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Conserved domains on  [gi|2238827606|ref|XP_048026286|]
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LOW QUALITY PROTEIN: C-terminal binding protein 2, like [Megalobrama amblycephala]

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 ...
491-809 6.85e-145

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


:

Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 431.17  E-value: 6.85e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 491 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIIRIGSGYD 566
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 567 NIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 646
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 647 RSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 726
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 727 TARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 806
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2238827606 807 PDS 809
Cdd:cd05299   310 PRN 312
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
305-495 2.90e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 305 HLIQPPPSALQSVSPrmgeflgrrPSSAPSQHLLETTTYPAVRPIGGLPVSPGGYSTALPQP--RPLSMYNAHTGLAMSA 382
Cdd:pfam03154 165 QILQTQPPVLQAQSG---------AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPpnQTQSTAAPHTLIQQTP 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 383 QQHPMNTPgvapktfsSTYSPMELMKRPPnlPPlsPAHSPHHSPQLLRKGAAPvesavlPASSTLQhqtvnpnnkltrrT 462
Cdd:pfam03154 236 TLHPQRLP--------SPHPPLQPMTQPP--PP--SQVSPQPLPQPSLHGQMP------PMPHSLQ-------------T 284
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2238827606 463 GPPVIVSTMASPDTSIRPQMVNGPMHPRPLVAL 495
Cdd:pfam03154 285 GPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
491-809 6.85e-145

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


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 431.17  E-value: 6.85e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 491 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIIRIGSGYD 566
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 567 NIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 646
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 647 RSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 726
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 727 TARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 806
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2238827606 807 PDS 809
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
493-816 1.30e-92

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: 295.07  E-value: 1.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDI 570
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 571 KAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRSGQ 650
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 651 AVAVRAKVFGFNVIFYDPYLQDGLERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 730
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 731 GLVDEKALSQALKEGRIRGAALDVHETEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPdsl 810
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 2238827606 811 RNCVNK 816
Cdd:COG1052   311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
493-815 7.88e-81

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: 263.38  E-value: 7.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIIRIGSGYDNIDIK 571
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 572 AAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRSGQA 651
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 652 VAVRAKVFGFNVIFYDPYLQDglERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 726
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 727 TARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 806
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 2238827606 807 PdslRNCVN 815
Cdd:pfam00389 306 P---ANAVN 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
523-817 4.37e-53

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 188.46  E-value: 4.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 523 QEIHEKVLNEAV---GALMyhTITLTREDLEKFKA---LRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTL 596
Cdd:PRK13243   32 REIPREVLLEKVrdvDALV--TMLSERIDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 597 CHVLNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLER 676
Cdd:PRK13243  110 ALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEK 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 677 SLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHE 756
Cdd:PRK13243  190 ELGAEYR-PLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFE 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238827606 757 TEPFSfaQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPDSLrncVNKE 817
Cdd:PRK13243  269 EEPYY--NEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNRE 324
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
305-495 2.90e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 305 HLIQPPPSALQSVSPrmgeflgrrPSSAPSQHLLETTTYPAVRPIGGLPVSPGGYSTALPQP--RPLSMYNAHTGLAMSA 382
Cdd:pfam03154 165 QILQTQPPVLQAQSG---------AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPpnQTQSTAAPHTLIQQTP 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 383 QQHPMNTPgvapktfsSTYSPMELMKRPPnlPPlsPAHSPHHSPQLLRKGAAPvesavlPASSTLQhqtvnpnnkltrrT 462
Cdd:pfam03154 236 TLHPQRLP--------SPHPPLQPMTQPP--PP--SQVSPQPLPQPSLHGQMP------PMPHSLQ-------------T 284
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2238827606 463 GPPVIVSTMASPDTSIRPQMVNGPMHPRPLVAL 495
Cdd:pfam03154 285 GPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
491-809 6.85e-145

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


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 431.17  E-value: 6.85e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 491 PLVALLDGR--DCTVEMPILKDlATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLTREDLEKFKALRIIIRIGSGYD 566
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 567 NIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVeqirevASGAARIRGETLGLIGFG 646
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 647 RSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVqRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 726
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 727 TARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 806
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 2238827606 807 PDS 809
Cdd:cd05299   310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
493-800 7.17e-101

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: 316.49  E-value: 7.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGRDCTVEMPILKDL-ATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIK 571
Cdd:cd05198     2 VLVLEPLFPPEALEALEATgFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 572 AAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRvqsveqIREVASGAARIRGETLGLIGFGRSGQA 651
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 652 VAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGG 731
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238827606 732 LVDEKALSQALKEGRIRGAALDVHETEPFSFAqGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRR 800
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
493-816 1.30e-92

