DAQSTQEIHEKvLNEAVGALMyHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLC 152
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 153 HILTLYRRTTWLHQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGLGRVGQAVALRAKAFGFNVIfydpyL 225
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 226 ADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGA 305
Cdd:PRK06487  177 GQLPGRPARPDRLP-LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1838075539 306 ALDVHETEPfSFSQGPL--KDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGR 360
Cdd:PRK06487  256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
69-354 6.63e-50

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 172.39  E-value: 6.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  69 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLMREDLEKFK--GLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAaSVEE 145
Cdd:cd12185    27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKeaGVKYISTRSIGYDHIDLDAAKELGIKVSNVTY-SPNS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 146 TADSTLCHILTLYRRTTW-LHQALREGTRVQSVeQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY 224
Cdd:cd12185   104 VADYTVMLMLMALRKYKQiMKRAEVNDYSLGGL-QGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 225 LADGVERslGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRG 304
Cdd:cd12185   176 PNEEVKK--YAEYVD-LDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGG 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 305 AALDVHETEPFSFSQ------------GPLKDAPNLICTPHAAWYSEQASLEMREEAAREIR 354
Cdd:cd12185   253 AALDVIEGEDGIYYNdrkgdilsnrelAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLV 314
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
119-355 2.09e-47

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


Pssm-ID: 240653  Cd Length: 304  Bit Score: 165.44  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 119 GYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqsveQIREVASGAARIRGETLGLI 198
Cdd:cd12176    74 GTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG-------IWNKSATGSHEVRGKTLGII 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 199 GLGRVGQAVALRAKAFGFNVIFYD--PYLADGVERslglqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQG 276
Cdd:cd12176   147 GYGHIGSQLSVLAEALGMRVIFYDiaEKLPLGNAR-----QVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKG 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 277 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFS----FSQgPLKDAPNLICTPHAAWYSEQASLEMREEAARE 352
Cdd:cd12176   222 AILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngepFSS-PLQGLPNVILTPHIGGSTEEAQENIGLEVAGK 300

                  ...
gi 1838075539 353 IRR 355
Cdd:cd12176   301 LVK 303
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
98-372 2.89e-47

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: 165.81  E-value: 2.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  98 TLMREDLEKFKGLRIIVRI-GSGYDNIDiKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQs 176
Cdd:cd12167    61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 177 veqiREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCS 256
Cdd:cd12167   139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVS-LDELLARSDVVSLHAP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 257 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPFSFSQgPLKDAPNLICTPHAAW 336
Cdd:cd12167   214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLPPDS-PLRTLPNVLLTPHIAG 291
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1838075539 337 YSEQASLEMREEAAREIRRAITGRIPdslKNCVNKE 372
Cdd:cd12167   292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPE 324
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
99-353 1.17e-46

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 163.82  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  99 LMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTL-YRRTTWLHQALreGTRVQSV 177
Cdd:PRK06932   55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALkHSLMGWYRDQL--SDRWATC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 178 EQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFydpylADGVERSLGLQRVTTLQDLLFHSDCVSLHCSL 257
Cdd:PRK06932  133 KQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLY-----AEHKGASVCREGYTPFEEVLKQADIVTLHCPL 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 258 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPL----KDAPNLICTPH 333
Cdd:PRK06932  208 TETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLPNLLITPH 286
                         250       260
                  ....*....|....*....|
gi 1838075539 334 AAWYSEQASLEMREEAAREI 353
Cdd:PRK06932  287 IAWASDSAVTTLVNKVAQNI 306
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
94-333 1.48e-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: 164.42  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  94 YHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTR 173
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 174 vqsveQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY-LADGVERSLGLQRVTTLQDLLFHSDCVS 252
Cdd:cd05302   149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 253 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDAPNLICTP 332
Cdd:cd05302   224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302

                  .
gi 1838075539 333 H 333
Cdd:cd05302   303 H 303
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
104-347 2.15e-46

