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Conserved domains on  [gi|2106618234|ref|XP_043982674|]
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C-terminal-binding protein 1 isoform X1 [Gambusia affinis]

Protein Classification

C-terminal binding protein( domain architecture ID 10143094)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 3.20e-147

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


:

Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 421.54  E-value: 3.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGYD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 104 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 184 RVGQAVALRAKAFGFNVVFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2106618234 344 PDS 346
Cdd:cd05299   310 PRN 312
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 3.20e-147

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 421.54  E-value: 3.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGYD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 104 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 184 RVGQAVALRAKAFGFNVVFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2106618234 344 PDS 346
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 4.24e-97

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


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 293.92  E-value: 4.24e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDI 107
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 108 KSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIrevasgAARIRGETLGLIGLGRVGQ 187
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 188 AVALRAKAFGFNVVFYDPYLADGVERsLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 267
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 268 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPdsl 347
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 2106618234 348 KNCVNK 353
Cdd:COG1052   311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 6.44e-82

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 254.91  E-value: 6.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKALRIIVRIGSGYDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 109 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREVasgaariRGETLGLIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 189 VALRAKAFGFNVVFYDPYLADGVERSLGLQRVTTLQDLLF---HSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 266 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 2106618234 346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-356 2.47e-58

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 194.63  E-value: 2.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  60 QEIHEKVLNEAV---GALmyhtITLMRE--DLEKFKA---LRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADS 131
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLSEriDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 132 TLCHILTLYRRITWLHQALREGTRVQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGV 211
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 212 ERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:PRK13243  188 EKELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2106618234 292 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPDSLkncVNKEFL 356
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 ...
28-346 3.20e-147

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 421.54  E-value: 3.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGYD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 104 NIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVeqirevASGAARIRGETLGLIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 184 RVGQAVALRAKAFGFNVVFYDPYLADGVERsLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAA-LGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2106618234 344 PDS 346
Cdd:cd05299   310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
30-337 1.11e-107

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 320.73  E-value: 1.11e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRDCTVEMPILKD-VATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIK 108
Cdd:cd05198     2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 109 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRvqsveqIREVASGAARIRGETLGLIGLGRVGQA 188
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 189 VALRAKAFGFNVVFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGG 268
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVVS-LDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2106618234 269 LVDEKALAQALKEGRIRGAALDVHETEPFSFSqGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRR 337
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 4.24e-97

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


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 293.92  E-value: 4.24e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDI 107
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 108 KSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIrevasgAARIRGETLGLIGLGRVGQ 187
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 188 AVALRAKAFGFNVVFYDPYLADGVERsLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 267
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYVS-LDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 268 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPdsl 347
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 2106618234 348 KNCVNK 353
Cdd:COG1052   311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
49-352 5.96e-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: 290.94  E-value: 5.96e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  49 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEET 128
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 129 ADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLA 208
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 209 DGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAA 288
Cdd:COG0111   175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2106618234 289 LDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRipdSLKNCVN 352
Cdd:COG0111   255 LDVFEPEPLPADS-PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
58-338 1.97e-87

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: 268.97  E-value: 1.97e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  58 STQEIHEKvLNEAVGAL-MYHTITlmREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHI 136
Cdd:cd12172    37 TEEELIEL-LKDADGVIaGLDPIT--EEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 137 LTLYRRITWLHQALREG--TRVQSVEqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERS 214
Cdd:cd12172   114 LALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 215 LGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:cd12172   183 HGVEFVS-LEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEE 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2106618234 295 EPFSfSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRA 338
Cdd:cd12172   262 EPPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
83-342 2.01e-87

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: 268.90  E-value: 2.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGT----RVQS 158
Cdd:cd12173    54 AEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFMG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 159 VEqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERSLGlQRVTTLQDLLFHSDCVSLHCS 238
Cdd:cd12173   134 VE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISLHTP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 239 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAW 318
Cdd:cd12173   202 LTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLGA 280
                         250       260
                  ....*....|....*....|....
gi 2106618234 319 YSEQASLEMREEAAREIRRAVTGR 342
Cdd:cd12173   281 STEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 6.44e-82

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 254.91  E-value: 6.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKALRIIVRIGSGYDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 109 SAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREVasgaariRGETLGLIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 189 VALRAKAFGFNVVFYDPYLADGVERSLGLQRVTTLQDLLF---HSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 266 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 2106618234 346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
83-344 3.25e-78

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


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 245.56  E-value: 3.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqsvEQI 162
Cdd:cd12175    57 AELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG------RWG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 163 REVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPY-LADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNE 241
Cdd:cd12175   131 RPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYVE-LDELLAESDVVSLHVPLTP 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 242 HNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSE 321
Cdd:cd12175   210 ETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDD-PLLRLDNVILTPHIAGVTD 288
                         250       260
                  ....*....|....*....|...
gi 2106618234 322 QASLEMREEAAREIRRAVTGRIP 344
Cdd:cd12175   289 ESYQRMAAIVAENIARLLRGEPP 311
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
83-352 7.69e-78