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: 295.07  E-value: 1.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGRDCTVE-MPILKDLA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDI 570
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 571 KAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIrevasgAARIRGETLGLIGFGRSGQ 650
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 651 AVAVRAKVFGFNVIFYDPYLQDGLERsLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 730
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 731 GLVDEKALSQALKEGRIRGAALDVHETEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPdsl 810
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 2238827606 811 RNCVNK 816
Cdd:COG1052   311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
512-815 1.44e-90

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: 289.40  E-value: 1.44e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 512 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEET 591
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 592 ADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQ 671
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 672 DGLERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAA 751
Cdd:COG0111   175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238827606 752 LDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRipdSLRNCVN 815
Cdd:COG0111   255 LDVFEPEPLP-ADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
521-801 3.32e-85

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: 275.14  E-value: 3.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 521 STQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVL 600
Cdd:cd12172    37 TEEELIEL-LKDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 601 NLYRRNTWLYQALREG--TRVQSVEqirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSL 678
Cdd:cd12172   115 ALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 679 GVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETE 758
Cdd:cd12172   184 GVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2238827606 759 PFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 801
Cdd:cd12172   263 PPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
493-815 7.88e-81

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: 263.38  E-value: 7.88e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGRdCTVEMPILKDlATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LTREDLEKFKALRIIIRIGSGYDNIDIK 571
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 572 AAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIREVasgaariRGETLGLIGFGRSGQA 651
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 652 VAVRAKVFGFNVIFYDPYLQDglERSLGVQRVYTLQDLLYQS-----DCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVN 726
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNP--ERAEAGGVEVLSLLLLLLDlpesdDVLTVNPLTTMKTGVIIINEARGMLKDAVAIIN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 727 TARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRI 806
Cdd:pfam00389 228 AAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGP 305

                  ....*....
gi 2238827606 807 PdslRNCVN 815
Cdd:pfam00389 306 P---ANAVN 311
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
545-805 1.32e-80

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: 262.74  E-value: 1.32e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 545 TREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGT----RVQ 620
Cdd:cd12173    53 TAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFM 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 621 SVEqirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHC 700
Cdd:cd12173   133 GVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGGVELV-SLDELLAEADFISLHT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 701 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTA 780
Cdd:cd12173   201 PLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLG 279
                         250       260
                  ....*....|....*....|....*
gi 2238827606 781 WYSEQASLEMREAAATEIRRAITGR 805
Cdd:cd12173   280 ASTEEAQERVAVDAAEQVLAVLAGE 304
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
541-807 8.92e-76

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


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 249.80  E-value: 8.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 541 TITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGtrvq 620
Cdd:cd12175    52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG---- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 621 svEQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVyTLQDLLYQSDCVSLH 699
Cdd:cd12175   128 --RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 700 CNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHT 779
Cdd:cd12175   205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLP-PDDPLLRLDNVILTPHI 283
                         250       260
                  ....*....|....*....|....*...
gi 2238827606 780 AWYSEQASLEMREAAATEIRRAITGRIP 807
Cdd:cd12175   284 AGVTDESYQRMAAIVAENIARLLRGEPP 311
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
544-792 1.07e-71

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


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 238.89  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVE 623
Cdd:cd12162    55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 624 Q------IREVAsgaarirGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLerslGVQRVyTLQDLLYQSDCVS 697
Cdd:cd12162   135 FcfwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPL----REGYV-SLDELLAQSDVIS 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 698 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPL-KDAPNLICT 776
Cdd:cd12162   203 LHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPPR-ADNPLlKAAPNLIIT 281
                         250
                  ....*....|....*.
gi 2238827606 777 PHTAWyseqASLEMRE 792
Cdd:cd12162   282 PHIAW----ASREARQ 293
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
545-815 1.25e-69

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


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 233.67  E-value: 1.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 545 TREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRntwlyqaLREGTRvqsveQ 624
Cdd:cd12178    56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR-------IAEGDR-----L 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 625 IRE-VASGAAR-------IRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVyTLQDLLYQSDC 695
Cdd:cd12178   124 MRRgGFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDF 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 696 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfSFAQGpLKDAPNLIC 775
Cdd:cd12178   203 VSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVIL 280
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2238827606 776 TPHTAWYSEQASLEMREAAATEIRRAITGRIPDslrNCVN 815
Cdd:cd12178   281 TPHIGNATVEARDAMAKEAADNIISFLEGKRPK---NIVN 317
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
505-804 1.43e-67

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: 227.66  E-value: 1.43e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 505 MPILKDLATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVC 581
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 582 NIPSAAVEETADSTLCHVLNLYRRntwlyqaLREGtrvqsveqIREVASGA-----------ARIRGETLGLIGFGRSGQ 650
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARR-------VVEG--------DRFVRAGEwkgwsptlllgTDLHGKTLGIVGMGRIGQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 651 AVAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 730
Cdd:cd05301   158 AVARRAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARG 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238827606 731 GLVDEKALSQALKEGRIRGAALDVHETEPFSFAQgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 804
Cdd:cd05301   237 GVVDEDALVEALKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
555-804 1.57e-66