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240633 [Multi-domain]  Cd Length: 301  Bit Score: 162.64  E-value: 2.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 104 LEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtrvqsvEQIREV 183
Cdd:cd12156    59 IAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------RWPKGA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 184 ASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVerslGLQRVTTLQDLLFHSDCVSLHCSLNEHNHH 263
Cdd:cd12156   133 FPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDV----PYRYYASLLELAAESDVLVVACPGGPATRH 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 264 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGP--LKDAPNLICTPHAAWYSEQA 341
Cdd:cd12156   209 LVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIASATVET 284

                  ....*.
gi 1838075539 342 SLEMRE 347
Cdd:cd12156   285 RRAMGD 290
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
76-359 1.60e-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: 158.22  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  76 STQEIHEKVLN-EAVGALMYHTITlmREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHI 154
Cdd:cd12157    34 SREELLRRCKDaDGLMAFMPDRID--ADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 155 LTLYRRTTWLHQALREGTRvqsvEQIREVASGAArIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGV-ERSL 233
Cdd:cd12157   112 IGLGRHILAGDRFVRSGKF----GGWRPKFYGTG-LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAeEQAL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 234 GLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE 313
Cdd:cd12157   187 NLRRVE-LDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 314 -------PFSFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITG 359
Cdd:cd12157   266 dwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
75-339 1.88e-44

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: 157.45  E-value: 1.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  75 QSTQEIHEKVlnEAVGALMYHTITLM-REDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCH 153
Cdd:cd12179    29 ISREEILAII--PQYDGLIIRSRFPIdKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 154 ILTLyrrttwLHQALREGTRVQSVEQIREVASGAaRIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYladgveRSL 233
Cdd:cd12179   107 LLAL------FNKLNRADQEVRNGIWDREGNRGV-ELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKY------KNF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 234 GLQRV--TTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHE 311
Cdd:cd12179   174 GDAYAeqVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLE 253
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1838075539 312 TEPFSF---SQGP-----LKDAPNLICTPH-AAWYSE 339
Cdd:cd12179   254 YEKASFesiFNQPeafeyLIKSPKVILTPHiAGWTFE 290
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
101-347 6.29e-43

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240660  Cd Length: 330  Bit Score: 154.37  E-value: 6.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFK--GLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTT-WLHQALREGTRVQSV 177
Cdd:cd12184    58 KENLEIYKeyGIKYVFTRTVGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAyTASRTANKNFKVDPF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 178 EQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVErslglQRVT--TLQDLLFHSDCVSLHC 255
Cdd:cd12184   138 MFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAK-----DVVTfvSLDELLKKSDIISLHV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 256 S-LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--HETEPF--SFSQGPLKDA----- 325
Cdd:cd12184   206 PyIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvvekl 285
                         250       260
                  ....*....|....*....|....*.
gi 1838075539 326 ----PNLICTPHAAWYSEQASLEMRE 347
Cdd:cd12184   286 ldlyPRVLLTPHIGSYTDEALSNMIE 311
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
82-363 7.57e-43

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: 153.55  E-value: 7.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  82 EKVLNEAvGALMYHTITLmREDLEKFKGLRIIVRIGSGYDNIDIKSAGElGIAVCNMPAASvEETADSTLCHILTLYRRT 161
Cdd:cd12165    35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHGNS-PAVAEHALALILALAKRI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 162 TWLHQALREGTRVQSVEQIREVASgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYD--PYLADGVERSLGlqrVT 239
Cdd:cd12165   111 VEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGT---LS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 240 TLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--------HE 311
Cdd:cd12165   184 DLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDP 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 312 TEPFSFsqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPD 363
Cdd:cd12165   264 VAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
99-353 7.67e-42

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 152.91  E-value: 7.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  99 LMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRvqsve 178
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 179 QIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPY-LADGVERSLGLQRVTTLQDLLFHSDCVSLHCSL 257
Cdd:PRK07574  179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 258 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHetepfsFSQGPLKD-----APNLICTP 332
Cdd:PRK07574  259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVW------FPQPAPADhpwrtMPRNGMTP 332
                         250       260
                  ....*....|....*....|..
gi 1838075539 333 HAAWYSEQAslEMREEA-AREI 353
Cdd:PRK07574  333 HISGTTLSA--QARYAAgTREI 352
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
99-333 2.46e-40