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


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 244.84  E-value: 7.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqsveqi 162
Cdd:cd12178    57 KEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRG--------- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 163 reVASGAAR-------IRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPY-LADGVERSLGLQRVTtLQDLLFHSDCVS 234
Cdd:cd12178   128 --GFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYVD-LDELLKESDFVS 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGpLKDAPNLICTP 314
Cdd:cd12178   205 LHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVILTP 282
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2106618234 315 HAAWYSEQASLEMREEAAREIRRAVTGRIPdslKNCVN 352
Cdd:cd12178   283 HIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
92-341 1.20e-72

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: 231.28  E-value: 1.20e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  92 LRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEqirevASGAAR 171
Cdd:cd12168    77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 172 IRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPY-LADGVERSLGLqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDF 250
Cdd:cd12168   152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALAT-YYVSLDELLAQSDVVSLNCPLTAATRHLINKK 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 251 TIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFsFSQGpLKDAPNLICTPHAAWYSEQASLEMREE 330
Cdd:cd12168   231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPE-VNPG-LLKMPNVTLLPHMGTLTVETQEKMEEL 308
                         250
                  ....*....|.
gi 2106618234 331 AAREIRRAVTG 341
Cdd:cd12168   309 VLENIEAFLET 319
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
42-341 5.04e-72

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: 229.59  E-value: 5.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  42 MPILKDVATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVC 118
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 119 NMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGF 198
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAG----EWKGWSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 199 NVVFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 278
Cdd:cd05301   169 KILYHNRSRKPEAEEELGARYVS-LDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEA 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 279 LKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTG 341
Cdd:cd05301   248 LKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
83-329 6.03e-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: 6.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQ- 161
Cdd:cd12162    57 AEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPDFc 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 162 -----IREVAsgaarirGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVerslGLQRVTtLQDLLFHSDCVSLH 236
Cdd:cd12162   137 fwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYVS-LDELLAQSDVISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 237 CSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsqgP------LKDAPNL 310
Cdd:cd12162   205 CPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplLKAAPNL 278
                         250
                  ....*....|....*....
gi 2106618234 311 ICTPHAAWyseqASLEMRE 329
Cdd:cd12162   279 IITPHIAW----ASREARQ 293
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
30-342 3.42e-70

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


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 225.26  E-value: 3.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGRDctVEMPILKDVA-----TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYDN 104
Cdd:cd01619     3 VLIYDYRD--DELEIEKEILkaggvDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 105 IDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGR 184
Cdd:cd01619    81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRE-------LEDQTVGVVGTGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 185 VGQAVALRAKAFGFNVVFYDPYLADGVERSLGlqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNT 264
Cdd:cd01619   154 IGRAVAQRAKGFGMKVIAYDPFRNPELEDKGV--KYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 265 ARGGLVDEKALAQALKEGRIRGAALDVHETE-----------PFSFSQGP-LKDAPNLICTPHAAWYSEQASLEMREEAA 332
Cdd:cd01619   232 ARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISC 311
                         330
                  ....*....|
gi 2106618234 333 REIRRAVTGR 342
Cdd:cd01619   312 ENIVDFLEGE 321
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
83-315 8.69e-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: 220.87  E-value: 8.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqsveQI 162
Cdd:cd05303    55 KEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG-------KW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 163 REVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEH 242
Cdd:cd05303   128 NKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTVS-LEELLKNSDFISLHVPLTPE 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 243 NHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgpLKDAPNLICTPH 315
Cdd:cd05303   207 TKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
133-317 1.92e-67

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


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 213.13  E-value: 1.92e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 133 LCHILTLYRRITWLHQALREGT-RVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGV 211
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 212 ERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 2106618234 292 HETEPFSFSQgPLKDAPNLICTPHAA 317
Cdd:pfam02826 154 FEPEPLPADH-PLLDLPNVILTPHIA 178
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
31-349 3.04e-66

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 214.88  E-value: 3.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  31 ALLDGRDCTVEMPILKDVATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLMREDLEKFKALRIIVRIGSGYDN 104
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 105 IDIKSAGELGIAVCNMPAA----SVEETAdstLCHILTLYRRITWLHQALREGtrvqsveQIREVASGAAR-IRGETLGL 179
Cdd:cd12177    83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 180 IGLGRVGQAVA-LRAKAFGFNVVFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQG 258
Cdd:cd12177   153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPVS-LEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 259 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRA 338
Cdd:cd12177   232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADH-PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                         330
                  ....*....|.
gi 2106618234 339 VTGRIPDSLKN 349
Cdd:cd12177   311 LAGKEPKGILN 321
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-337 1.84e-65

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


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 212.40  E-value: 1.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  61 EIHEKVLNEAVGA--LMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILT 138
Cdd:cd12171    35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 139 LYRRITWLHQALREGtrvqsveQIREVASGAAR----IRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYlADGVERS 214
Cdd:cd12171   115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPY-VDPEKIE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 215 LGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:cd12171   187 ADGVKKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2106618234 295 EPFSfSQGPLKDAPNLICTPHAAWYSEQA---SLEMreeAAREIRR 337
Cdd:cd12171   267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
83-352 5.89e-65