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


Pssm-ID: 240645 [Multi-domain]  Cd Length: 321  Bit Score: 225.12  E-value: 1.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 555 LRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEqirevASGAAR 634
Cdd:cd12168    77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 635 IRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDF 713
Cdd:cd12168   152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALATYYV-SLDELLAQSDVVSLNCPLTAATRHLINKK 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 714 TIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsFAQGPLKDAPNLICTPHTAWYSEQASLEMREA 793
Cdd:cd12168   231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEP--EVNPGLLKMPNVTLLPHMGTLTVETQEKMEEL 308
                         250
                  ....*....|.
gi 2238827606 794 AATEIRRAITG 804
Cdd:cd12168   309 VLENIEAFLET 319
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
507-805 1.23e-65

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: 222.95  E-value: 1.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 507 ILKDL-ATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPS 585
Cdd:cd01619    19 ILKAGgVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 586 AAVEETADSTLCHVLNLYRRntwlyqalREGTRVQSVEQIREVAS-GAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVI 664
Cdd:cd01619    99 YSPNAVAEHTIALILALLRN--------RKYIDERDKNQDLQDAGvIGRELEDQTVGVVGTGKIGRAVAQRAKGFGMKVI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 665 FYDPYLQDGLERSlGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKE 744
Cdd:cd01619   171 AYDPFRNPELEDK-GVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDS 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238827606 745 GRIRGAALDVHETE-----------PFSFAQGP-LKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 805
Cdd:cd01619   249 GKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEGE 321
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
494-812 1.37e-65

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 222.58  E-value: 1.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 494 ALLDGRDCTVEMPILKDLATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLTREDLEKFKALRIIIRIGSGYDN 567
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 568 IDIKAAGELGIAVCNIPSA----AVEETAdstLCHVLNLYRRNTWLYQALREGtrvqsveQIREVASGAAR-IRGETLGL 642
Cdd:cd12177    83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 643 IGFGRSGQAVAVRAKV-FGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQG 721
Cdd:cd12177   153 IGYGNIGSRVAEILKEgFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 722 AFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRA 801
Cdd:cd12177   232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIK-ADHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                         330
                  ....*....|.
gi 2238827606 802 ITGRIPDSLRN 812
Cdd:cd12177   311 LAGKEPKGILN 321
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
596-780 7.40e-64

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: 212.36  E-value: 7.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 596 LCHVLNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGL 674
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 675 ERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDV 754
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 2238827606 755 HETEPFSfAQGPLKDAPNLICTPHTA 780
Cdd:pfam02826 154 FEPEPLP-ADHPLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
543-778 1.15e-63

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: 216.64  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 543 TLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGtrvqsv 622
Cdd:cd05303    52 KVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG------ 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 623 eQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNL 702
Cdd:cd05303   126 -KWNKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLHVPL 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238827606 703 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAQgpLKDAPNLICTPH 778
Cdd:cd05303   204 TPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
524-800 3.73e-62

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: 212.78  E-value: 3.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 524 EIHEKVLNEAVGA--LMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLN 601
Cdd:cd12171    35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 602 LYRRNTWLYQALREGtrvqsveQIREVASGAAR----IRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERS 677
Cdd:cd12171   115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 678 LGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHET 757
Cdd:cd12171   188 DGVKKV-SLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2238827606 758 EPFSfAQGPLKDAPNLICTPHTAWYSEQA---SLEMreaAATEIRR 800
Cdd:cd12171   267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
546-815 8.72e-60

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: 206.26  E-value: 8.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 546 REDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSA---AVEETAdstLCHVLNLYRRntwLYQALREGTRVQSV 622
Cdd:cd12174    42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGAnanAVAELV---IAMMLALSRN---IIQAIKWVTNGDGD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 623 EQIREVASGAAR-----IRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLG--VQRVYTLQDLLYQSDC 695
Cdd:cd12174   116 DISKGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSveVQRVTSLEELLATADY 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 696 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEpfsfaqgPLKDAPNLIC 775
Cdd:cd12174   196 ITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIA 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2238827606 776 TPHTAWYSEQASLEMREAAATEIRRAI-TGRIPdslrNCVN 815
Cdd:cd12174   269 TPHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
521-804 3.71e-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: 196.99  E-value: 3.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 521 STQEIHEKVLNEAVGA---LMYHTITLTREDLEKFKAL---RIIIRIgSGYDNIDIKAAGELGIAVCNIPSAAVEETADS 594
Cdd:cd12186    30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEYgikQIALRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 595 TLCHVLNLYRRNTWLYQALREGT-RVQSVEQIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDG 673
Cdd:cd12186   109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 674 LErSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALD 753
Cdd:cd12186   182 LE-KFLLYYD-SLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238827606 754 VHETE----PFSFAQGPLKDA--------PNLICTPHTAWYSEQASLEMREAAATEIRRAITG 804
Cdd:cd12186   260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEG 322
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
544-786 1.17e-54