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 149.17  E-value: 2.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  99 LMREDLEKFKGLriiVRIGS---GYDNIDIKSAGELGIAVCNMPAA---SVEETAdstLCHILTLYRRTTWLHQALREGT 172
Cdd:PRK11790   65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSntrSVAELV---IGEIILLLRGIPEKNAKAHRGG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 173 RVQSveqirevASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDpyladgVERSLGL---QRVTTLQDLLFHSD 249
Cdd:PRK11790  139 WNKS-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDKLPLgnaRQVGSLEELLAQSD 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 250 CVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQG---PLKDAP 326
Cdd:PRK11790  206 VVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLD 285

                  ....*..
gi 1838075539 327 NLICTPH 333
Cdd:PRK11790  286 NVILTPH 292
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
100-372 2.16e-37

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: 138.81  E-value: 2.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 100 MREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGtRVQSVEQ 179
Cdd:cd05300    50 LPELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAER-RWQRRGP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 180 IREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIfydpyladGVERSL-----GLQRVTT---LQDLLFHSDCV 251
Cdd:cd05300   129 VRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEADYV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 252 SLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICT 331
Cdd:cd05300   194 VNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVIIT 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1838075539 332 PHAAWYSEqaslEMREEAA----REIRRAITGRipdSLKNCVNKE 372
Cdd:cd05300   273 PHISGDSP----SYPERVVeiflENLRRYLAGE---PLLNVVDKD 310
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
77-374 3.84e-37

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 138.35  E-value: 3.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  77 TQEIHEKVLNEAVGaLMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILT 156
Cdd:PRK15409   35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 157 LYRRttwlhqALREGTRVQSVEQIREVASG--AARIRGETLGLIGLGRVGQAVALRAKaFGFN--VIFYDPYLADGVERS 232
Cdd:PRK15409  114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNmpILYNARRHHKEAEER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 233 LGlQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 312
Cdd:PRK15409  187 FN-ARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 313 EPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPdslKNCVNKEFL 374
Cdd:PRK15409  266 EPLSVDS-PLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVNPQVA 323
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
116-338 4.66e-37

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


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 138.82  E-value: 4.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 116 IGS---GYDNIDIKSAGELGIAVCNMP---AASVeetADSTLCHILTLYRRTTWLhqalregtrvqsveqirevasgaar 189
Cdd:cd12158    61 VGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSALLVLAQRQGFS------------------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 190 IRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLAdgvERSlGLQRVTTLQDLLFHSDCVSLHCSLNEH----NHHLI 265
Cdd:cd12158   113 LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAE-GDPGFVSLEELLAEADIITLHVPLTRDgehpTYHLL 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838075539 266 NDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDApnLICTPHAAWYS 338
Cdd:cd12158   189 DEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP-EIDLELLDKV--DIATPHIAGYS 258
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
109-341 4.08e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 136.03  E-value: 4.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 109 GLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREgtrvqsvEQIREVASGAA 188
Cdd:PRK08605   69 GIKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVRE-------HDFRWEPPILS 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 189 R-IRGETLGLIGLGRVGQAVA-LRAKAFGFNVIFYDPYLADGVERSLglQRVTTLQDLLFHSDCVSLHCSLNEHNHHLIN 266
Cdd:PRK08605  142 RsIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATYV--DYKDTIEEAVEGADIVTLHMPATKYNHYLFN 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 267 DFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICTPHA 334
Cdd:PRK08605  220 ADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHI 299

                  ....*..
gi 1838075539 335 AWYSEQA 341
Cdd:PRK08605  300 AFYTDAA 306
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
103-340 1.14e-34