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


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 210.88  E-value: 5.89e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITwlhQALREGTRVQSVEQI 162
Cdd:cd12174    42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNII---QAIKWVTNGDGDDIS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 163 REVASGAAR-----IRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLAdgVERSLGL----QRVTTLQDLLFHSDCV 233
Cdd:cd12174   119 KGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLS--VEAAWKLsvevQRVTSLEELLATADYI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 234 SLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEpfsfsqgPLKDAPNLICT 313
Cdd:cd12174   197 TLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIAT 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2106618234 314 PHAAWYSEQASLEMREEAAREIRRAV-TGRIPdslkNCVN 352
Cdd:cd12174   270 PHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
39-342 2.28e-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: 194.80  E-value: 2.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  39 TVEMPILKDVATVaFCDAqstqeihekvlnEAVGALMYHTITlmREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVC 118
Cdd:cd12187    26 FTSQELLDDNVEE-FKDA------------EVISVFVYSRLD--AEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 119 NMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGF 198
Cdd:cd12187    91 NVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFE-------LAGKTLGVVGTGRIGRRVARIARGFGM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 199 NVVFYDPYLADGVERSLGLqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 278
Cdd:cd12187   164 KVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 279 LKEGRIRGAALDVHETEPF----------SFSQGPLKDA---------PNLICTPHAAWYSEQASLEMREEAAREIRRAV 339
Cdd:cd12187   243 LKEGKLAGAGLDVLEQEEVlreeaelfreDVSPEDLKKLladhallrkPNVIITPHVAYNTKEALERILDTTVENIKAFA 322

                  ...
gi 2106618234 340 TGR 342
Cdd:cd12187   323 AGQ 325
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-356 2.47e-58

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 194.63  E-value: 2.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  60 QEIHEKVLNEAV---GALmyhtITLMRE--DLEKFKA---LRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADS 131
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLSEriDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 132 TLCHILTLYRRITWLHQALREGTRVQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGV 211
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 212 ERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:PRK13243  188 EKELGAEYRP-LEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2106618234 292 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPDSLkncVNKEFL 356
Cdd:PRK13243  267 FEEEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNREVV 326
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 2.02e-57

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 191.74  E-value: 2.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  30 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLMREDLEKFKALRIIVRIGSGYDNID 106
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 107 IKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSvEQIREVASGAARIRGETLGLIGLGRVG 186
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 187 QAVALRAKAFGFNVVFYDPylaDGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTAR 266
Cdd:PRK08410  158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERVS-LEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2106618234 267 GGLVDEKALAQALKEGRIrGAALDVHETEPFSfSQGPL---KDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTG 341
Cdd:PRK08410  234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
58-335 3.55e-56

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: 188.90  E-value: 3.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  58 STQEIHEKVLNEAVGA---LMYHTITLMREDLEKFKAL---RIIVRIgSGYDNIDIKSAGELGIAVCNMPAASVEETADS 131
Cdd:cd12186    30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEYgikQIALRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 132 TLCHILTLYRRITWLHQALREGT-RVQSVEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADG 210
Cdd:cd12186   109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 211 VErSLGLQrVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALD 290
Cdd:cd12186   182 LE-KFLLY-YDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 291 VHETE----PFSFSQGPLKDA--------PNLICTPHAAWYSEQASLEMRE---EAAREI 335
Cdd:cd12186   260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEislDDALEI 319
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
43-341 3.98e-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: 3.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  43 PILKDVATV-AFCDaqstqeiHEKVLNEAVGALM-YHTITLMRED-------LEKFKALRIIVRIGSGYDNIDIKSAGEL 113
Cdd:cd12169    19 SKLDDRAEVtVFND-------HLLDEDALAERLApFDAIVLMRERtpfpaalLERLPNLKLLVTTGMRNASIDLAAAKER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 114 GIAVCNmPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVeqirevasgAARIRGETLGLIGLGRVGQAVALRA 193
Cdd:cd12169    92 GIVVCG-TGGGPTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 194 KAFGFNVVFYDPYLADGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEK 273
Cdd:cd12169   162 QAFGMRVIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEG 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2106618234 274 ALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTG 341
Cdd:cd12169   242 ALLAALRAGRIAGAALDVFDVEPLPADH-PLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
42-332 4.04e-56