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


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 192.49  E-value: 1.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVE 623
Cdd:cd12187    53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 624 QIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVqRVYTLQDLLYQSDCVSLHCNLN 703
Cdd:cd12187   133 RGFE-------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGF-RYVSLEELLQESDIISLHVPYT 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 704 EHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEP--------FSFAQGPLKDA----- 770
Cdd:cd12187   205 PQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelFREDVSPEDLKkllad 284
                         250       260
                  ....*....|....*....|..
gi 2238827606 771 ------PNLICTPHTAWYSEQA 786
Cdd:cd12187   285 hallrkPNVIITPHVAYNTKEA 306
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
505-791 4.07e-54

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: 190.51  E-value: 4.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 505 MPILKDLATVAFCDAQSTQEihEKVLNEAVGA--LMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCN 582
Cdd:cd12161    20 APLEEQGHEFVYYDTKTTDT--AELIERSKDAdiVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 583 IPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQiREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFN 662
Cdd:cd12161    98 AAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 663 VIFYDPYLQDGLErSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQAL 742
Cdd:cd12161   170 VLAYSRSEKEEAK-ALGIEYV-SLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADAL 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2238827606 743 KEGRIRGAALDVHETEPFSFAQGPLKDAPNLICTPHTAWYSEQAsLEMR 791
Cdd:cd12161   248 NEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFATEEA-MEKR 295
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
506-804 1.38e-53

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: 188.87  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 506 PILKDLATV-AFCD-AQSTQEIHEKVLN-EAVGALMYHTiTLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCN 582
Cdd:cd12169    19 SKLDDRAEVtVFNDhLLDEDALAERLAPfDAIVLMRERT-PFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 583 IPSAaVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVeqirevasgAARIRGETLGLIGFGRSGQAVAVRAKVFGFN 662
Cdd:cd12169    98 TGGG-PTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIGQAFGMR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 663 VIFYDPYLQDGLERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQAL 742
Cdd:cd12169   168 VIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAAL 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2238827606 743 KEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 804
Cdd:cd12169   248 RAGRIAGAALDVFDVEPLP-ADHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
PRK13243 PRK13243
glyoxylate reductase; Reviewed
523-817 4.37e-53

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 188.46  E-value: 4.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 523 QEIHEKVLNEAV---GALMyhTITLTREDLEKFKA---LRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTL 596
Cdd:PRK13243   32 REIPREVLLEKVrdvDALV--TMLSERIDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 597 CHVLNLYRRNTWLYQALREGTRVQSVEQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLER 676
Cdd:PRK13243  110 ALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEK 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 677 SLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHE 756
Cdd:PRK13243  190 ELGAEYR-PLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFE 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2238827606 757 TEPFSfaQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPDSLrncVNKE 817
Cdd:PRK13243  269 EEPYY--NEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNRE 324
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
493-804 6.34e-51

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 181.34  E-value: 6.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 493 VALLDGR---DCTVEmpILKDLATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLTREDLEKFKALRIIIRIGSGYDNID 569
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 570 IKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSvEQIREVASGAARIRGETLGLIGFGRSG 649
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 650 QAVAVRAKVFGFNVIFYDPylqDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTAR 729
Cdd:PRK08410  158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2238827606 730 GGLVDEKALSQALKEGRIrGAALDVHETEPFSfAQGPL---KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITG 804
Cdd:PRK08410  234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
518-805 3.58e-50

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 179.51  E-value: 3.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 518 DAQSTQEIHEKvLNEAVGALMyHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLC 597
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 598 HVLNLYRRNTWLYQALREGtRVQSVEQ-------IREVAsgaarirGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpyL 670
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 671 QDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGA 750
Cdd:PRK06487  177 GQLPGRPARPDRL-PLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2238827606 751 ALDVHETEPfSFAQGPL--KDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGR 805
Cdd:PRK06487  256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
551-799 1.03e-48

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: 175.71  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 551 KFKALRIiirigSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREG-------TRVQsve 623
Cdd:cd12183    70 KLIALRC-----AGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGnfsldglLGFD--- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 624 qirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERsLGVQRVyTLQDLLYQSDCVSLHCNLN 703
Cdd:cd12183   142 -----------LHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELAK-LGVEYV-DLDELLAESDIISLHCPLT 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 704 EHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAQG----PLKDA--------P 771
Cdd:cd12183   209 PETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDhsdeIIQDDvlarllsfP 288
                         250       260
                  ....*....|....*....|....*...
gi 2238827606 772 NLICTPHTAWYSEQAsleMREAAATEIR 799
Cdd:cd12183   289 NVLITGHQAFFTKEA---LTNIAETTLE 313
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
514-792 1.77e-48