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 131.55  E-value: 1.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 103 DLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRttwLHQALRegtrvQSVEQIRE 182
Cdd:cd12155    54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKG---LKKAYK-----NQKEKKWK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 183 VASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIfydpyladGVERS----LGLQRVTTLQDL---LFHSDCVSLHC 255
Cdd:cd12155   126 MDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 256 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAA 335
Cdd:cd12155   198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                  ....*
gi 1838075539 336 WYSEQ 340
Cdd:cd12155   277 GVSEH 281
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
188-360 5.28e-33

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: 126.69  E-value: 5.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 188 ARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYD----PYLADGVERslglqrVTTLQDLLFHSDCVSLHCSLNEHNHH 263
Cdd:cd12180   131 GSLAGSTLGIVGFGAIGQALARRALALGMRVLALRrsgrPSDVPGVEA------AADLAELFARSDHLVLAAPLTPETRH 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 264 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSEQASL 343
Cdd:cd12180   205 LINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDGRR 283
                         170
                  ....*....|....*..
gi 1838075539 344 EMREEAAREIRRAITGR 360
Cdd:cd12180   284 NLADRFLENLARYRAGQ 300
PLN02306 PLN02306
hydroxypyruvate reductase
119-411 8.11e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 125.36  E-value: 8.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 119 GYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIREvasgAARIRGETLGLI 198
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 199 GLGRVGQAVA-LRAKAFGFNVIFYDPYLADGVERSLGL---------------QRVTTLQDLLFHSDCVSLHCSLNEHNH 262
Cdd:PLN02306  172 GAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEKFVTAygqflkangeqpvtwKRASSMEEVLREADVISLHPVLDKTTY 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 263 HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsFSQGPLKDAPNLICTPHAAwyseQAS 342
Cdd:PLN02306  252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SAS 325
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 343 LEMREEAAREIRRAITGRIpdslkncvnKEFLSQNNhwtgvePATVHPELNGAYRYP---PGVVNLPAGGLP 411
Cdd:PLN02306  326 KWTREGMATLAALNVLGKL---------KGYPVWGD------PNRVEPFLNENAPPPaasPSIVNAKALGLP 382
PLN02928 PLN02928
oxidoreductase family protein
100-366 1.16e-30

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 121.33  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 100 MRED---LEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAA---SVEETADSTLCHILTLYRRttwlHQALRegtr 173
Cdd:PLN02928   70 MRLDadiIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRK----QNEMQ---- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 174 vQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERSLGLQRVTT------------L 241
Cdd:PLN02928  142 -ISLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVddlvdekgghedI 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 242 QDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgP 321
Cdd:PLN02928  221 YEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDD-P 299
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1838075539 322 LKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAITGRIPDSLK 366
Cdd:PLN02928  300 ILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIE 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
94-333 1.81e-29

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 118.80  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  94 YHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRR--TTWlHQALREG 171
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNflPGY-HQVVSGE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 172 TRVQsveqirEVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADG-VERSLGLQRVTTLQDLLFHSDC 250
Cdd:PLN03139  185 WNVA------GIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDV 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 251 VSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLIC 330
Cdd:PLN03139  259 VVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAM 337

                  ...
gi 1838075539 331 TPH 333
Cdd:PLN03139  338 TPH 340
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
104-341 3.74e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 111.16  E-value: 3.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 104 LEKFkGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWLHQalregtRVQSVEQIREV 183
Cdd:PRK12480   65 LESY-GIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIER------RVQAHDFTWQA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 184 ASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLADGVERslgLQRVTTLQDLLFHSDCVSLHCSLNEHNHH 263
Cdd:PRK12480  138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 264 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICT 331
Cdd:PRK12480  215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayfTNDWTNKDIDDKtlleliehERILVT 294
                         250
                  ....*....|
gi 1838075539 332 PHAAWYSEQA 341
Cdd:PRK12480  295 PHIAFFSDEA 304
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
102-357 5.24e-25