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


Pssm-ID: 240638 [Multi-domain]  Cd Length: 315  Bit Score: 188.20  E-value: 4.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  42 MPILKDVATVAFCDAQSTQEihEKVLNEAVGA--LMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCN 119
Cdd:cd12161    20 APLEEQGHEFVYYDTKTTDT--AELIERSKDAdiVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 120 MPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQiREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFN 199
Cdd:cd12161    98 AAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 200 VVFYDPYLADGVErSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQAL 279
Cdd:cd12161   170 VLAYSRSEKEEAK-ALGIEYVS-LDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADAL 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 280 KEGRIRGAALDVHETEPFSFSQGPLKDAPNLICTPHAAWYSEQAsLEMREEAA 332
Cdd:cd12161   248 NEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFATEEA-MEKRAEIV 299
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
88-323 2.02e-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: 186.88  E-value: 2.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  88 KFKALRIivrigSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRItwlHQAlregtrvqsveqirevas 167
Cdd:cd12183    70 KLIALRC-----AGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKI---HRA------------------ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 168 gAARIR---------------GETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERSLGlqRVTTLQDLLFHSDC 232
Cdd:cd12183   124 -YNRVRegnfsldgllgfdlhGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAKLGV--EYVDLDELLAESDI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 233 VSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSF----SQGPLKDA- 307
Cdd:cd12183   201 ISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFfedhSDEIIQDDv 280
                         250       260
                  ....*....|....*....|...
gi 2106618234 308 -------PNLICTPHAAWYSEQA 323
Cdd:cd12183   281 larllsfPNVLITGHQAFFTKEA 303
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
55-342 6.75e-54

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 182.59  E-value: 6.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  55 DAQSTQEIHEKvLNEAVGALMyHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLC 134
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 135 HILTLYRRITWLHQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGLGRVGQAVALRAKAFGFNVVfydpyL 207
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 208 ADGVERSLGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGA 287
Cdd:PRK06487  177 GQLPGRPARPDRLP-LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2106618234 288 ALDVHETEPfSFSQGPL--KDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGR 342
Cdd:PRK06487  256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
51-336 3.12e-49

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: 170.47  E-value: 3.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  51 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLMREDLEKFKAL-------RIIvrigsGYDNIDIKSAGELGIAVCNMPA 122
Cdd:cd12185    27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVTY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 123 aSVEETADSTLCHILTLYRRITW-LHQALREGTRVQSVeQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVV 201
Cdd:cd12185   100 -SPNSVADYTVMLMLMALRKYKQiMKRAEVNDYSLGGL-QGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCKIL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 202 FYDPYLADGVERslGLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKE 281
Cdd:cd12185   171 AYDPYPNEEVKK--YAEYVD-LDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLES 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2106618234 282 GRIRGAALDVHETEPFSFSQ------------GPLKDAPNLICTPHAAWYSEQASLEMREEAAREIR 336
Cdd:cd12185   248 GKIGGAALDVIEGEDGIYYNdrkgdilsnrelAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLV 314
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
86-329 2.68e-48

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: 167.26  E-value: 2.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  86 LEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqsvEQIREV 165
Cdd:cd12156    59 IAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------RWPKGA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 166 ASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVerslGLQRVTTLQDLLFHSDCVSLHCSLNEHNHH 245
Cdd:cd12156   133 FPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDV----PYRYYASLLELAAESDVLVVACPGGPATRH 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGP--LKDAPNLICTPHAAWYSEQA 323
Cdd:cd12156   209 LVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIASATVET 284

                  ....*.
gi 2106618234 324 SLEMRE 329
Cdd:cd12156   285 RRAMGD 290
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
101-337 6.78e-48

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


Pssm-ID: 240653  Cd Length: 304  Bit Score: 166.21  E-value: 6.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 101 GYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtrvqsveQIREVASGAARIRGETLGLI 180
Cdd:cd12176    74 GTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG-------IWNKSATGSHEVRGKTLGII 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 181 GLGRVGQAVALRAKAFGFNVVFYD--PYLADGVERslglqRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQG 258
Cdd:cd12176   147 GYGHIGSQLSVLAEALGMRVIFYDiaEKLPLGNAR-----QVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKG 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 259 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFS----FSQgPLKDAPNLICTPHAAWYSEQASLEMREEAARE 334
Cdd:cd12176   222 AILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngepFSS-PLQGLPNVILTPHIGGSTEEAQENIGLEVAGK 300

                  ...
gi 2106618234 335 IRR 337
Cdd:cd12176   301 LVK 303
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
81-335 3.59e-47

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 164.97  E-value: 3.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  81 LMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTL-YRRITWLHQALreGTRVQSV 159
Cdd:PRK06932   55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALkHSLMGWYRDQL--SDRWATC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 160 EQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFydpylADGVERSLGLQRVTTLQDLLFHSDCVSLHCSL 239
Cdd:PRK06932  133 KQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLY-----AEHKGASVCREGYTPFEEVLKQADIVTLHCPL 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 240 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPL----KDAPNLICTPH 315
Cdd:PRK06932  208 TETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLPNLLITPH 286
                         250       260
                  ....*....|....*....|
gi 2106618234 316 AAWYSEQASLEMREEAAREI 335
Cdd:PRK06932  287 IAWASDSAVTTLVNKVAQNI 306
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
80-354 7.37e-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: 164.27  E-value: 7.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  80 TLMREDLEKFKALRIIVRI-GSGYDNIDiKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQs 158
Cdd:cd12167    61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 159 veqiREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERSLGLQRVTtLQDLLFHSDCVSLHCS 238
Cdd:cd12167   139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELVS-LDELLARSDVVSLHAP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 239 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPFSFSQgPLKDAPNLICTPHAAW 318
Cdd:cd12167   214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLPPDS-PLRTLPNVLLTPHIAG 291
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2106618234 319 YSEQASLEMREEAAREIRRAVTGRIPdslKNCVNKE 354
Cdd:cd12167   292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPE 324
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
76-315 3.76e-46