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 175.09  E-value: 1.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 514 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLTREDLEKFKAL-------RIIirigsGYDNIDIKAAGELGIAVCNIPS 585
Cdd:cd12185    27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVTY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 586 AAvEETADSTLCHVLNLYRRntwlYQALREGTRVQ--SVEQIRevasgAARIRGETLGLIGFGRSGQAVAVRAKVFGFNV 663
Cdd:cd12185   100 SP-NSVADYTVMLMLMALRK----YKQIMKRAEVNdySLGGLQ-----GRELRNLTVGVIGTGRIGQAVIKNLSGFGCKI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 664 IFYDPYLQDGLERslGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALK 743
Cdd:cd12185   170 LAYDPYPNEEVKK--YAEYV-DLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLE 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238827606 744 EGRIRGAALDV--HETEPF------------SFAQgpLKDAPNLICTPHTAWYSEQASLEMRE 792
Cdd:cd12185   247 SGKIGGAALDVieGEDGIYyndrkgdilsnrELAI--LRSFPNVILTPHMAFYTDQAVSDMVE 307
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
543-817 4.09e-45

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 165.43  E-value: 4.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 543 TLTREDLEKFKALRIIIRI-GSGYDNIDiKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQs 621
Cdd:cd12167    61 PLDAELLARAPRLRAVVHAaGSVRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 622 veqiREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVyTLQDLLYQSDCVSLHCN 701
Cdd:cd12167   139 ----WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSLHAP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 702 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRgAALDVHETEPFSfAQGPLKDAPNLICTPHTAW 781
Cdd:cd12167   214 LTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLP-PDSPLRTLPNVLLTPHIAG 291
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2238827606 782 YSEQASLEMREAAATEIRRAITGRIPdslRNCVNKE 817
Cdd:cd12167   292 STGDERRRLGDYALDELERFLAGEPL---LHEVTPE 324
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
544-786 8.78e-45

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 164.20  E-value: 8.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIP---SAAVEETADS---TLCHVLNLYRRNtwlyqalREGT 617
Cdd:PRK06932   55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTgysSTTVPEHVLGmifALKHSLMGWYRD-------QLSD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 618 RVQSVEQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDpylqdglERSLGVQRV-YT-LQDLLYQSDC 695
Cdd:PRK06932  128 RWATCKQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREgYTpFEEVLKQADI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 696 VSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPL----KDAP 771
Cdd:PRK06932  201 VTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLP 279
                         250
                  ....*....|....*
gi 2238827606 772 NLICTPHTAWYSEQA 786
Cdd:PRK06932  280 NLLITPHIAWASDSA 294
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
539-805 1.16e-43

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: 162.11  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 539 YHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTR 618
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 619 vqsveQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVYTLQDLLYQSDCVS 697
Cdd:cd05302   149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 698 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfSFAQGPLKDAPNLICTP 777
Cdd:cd05302   224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302
                         250       260       270
                  ....*....|....*....|....*....|
gi 2238827606 778 HTAWYSEQAslEMREAAATE--IRRAITGR 805
Cdd:cd05302   303 HISGTTLDA--QARYAAGTKeiLERFFEGE 330
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
543-778 6.82e-43

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: 158.51  E-value: 6.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 543 TLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRntwLYQALREGTRvqsv 622
Cdd:cd12176    53 QLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARR---LPDRNAAAHR---- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 623 EQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDpyLQDGLErsLGVQR-VYTLQDLLYQSDCVSLHCN 701
Cdd:cd12176   126 GIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD--IAEKLP--LGNARqVSSLEELLAEADFVTLHVP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 702 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAQG---PLKDAPNLICTPH 778
Cdd:cd12176   202 ATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASNGEPfssPLQGLPNVILTPH 281
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
546-784 5.02e-42

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: 155.91  E-value: 5.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 546 REDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSA---AVEETADSTLCHVLNLYRRNTWLYQA---LREGTRv 619
Cdd:cd12179    54 KEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGnrdAVGEHALGMLLALFNKLNRADQEVRNgiwDREGNR- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 620 qSVEqirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERslgVQRVyTLQDLLYQSDCVSLH 699
Cdd:cd12179   133 -GVE-----------LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAY---AEQV-SLETLFKEADILSLH 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 700 CNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSF---AQGP-----LKDAP 771
Cdd:cd12179   197 IPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFesiFNQPeafeyLIKSP 276
                         250
                  ....*....|....
gi 2238827606 772 NLICTPHTA-WYSE 784
Cdd:cd12179   277 KVILTPHIAgWTFE 290
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
507-804 1.08e-40