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: 104.50  E-value: 5.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 102 EDLEKFKGLRIIVRIGSGYDNIDiKSAGELGIAVCNMPAASVEET-ADSTLCHILTLYRRTTwlhqALREGTRVQSVEQI 180
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRDMD----RYAAQQRRGVWKPL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 181 REVASGAARIrgetlGLIGLGRVGQAVALRAKAFGFNVIfydpyladGVERSL-GLQRVTT------LQDLLFHSDCVSL 253
Cdd:cd12164   126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkDIEGVTCfhgeegLDAFLAQTDILVC 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 254 HCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPH 333
Cdd:cd12164   193 LLPLTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTVTPH 271
                         250       260
                  ....*....|....*....|....
gi 1838075539 334 AawyseqASLEMREEAAREIRRAI 357
Cdd:cd12164   272 I------AAITDPDSAAAQVAENI 289
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
119-358 1.85e-23

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 101.65  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 119 GYDNIDIKSAGELGIAVCNMP---AASVeetADSTLCHILTLyrrttwlhqALREGtrvqsveqirevasgaARIRGETL 195
Cdd:PRK00257   68 GTDHLDLDYFAEAGITWSSAPgcnARGV---VDYVLGSLLTL---------AEREG----------------VDLAERTY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 196 GLIGLGRVGQAVALRAKAFGFNVIFYDPYLADgverSLGLQRVTTLQDLLFHSDCVSLHCSLN-EHNH---HLINDFTIK 271
Cdd:PRK00257  120 GVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQE----AEGDGDFVSLERILEECDVISLHTPLTkEGEHptrHLLDEAFLA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 272 QMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGPLKDAPN-LICTPHAAWYseqaSLEMREEAA 350
Cdd:PRK00257  196 SLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTIATPHIAGY----SLDGKARGT 267

                  ....*...
gi 1838075539 351 REIRRAIT 358
Cdd:PRK00257  268 AQIYQALC 275
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
101-365 1.46e-22

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: 97.28  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 101 REDLEKFKGLRIIVRIGSGYDNIdIKSAGElGIAVCNmpAASVEE--TADSTLCHILTLYRRttwLHQALREGTRVQ-SV 177
Cdd:cd12166    52 LEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRG---LPRFVRAQARGRwEP 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 178 EQIREVAsgaarirGETLGLIGLGRVGQAVALRAKAFGFNVIfydpyladGVERS----LGLQRVTTLQDLLFHSDCVSL 253
Cdd:cd12166   125 RRTPSLA-------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEADVVVL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 254 HCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPfsFSQG-PLKDAPNLICTP 332
Cdd:cd12166   190 IVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEP--LPPGhPLWSAPGVLITP 266
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1838075539 333 HAAWYSEQASLEMREEAAREIRRAITGRIPDSL 365
Cdd:cd12166   267 HVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
147-360 8.74e-22

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 95.52  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 147 ADSTLCHILTLYRRTTWLHQALREGTRVQSV--EQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIfydpy 224
Cdd:cd12160    96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT----- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 225 ladGVERSLGLQ---RVTT---LQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALK 298
Cdd:cd12160   171 ---GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALE 247
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 299 EGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMreeAAREIRRAITGR 360
Cdd:cd12160   248 SGRLGGAALDVTATEPLPASS-PLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
132-335 2.98e-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: 93.87  E-value: 2.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 132 GIAVCNMPAASVEETADSTLCHILTLYRRttwLHQALREGTRVQSveqirEVASGAARIRGETLGLIGLGRVGQAVALRA 211
Cdd:cd12159    73 GRRWTNAAGAYAETVAEHALALLLAGLRQ---LPARARATTWDPA-----EEDDLVTLLRGSTVAIVGAGGIGRALIPLL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 212 KAFGFNVIfydpyladGVERS----LGLQRVTTLQDL---LFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTAR 284
Cdd:cd12159   145 APFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVAR 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1838075539 285 GGLVDEKALAQALKEGRIRGAALDVHETEPfsFSQG-PLKDAPNLICTPHAA 335
Cdd:cd12159   217 GPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
191-339 1.12e-17