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


Pssm-ID: 240627  Cd Length: 348  Bit Score: 162.88  E-value: 3.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  76 YHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTR 155
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 156 vqsveQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPY-LADGVERSLGLQRVTTLQDLLFHSDCVS 234
Cdd:cd05302   149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDAPNLICTP 314
Cdd:cd05302   224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302

                  .
gi 2106618234 315 H 315
Cdd:cd05302   303 H 303
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
58-341 2.06e-45

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 160.15  E-value: 2.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  58 STQEIHEKVLN-EAVGALMYHTITlmREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHI 136
Cdd:cd12157    34 SREELLRRCKDaDGLMAFMPDRID--ADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 137 LTLYRRITWLHQALREGTRvqsvEQIREVASGAArIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGV-ERSL 215
Cdd:cd12157   112 IGLGRHILAGDRFVRSGKF----GGWRPKFYGTG-LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAeEQAL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 216 GLQRVTtLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE 295
Cdd:cd12157   187 NLRRVE-LDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 296 -------PFSFSQGPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTG 341
Cdd:cd12157   266 dwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
57-321 1.56e-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: 1.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  57 QSTQEIHEKVlnEAVGALMYHTITLM-REDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCH 135
Cdd:cd12179    29 ISREEILAII--PQYDGLIIRSRFPIdKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 136 ILTLYRRITWLHQALREGtrvqsvEQIREVASGAaRIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYladgveRSL 215
Cdd:cd12179   107 LLALFNKLNRADQEVRNG------IWDREGNRGV-ELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKY------KNF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 216 GLQRV--TTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHE 293
Cdd:cd12179   174 GDAYAeqVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLE 253
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2106618234 294 TEPFSF---SQGP-----LKDAPNLICTPH-AAWYSE 321
Cdd:cd12179   254 YEKASFesiFNQPeafeyLIKSPKVILTPHiAGWTFE 290
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
64-345 2.42e-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: 154.71  E-value: 2.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  64 EKVLNEAvGALMYHTITLmREDLEKFKALRIIVRIGSGYDNIDIKSAGElGIAVCNMPAASvEETADSTLCHILTLYRRI 143
Cdd:cd12165    35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHGNS-PAVAEHALALILALAKRI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 144 TWLHQALREGTRVQSVEQIREVASgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYD--PYLADGVERSLGlqrVT 221
Cdd:cd12165   111 VEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGT---LS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 222 TLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--------HE 293
Cdd:cd12165   184 DLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsrgDP 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2106618234 294 TEPFSFsqgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPD 345
Cdd:cd12165   264 VAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
83-329 1.26e-41

(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: 150.52  E-value: 1.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRI---IVRIgSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRIT-WLHQALREGTRVQS 158
Cdd:cd12184    58 KENLEIYKEYGIkyvFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAyTASRTANKNFKVDP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 159 VEQIREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVErslglQRVT--TLQDLLFHSDCVSLH 236
Cdd:cd12184   137 FMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAK-----DVVTfvSLDELLKKSDIISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 237 CS-LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--HETEPF--SFSQGPLKDA---- 307
Cdd:cd12184   205 VPyIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvvek 284
                         250       260
                  ....*....|....*....|....*..
gi 2106618234 308 -----PNLICTPHAAWYSEQASLEMRE 329
Cdd:cd12184   285 lldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
81-335 1.41e-41

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 151.75  E-value: 1.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  81 LMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRvqsve 160
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 161 QIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPY-LADGVERSLGLQRVTTLQDLLFHSDCVSLHCSL 239
Cdd:PRK07574  179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 240 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHetepfsFSQGPLKD-----APNLICTP 314
Cdd:PRK07574  259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVW------FPQPAPADhpwrtMPRNGMTP 332
                         250       260
                  ....*....|....*....|..
gi 2106618234 315 HAAWYSEQAslEMREEA-AREI 335
Cdd:PRK07574  333 HISGTTLSA--QARYAAgTREI 352
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
105-315 2.75e-41

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 151.48  E-value: 2.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 105 IDIKSAGELGIAVCNMPAA---SVEETAdstLCHILTLYRRITWLHQALREGTRVQSveqirevASGAARIRGETLGLIG 181
Cdd:PRK11790   89 VDLDAAAKRGIPVFNAPFSntrSVAELV---IGEIILLLRGIPEKNAKAHRGGWNKS-------AAGSFEVRGKTLGIVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 182 LGRVGQAVALRAKAFGFNVVFYDpyladgVERSLGL---QRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQG 258
Cdd:PRK11790  159 YGHIGTQLSVLAESLGMRVYFYD------IEDKLPLgnaRQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPG 232
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 259 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQG---PLKDAPNLICTPH 315
Cdd:PRK11790  233 AILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDNVILTPH 292
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
59-356 3.85e-37