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: 152.44  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 507 ILKDLATvaFCDAQSTQ--------EIHEKVLNeAVGALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGI 578
Cdd:cd12157    14 VLELLKP--HCEVISNQtdeplsreELLRRCKD-ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 579 AVCNIPSAAVEETADSTLCHVLNLYRRntwlyqaLREGTRVqsveqIREVASGAAR-------IRGETLGLIGFGRSGQA 651
Cdd:cd12157    91 WVTIVPDLLTEPTAELTIGLLIGLGRH-------ILAGDRF-----VRSGKFGGWRpkfygtgLDGKTVGILGMGALGRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 652 VAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARG 730
Cdd:cd12157   159 IARRLSGFGATLLYYDPHpLDQAEEQALNLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 731 GLVDEKALSQALKEGRIRGAALDVHETE-------PFSFAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAIT 803
Cdd:cd12157   238 SVVDEAAVAEALKSGHLGGYAADVFEMEdwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQ 317

                  .
gi 2238827606 804 G 804
Cdd:cd12157   318 G 318
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
527-808 1.67e-40

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


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 151.63  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 527 EKVLNEAvGALMYHTITLtREDLEKFKALRIIIRIGSGYDNIDIKAAGElGIAVCNIP--SAAVEETAdstLCHVLNLYR 604
Cdd:cd12165    35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHgnSPAVAEHA---LALILALAK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 605 RNTWLYQALREGTRVQSVEQIREVASgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERS----LGV 680
Cdd:cd12165   109 RIVEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVI--------GVSRSpkedEGA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 681 QRVYTLQDL---LYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDV--- 754
Cdd:cd12165   177 DFVGTLSDLdeaLEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwr 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2238827606 755 -----HETEPFSFaqgPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPD 808
Cdd:cd12165   257 ypsrgDPVAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
544-795 1.85e-40

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: 151.08  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGtrvqsvE 623
Cdd:cd12156    54 LSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------R 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 624 QIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERslgvQRVYTLQDLLYQSDCVSLHCNLN 703
Cdd:cd12156   128 WPKGAFPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVPY----RYYASLLELAAESDVLVVACPGG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 704 EHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsfaQGP--LKDAPNLICTPHTAw 781
Cdd:cd12156   204 PATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIA- 278
                         250
                  ....*....|....
gi 2238827606 782 yseQASLEMREAAA 795
Cdd:cd12156   279 ---SATVETRRAMG 289
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
543-792 1.73e-39

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


Pssm-ID: 240660  Cd Length: 330  Bit Score: 149.36  E-value: 1.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 543 TLTREDLEKFKALRI--IIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRR-NTWLYQALREGTRV 619
Cdd:cd12184    55 FADKENLEIYKEYGIkyVFTRTVGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHtAYTASRTANKNFKV 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 620 QSVEQIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERslgVQRVYTLQDLLYQSDCVSLH 699
Cdd:cd12184   135 DPFMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKD---VVTFVSLDELLKKSDIISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 700 C-NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDV--HETEPF--SFAQGPLKDA---- 770
Cdd:cd12184   205 VpYIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvvek 284
                         250       260
                  ....*....|....*....|....*..
gi 2238827606 771 -----PNLICTPHTAWYSEQASLEMRE 792
Cdd:cd12184   285 lldlyPRVLLTPHIGSYTDEALSNMIE 311
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
544-778 3.24e-39

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 150.71  E-value: 3.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALriiIRIGS---GYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQ 620
Cdd:PRK11790   65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 621 SveqirevASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDpyLQDGLerSLG-VQRVYTLQDLLYQSDCVSLH 699
Cdd:PRK11790  142 S-------AAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD--IEDKL--PLGnARQVGSLEELLAQSDVVSLH 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 700 CNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFS----FaQGPLKDAPNLIC 775
Cdd:PRK11790  211 VPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSngdpF-ESPLRGLDNVIL 289

                  ...
gi 2238827606 776 TPH 778
Cdd:PRK11790  290 TPH 292
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
544-797 1.11e-38

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 148.67  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRvqsve 623
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGW----- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 624 QIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPY-LQDGLERSLGVQRVYTLQDLLYQSDCVSLHCNL 702
Cdd:PRK07574  179 NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVTIHCPL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 703 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfSFAQGPLKDAPNLICTPHTAWY 782
Cdd:PRK07574  259 HPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQP-APADHPWRTMPRNGMTPHISGT 337
                         250
                  ....*....|....*
gi 2238827606 783 SEQAslEMREAAATE 797
Cdd:PRK07574  338 TLSA--QARYAAGTR 350
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
546-817 1.28e-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: 143.43  E-value: 1.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 546 REDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCN---IPSAAVeetADSTLCHVLNLYRRnTWLYQALREGTRVQSV 622
Cdd:cd05300    51 PELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNargIFGPPI---AEYVLGYMLAFARK-LPRYARNQAERRWQRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 623 EQIREvasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERSL-----GVQRVYT---LQDLLYQSD 694
Cdd:cd05300   127 GPVRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVRRSGrpappVVDEVYTpdeLDELLPEAD 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 695 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLI 774
Cdd:cd05300   192 YVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVI 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2238827606 775 CTPHTAWYSEqaslEMREAAAtEI-----RRAITGRipdSLRNCVNKE 817
Cdd:cd05300   271 ITPHISGDSP----SYPERVV-EIflenlRRYLAGE---PLLNVVDKD 310
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
522-815 1.64e-36