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 83.86  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 191 RGETLGLIGLGRVGQAVALRAKAFGFNVIFY----------------------DPylaDGV--------ERSLGLQRVTT 240
Cdd:cd12163   132 VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkddgyivpgtgDP---DGSipsawfsgTDKASLHEFLR 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 241 LQ-DLLFhsdcVSLhcSLNEHNHHLIN--DFTIKQMRqGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSf 317
Cdd:cd12163   209 QDlDLLV----VSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLP- 280
                         170       180
                  ....*....|....*....|..
gi 1838075539 318 SQGPLKDAPNLICTPHAAWYSE 339
Cdd:cd12163   281 ADHPLWSAPNVIITPHVSWQTQ 302
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
91-338 6.00e-15

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 76.10  E-value: 6.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  91 ALMYHTITLMREDLEKFKGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRTTWlhqALRE 170
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 171 gtrvqsveqirevasgaarirgETLGLIGLGRVGQAVALRAKAFGFNVIFYDPYLAD-GVERSLglqrvTTLQDLLFHSD 249
Cdd:PRK15438  117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQEAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 250 CVSLHCSLNEHNH----HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDA 325
Cdd:PRK15438  170 ILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKV 248
                         250
                  ....*....|...
gi 1838075539 326 PnlICTPHAAWYS 338
Cdd:PRK15438  249 D--IGTPHIAGYT 259
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
108-383 1.05e-14

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 74.53  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 108 KGLRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEeTADSTLCHILTLYRRTTWLHQALREGTRVQSVEQIrevasga 187
Cdd:PRK06436   48 KKTKMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSIS-VAEHAFALLLAWAKNICENNYNMKNGNFKQSPTKL------- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 188 arIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYD-PYLADGVERSlglqrVTTLQDLLFHSDCVSLHCSLNEHNHHLIN 266
Cdd:PRK06436  120 --LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTrSYVNDGISSI-----YMEPEDIMKKSDFVLISLPLTDETRGMIN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 267 DFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPlkdaPNLICTPH-AAWYSEQASLEM 345
Cdd:PRK06436  193 SKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHvAGGMSGEIMQPA 268
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1838075539 346 REEAAREIRRAITGRiPdslKNCVNK-EFLSQNNHWTGV 383
Cdd:PRK06436  269 VALAFENIKNFFEGK-P---KNIVRKeEYIVRSERFLGI 303
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
75-341 1.73e-14

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


Pssm-ID: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 73.87  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539  75 QSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKGLRIIVRIGSGYD----NIDIKSAGELGIAVCNMPA---ASVEETA 147
Cdd:cd12170    35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 148 DSTLCHILTLYRRTTWLHQALRegtrvqsveqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYD----- 222
Cdd:cd12170   114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSrtrkp 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 223 PYLADGVerslglqRVTTLQDLLFHSDCVSLHcsLNEhNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGri 302
Cdd:cd12170   174 DAEAKGI-------RYLPLNELLKTVDVICTC--LPK-NVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS-- 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1838075539 303 rGAALDVHETEPfSFSQGPLKDAPNLICTPHAAWYSEQA 341
Cdd:cd12170   242 -GYNIFDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
103-328 2.01e-13

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: 70.72  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 103 DLEKFKGLRIIVRIGSGYDNIDIKSA-GELGIavcnmPAASVEETADSTLCHILTLYRRttwlhQALREGTRVQSVeQIR 181
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTEAlARAGL-----TAIAVEGVELPLLTSNSIGAGE-----LSVQFIARFLEV-QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 182 EVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVIFYD-PYLADGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEH 260
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDiNVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGK 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 261 NHHLINDFT-IKQMRQGAFLVNTARG-GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPLKDAPNL 328
Cdd:cd12154   230 RAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
264-358 7.14e-09

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 57.11  E-value: 7.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838075539 264 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSEQAsl 343
Cdd:PRK15469  207 IINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVAAVTRPA-- 283
                          90
                  ....*....|....*
gi 1838075539 344 emreEAAREIRRAIT 358
Cdd:PRK15469  284 ----EAVEYISRTIA 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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