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 138.35  E-value: 3.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  59 TQEIHEKVLNEAVGaLMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILT 138
Cdd:PRK15409   35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 139 LYRRITWLHQalregtRVQSVEQIREVASG--AARIRGETLGLIGLGRVGQAVALRAKaFGFNV-VFYDPYLA-DGVERS 214
Cdd:PRK15409  114 TARRVVEVAE------RVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 215 LGlQRVTTLQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:PRK15409  187 FN-ARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2106618234 295 EPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPdslKNCVNKEFL 356
Cdd:PRK15409  266 EPLSVDS-PLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVNPQVA 323
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
82-354 5.18e-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: 137.65  E-value: 5.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  82 MREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGtRVQSVEQ 161
Cdd:cd05300    50 LPELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAER-RWQRRGP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 162 IREvasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVfydpyladGVERSL-----GLQRVTT---LQDLLFHSDCV 233
Cdd:cd05300   129 VRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEADYV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 234 SLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICT 313
Cdd:cd05300   194 VNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVIIT 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2106618234 314 PHAAWYSEqaslEMREEAA----REIRRAVTGRipdSLKNCVNKE 354
Cdd:cd05300   273 PHISGDSP----SYPERVVeiflENLRRYLAGE---PLLNVVDKD 310
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
98-320 1.22e-36

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


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 137.28  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  98 IGS---GYDNIDIKSAGELGIAVCNMP---AASVeetADSTLCHILTLYRRITWLhqalregtrvqsveqirevasgaar 171
Cdd:cd12158    61 VGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSALLVLAQRQGFS------------------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 172 IRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLAdgvERSlGLQRVTTLQDLLFHSDCVSLHCSLNEH----NHHLI 247
Cdd:cd12158   113 LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAE-GDPGFVSLEELLAEADIITLHVPLTRDgehpTYHLL 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 248 NDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDApnLICTPHAAWYS 320
Cdd:cd12158   189 DEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP-EIDLELLDKV--DIATPHIAGYS 258
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
92-323 9.23e-36

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 134.87  E-value: 9.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  92 LRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREgtrvqsvEQIREVASGAAR 171
Cdd:PRK08605   70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVRE-------HDFRWEPPILSR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 172 -IRGETLGLIGLGRVGQAVA-LRAKAFGFNVVFYDPYLADGVERSLglQRVTTLQDLLFHSDCVSLHCSLNEHNHHLIND 249
Cdd:PRK08605  143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATYV--DYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 250 FTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICTPHAA 317
Cdd:PRK08605  221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                  ....*.
gi 2106618234 318 WYSEQA 323
Cdd:PRK08605  301 FYTDAA 306
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
85-322 1.97e-34

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


Pssm-ID: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 130.78  E-value: 1.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  85 DLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRItwlHQALRegtrvQSVEQIRE 164
Cdd:cd12155    54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGL---KKAYK-----NQKEKKWK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 165 VASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVfydpyladGVERS----LGLQRVTTLQDL---LFHSDCVSLHC 237
Cdd:cd12155   126 MDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 238 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAA 317
Cdd:cd12155   198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                  ....*
gi 2106618234 318 WYSEQ 322
Cdd:cd12155   277 GVSEH 281
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
170-342 3.93e-32

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


Pssm-ID: 240657  Cd Length: 308  Bit Score: 124.38  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 170 ARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYD----PYLADGVERslglqrVTTLQDLLFHSDCVSLHCSLNEHNHH 245
Cdd:cd12180   131 GSLAGSTLGIVGFGAIGQALARRALALGMRVLALRrsgrPSDVPGVEA------AADLAELFARSDHLVLAAPLTPETRH 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSEQASL 325
Cdd:cd12180   205 LINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDGRR 283
                         170
                  ....*....|....*..
gi 2106618234 326 EMREEAAREIRRAVTGR 342
Cdd:cd12180   284 NLADRFLENLARYRAGQ 300
PLN02306 PLN02306
hydroxypyruvate reductase
101-343 1.23e-31

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 124.58  E-value: 1.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 101 GYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTRVQSVEQIREvasgAARIRGETLGLI 180
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 181 GLGRVGQAVA-LRAKAFGFNVVFYDPYLADGVERSLGL---------------QRVTTLQDLLFHSDCVSLHCSLNEHNH 244
Cdd:PLN02306  172 GAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEKFVTAygqflkangeqpvtwKRASSMEEVLREADVISLHPVLDKTTY 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 245 HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsFSQGPLKDAPNLICTPHAAwyseQAS 324
Cdd:PLN02306  252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SAS 325
                         250
                  ....*....|....*....
gi 2106618234 325 LEMREEAAREIRRAVTGRI 343
Cdd:PLN02306  326 KWTREGMATLAALNVLGKL 344
PLN02928 PLN02928
oxidoreductase family protein
82-348 8.71e-31

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 121.33  E-value: 8.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  82 MRED---LEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAA---SVEETADSTLCHILTLYRRitwlHQALRegtr 155
Cdd:PLN02928   70 MRLDadiIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRK----QNEMQ---- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 156 vQSVEQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERSLGLQRVTT------------L 223
Cdd:PLN02928  142 -ISLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVddlvdekgghedI 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 224 QDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgP 303
Cdd:PLN02928  221 YEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDD-P 299
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2106618234 304 LKDAPNLICTPHAAWYSEQASLEMREEAAREIRRAVTGRIPDSLK 348
Cdd:PLN02928  300 ILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIE 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
76-315 2.47e-29