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 140.66  E-value: 1.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 522 TQEIHEKVLNEAVGaLMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLN 601
Cdd:PRK15409   35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 602 LYRRntwlyqALREGTRVQSVEQIREVASG--AARIRGETLGLIGFGRSGQAVAVRAKvFGFNV-IFYDPYLQ-DGLERS 677
Cdd:PRK15409  114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 678 LGVQRVyTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHET 757
Cdd:PRK15409  187 FNARYC-DLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2238827606 758 EPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPdslRNCVN 815
Cdd:PRK15409  266 EPLS-VDSPLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVN 319
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
561-802 1.12e-34

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: 135.74  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 561 IGS---GYDNIDIKAAGELGIAVCNIP---SAAVeetADSTLCHVLNLYRRNTWLyqalregtrvqsveqirevasgaar 634
Cdd:cd12158    61 VGTatiGTDHIDTDYLKERGIGFANAPgcnANSV---AEYVLSALLVLAQRQGFS------------------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 635 IRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQdglERSLGVQRVyTLQDLLYQSDCVSLHCNLN---EHN-HHLI 710
Cdd:cd12158   113 LKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRA---EAEGDPGFV-SLEELLAEADIITLHVPLTrdgEHPtYHLL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 711 NDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsfaqgplkdAPNL-------ICTPHTAWYs 783
Cdd:cd12158   189 DEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP----------EIDLelldkvdIATPHIAGY- 257
                         250
                  ....*....|....*....
gi 2238827606 784 eqaSLEMREAAATEIRRAI 802
Cdd:cd12158   258 ---SLEGKARGTEMIYEAL 273
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
633-815 1.66e-33

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


Pssm-ID: 240657  Cd Length: 308  Bit Score: 131.31  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 633 ARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERS------LGVQRVYTLQDLLYQSDCVSLHCNLNEHN 706
Cdd:cd12180   131 GSLAGSTLGIVGFGAIGQALARRALALGMRVL--------ALRRSgrpsdvPGVEAAADLAELFARSDHLVLAAPLTPET 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 707 HHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQA 786
Cdd:cd12180   203 RHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDG 281
                         170       180
                  ....*....|....*....|....*....
gi 2238827606 787 SLEMREAAATEIRRAITGRipdSLRNCVN 815
Cdd:cd12180   282 RRNLADRFLENLARYRAGQ---PLHDLVD 307
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
563-786 5.61e-33

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 130.63  E-value: 5.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 563 SGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRntwlYQALREGTRVQSveqIREVASGAAR-IRGETLG 641
Cdd:PRK08605   78 AGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRH----FNQIQTKVREHD---FRWEPPILSRsIKDLKVA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 642 LIGFGRSGQAVA-VRAKVFGFNVIFYDPYLQDGLERSlgVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQ 720
Cdd:PRK08605  151 VIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKAATY--VDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKK 228
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2238827606 721 GAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETE----PFSFAQGPLKDA--------PNLICTPHTAWYSEQA 786
Cdd:PRK08605  229 GAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIAFYTDAA 306
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
548-785 4.21e-32

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: 127.31  E-value: 4.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 548 DLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTrVQSVEQIRE 627
Cdd:cd12155    54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKK-WKMDSSLLE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 628 VAsgaarirGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERS----LGVQRVYTLQDL---LYQSDCVSLHC 700
Cdd:cd12155   133 LY-------GKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLKEADIVVNVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 701 NLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTA 780
Cdd:cd12155   198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                  ....*
gi 2238827606 781 WYSEQ 785
Cdd:cd12155   277 GVSEH 281
PLN02928 PLN02928
oxidoreductase family protein
544-808 1.15e-31

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 127.10  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 544 LTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAV---EETADSTLCHVLNLYRRNTWLYQALRegtrvq 620
Cdd:PLN02928   72 LDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTgnaASCAEMAIYLMLGLLRKQNEMQISLK------ 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 621 sveqirevasgaARIRGETLG---------LIGFGRSGQAVAVRAKVFGFNVIFY------DPYLQDGLERSLGVQRVY- 684
Cdd:PLN02928  146 ------------ARRLGEPIGdtlfgktvfILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNGDVDDLVDe 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 685 -----TLQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEP 759
Cdd:PLN02928  214 kggheDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEP 293
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2238827606 760 FSfAQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPD 808
Cdd:PLN02928  294 FD-PDDPILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLT 341
PLN02306 PLN02306
hydroxypyruvate reductase
564-806 4.61e-31