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 118.03  E-value: 2.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  76 YHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQALREGTR 155
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 156 vqsveQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADG-VERSLGLQRVTTLQDLLFHSDCVS 234
Cdd:PLN03139  186 -----NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVVV 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTP 314
Cdd:PLN03139  261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMTP 339

                  .
gi 2106618234 315 H 315
Cdd:PLN03139  340 H 340
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
86-323 4.93e-27

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 110.77  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  86 LEKFKALRIIVRIgSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLYRRITWLHQalregtRVQSVEQIREV 165
Cdd:PRK12480   65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIER------RVQAHDFTWQA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 166 ASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLADGVERslgLQRVTTLQDLLFHSDCVSLHCSLNEHNHH 245
Cdd:PRK12480  138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICT 313
Cdd:PRK12480  215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayfTNDWTNKDIDDKtlleliehERILVT 294
                         250
                  ....*....|
gi 2106618234 314 PHAAWYSEQA 323
Cdd:PRK12480  295 PHIAFFSDEA 304
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
84-352 1.52e-23

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


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 100.26  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  84 EDLEKFKALRIIVRIGSGYDNIDiKSAGELGIAVCNMPAASVEET-ADSTLCHILTLYRRITwlhqALREGTRVQSVEQI 162
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRDMD----RYAAQQRRGVWKPL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 163 REVASGAARIrgetlGLIGLGRVGQAVALRAKAFGFNVVfydpyladGVERSL-GLQRVTT------LQDLLFHSDCVSL 235
Cdd:cd12164   126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkDIEGVTCfhgeegLDAFLAQTDILVC 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 236 HCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPH 315
Cdd:cd12164   193 LLPLTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTVTPH 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2106618234 316 AawyseqASLEMREEAARE----IRRAVTGRipdSLKNCVN 352
Cdd:cd12164   272 I------AAITDPDSAAAQvaenIRRLEAGE---PLPNLVD 303
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
83-347 7.37e-23

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 98.05  E-value: 7.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  83 REDLEKFKALRIIVRIGSGYDNIdIKSAGElGIAVCNmpAASVEE--TADSTLCHILTLYRRITWLHQALREG----TRV 156
Cdd:cd12166    52 LEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGLPRFVRAQARGrwepRRT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 157 QSVEqirevasgaarirGETLGLIGLGRVGQAVALRAKAFGFNVVfydpyladGVERS----LGLQRVTTLQDLLFHSDC 232
Cdd:cd12166   128 PSLA-------------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEADV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 233 VSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPfsFSQG-PLKDAPNLI 311
Cdd:cd12166   187 VVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEP--LPPGhPLWSAPGVL 263
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2106618234 312 CTPHAAWYSEQASLEMREEAAREIRRAVTGRIPDSL 347
Cdd:cd12166   264 ITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
101-340 2.20e-22

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 98.18  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 101 GYDNIDIKSAGELGIAVCNMP---AASVeetADSTLCHILTLyrritwlhqALREGtrvqsveqirevasgaARIRGETL 177
Cdd:PRK00257   68 GTDHLDLDYFAEAGITWSSAPgcnARGV---VDYVLGSLLTL---------AEREG----------------VDLAERTY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 178 GLIGLGRVGQAVALRAKAFGFNVVFYDPYLADgverSLGLQRVTTLQDLLFHSDCVSLHCSLN-EHNH---HLINDFTIK 253
Cdd:PRK00257  120 GVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQE----AEGDGDFVSLERILEECDVISLHTPLTkEGEHptrHLLDEAFLA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 254 QMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGPLKDAPN-LICTPHAAWYseqaSLEMREEAA 332
Cdd:PRK00257  196 SLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTIATPHIAGY----SLDGKARGT 267

                  ....*...
gi 2106618234 333 REIRRAVT 340
Cdd:PRK00257  268 AQIYQALC 275
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
129-342 2.75e-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: 96.68  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 129 ADSTLCHILTLYRRITWLHQALREGTRVQSV--EQIREVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVfydpy 206
Cdd:cd12160    96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT----- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 207 ladGVERSLGLQ---RVTT---LQDLLFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALK 280
Cdd:cd12160   171 ---GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALE 247
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2106618234 281 EGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASLEMreeAAREIRRAVTGR 342
Cdd:cd12160   248 SGRLGGAALDVTATEPLPASS-PLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
114-317 3.27e-20

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 90.79  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 114 GIAVCNMPAASVEETADSTLCHILTLYRRItwlHQALREGTRVQSveqirEVASGAARIRGETLGLIGLGRVGQAVALRA 193
Cdd:cd12159    73 GRRWTNAAGAYAETVAEHALALLLAGLRQL---PARARATTWDPA-----EEDDLVTLLRGSTVAIVGAGGIGRALIPLL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 194 KAFGFNVVfydpyladGVERS----LGLQRVTTLQDL---LFHSDCVSLHCSLNEHNHHLINDFTIKQMRQGAFLVNTAR 266
Cdd:cd12159   145 APFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVAR 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2106618234 267 GGLVDEKALAQALKEGRIRGAALDVHETEPfsFSQG-PLKDAPNLICTPHAA 317
Cdd:cd12159   217 GPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
137-321 4.77e-17

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 81.94  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 137 LTLYRRITWLHQALREGT--RVQSVEQIREVasgaariRGETLGLIGLGRVGQAVALRAKAFGFNVVFY----------- 203
Cdd:cd12163   101 LVLSHHFLQYIELQKEQTwgRRQEAYSVEDS-------VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesr 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 204 -----------DPylaDGV--------ERSLGLQRVTTLQ-DLLFhsdcVSLhcSLNEHNHHLIN--DFTIKQMRqGAFL 261
Cdd:cd12163   174 kddgyivpgtgDP---DGSipsawfsgTDKASLHEFLRQDlDLLV----VSL--PLTPATKHLLGaeEFEILAKR-KTFV 243
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 262 VNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSE 321
Cdd:cd12163   244 SNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAPNVIITPHVSWQTQ 302
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
73-320 2.06e-14

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 74.56  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  73 ALMYHTITLMREDLEKFKALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEETADSTLCHILTLyrritwlhqALRE 152
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML---------AERD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 153 GTRvqsveqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYDPYLAD-GVERSLglqrvTTLQDLLFHSD 231
Cdd:PRK15438  111 GFS----------------LHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQEAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 232 CVSLHCSLNEHNH----HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDA 307
Cdd:PRK15438  170 ILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKV 248
                         250
                  ....*....|...
gi 2106618234 308 PnlICTPHAAWYS 320
Cdd:PRK15438  249 D--IGTPHIAGYT 259
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
57-323 2.78e-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: 73.10  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  57 QSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGYD----NIDIKSAGELGIAVCNMPA---ASVEETA 129
Cdd:cd12170    35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 130 DSTLCHILTLYRRITWLHQALRegtrvqsveqirevasgaarIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYD----- 204
Cdd:cd12170   114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSrtrkp 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 205 PYLADGVerslglqRVTTLQDLLFHSDCVSLHcsLNEhNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGri 284
Cdd:cd12170   174 DAEAKGI-------RYLPLNELLKTVDVICTC--LPK-NVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS-- 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2106618234 285 rGAALDVHETEPfSFSQGPLKDAPNLICTPHAAWYSEQA 323
Cdd:cd12170   242 -GYNIFDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
90-354 4.68e-14

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 72.61  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  90 KALRIIVRIGSGYDNIDIKSAGELGIAVCNMPAASVEeTADSTLCHILTLYRRITWLHQALREGTRVQSVEQIrevasga 169
Cdd:PRK06436   48 KKTKMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSIS-VAEHAFALLLAWAKNICENNYNMKNGNFKQSPTKL------- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 170 arIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYD-PYLADGVERSlglqrVTTLQDLLFHSDCVSLHCSLNEHNHHLIN 248
Cdd:PRK06436  120 --LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTrSYVNDGISSI-----YMEPEDIMKKSDFVLISLPLTDETRGMIN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 249 DFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPlkdaPNLICTPH-AAWYSEQASLEM 327
Cdd:PRK06436  193 SKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHvAGGMSGEIMQPA 268
                         250       260
                  ....*....|....*....|....*..
gi 2106618234 328 REEAAREIRRAVTGRiPdslKNCVNKE 354
Cdd:PRK06436  269 VALAFENIKNFFEGK-P---KNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
85-310 2.41e-12

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


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 67.64  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234  85 DLEKFKALRIIVRIGSGYDNIDIKSA-GELGIAVCNMPAASVEETADSTlchILTLYRRITWLHQALREgtrvqsveQIR 163
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTEAlARAGLTAIAVEGVELPLLTSNS---IGAGELSVQFIARFLEV--------QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 164 EVASGAARIRGETLGLIGLGRVGQAVALRAKAFGFNVVFYD-PYLADGVERSLGLQRVTTLQDLLFHSDCVSLHCSLNEH 242
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDiNVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGK 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 243 NHHLINDFT-IKQMRQGAFLVNTARG-GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPLKDAPNL 310
Cdd:cd12154   230 RAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
246-343 1.61e-08

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 55.96  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106618234 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSEQAsl 325
Cdd:PRK15469  207 IINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVAAVTRPA-- 283
                          90       100
                  ....*....|....*....|...
gi 2106618234 326 EMREEAAREIRR-----AVTGRI 343
Cdd:PRK15469  284 EAVEYISRTIAQlekgeRVCGQV 306
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
177-227 5.89e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 38.58  E-value: 5.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2106618234 177 LGLIGLGRVGQAVALRAKAFGFNVVFYDPYlADGVER--SLGLQRVTTLQDLL 227
Cdd:PRK09599    3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRN-PEAVEAlaEEGATGADSLEELV 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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