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 126.13  E-value: 4.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 564 GYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTRVQSVEQIREvasgAARIRGETLGLI 643
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 644 GFGRSGQAVAvRAKVFGF--NVIFYDPYLQDGLE----------RSLGVQ-----RVYTLQDLLYQSDCVSLHCNLNEHN 706
Cdd:PLN02306  172 GAGRIGSAYA-RMMVEGFkmNLIYYDLYQSTRLEkfvtaygqflKANGEQpvtwkRASSMEEVLREADVISLHPVLDKTT 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 707 HHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsFAQGPLKDAPNLICTPHTAwyseQA 786
Cdd:PLN02306  251 YHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIA----SA 324
                         250       260
                  ....*....|....*....|
gi 2238827606 787 SLEMREAAATEIRRAITGRI 806
Cdd:PLN02306  325 SKWTREGMATLAALNVLGKL 344
PLN03139 PLN03139
formate dehydrogenase; Provisional
539-797 6.18e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 116.87  E-value: 6.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 539 YHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYQALREGTR 618
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEW 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 619 vqsveQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDG-LERSLGVQRVYTLQDLLYQSDCVS 697
Cdd:PLN03139  186 -----NVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDVVV 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 698 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTP 777
Cdd:PLN03139  261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAMTP 339
                         250       260
                  ....*....|....*....|
gi 2238827606 778 HTAWYSEQASLemREAAATE 797
Cdd:PLN03139  340 HISGTTIDAQL--RYAAGVK 357
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
549-786 7.61e-25

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 106.54  E-value: 7.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 549 LEKFKALRIIIRIgSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLYRRntwlYQALREgtRVQSVEQIREV 628
Cdd:PRK12480   65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRR----FPDIER--RVQAHDFTWQA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 629 ASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERslgVQRVYTLQDLLYQSDCVSLHCNLNEHNHH 708
Cdd:PRK12480  138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 709 LINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFA---QGPLKDAP---------NLICT 776
Cdd:PRK12480  215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEAAYFTndwTNKDIDDKtllelieheRILVT 294
                         250
                  ....*....|
gi 2238827606 777 PHTAWYSEQA 786
Cdd:PRK12480  295 PHIAFFSDEA 304
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
547-802 2.59e-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: 101.42  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 547 EDLEKFKALRIIIRIGSGYDNIDiKAAGELGIAVCNIPSAAVEET-ADSTLCHVLNLYRRntwlYQALREGTRVQSVEQI 625
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRD----MDRYAAQQRRGVWKPL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 626 REVASGAARIrgetlGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERSL----GVQRVY---TLQDLLYQSDCVsl 698
Cdd:cd12164   126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVS--------GWSRSPkdieGVTCFHgeeGLDAFLAQTDIL-- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 699 hCNL---NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLIC 775
Cdd:cd12164   191 -VCLlplTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHPRVTV 268
                         250       260
                  ....*....|....*....|....*..
gi 2238827606 776 TPHTawyseqASLEMREAAATEIRRAI 802
Cdd:cd12164   269 TPHI------AAITDPDSAAAQVAENI 289
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
536-783 1.14e-20

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 95.10  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 536 ALMYHTIT-LTREDLEKFKaLRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETADSTLCHVLNLyrrntwlyqALR 614
Cdd:PRK00257   40 VLLVRSVTrVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTL---------AER 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 615 EGtrvqsveqirevasgaARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVqrvyTLQDLLYQSD 694
Cdd:PRK00257  110 EG----------------VDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFV----SLERILEECD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 695 CVSLHCNLN-EHNH---HLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsfaQGPLKDA 770
Cdd:PRK00257  170 VISLHTPLTkEGEHptrHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELA 245
                         250
                  ....*....|....
gi 2238827606 771 PN-LICTPHTAWYS 783
Cdd:PRK00257  246 DLcTIATPHIAGYS 259
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
592-812 2.22e-19

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 90.13  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 592 ADSTLCHVLNLYRRNTWLYQALREGTRVQSV--EQIREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpy 669
Cdd:cd12160    96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT----- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 670 lqdGLERSLGVQ---RVYT---LQDLLYQSDCVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALK 743
Cdd:cd12160   171 ---GVARSAGERagfPVVAedeLPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALE 247
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238827606 744 EGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSEQASLEMreaAATEIRRAITGRipdSLRN 812
Cdd:cd12160   248 SGRLGGAALDVTATEPLP-ASSPLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG---PLRN 309
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
625-780 4.15e-19

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 88.86  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 625 IREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERS----LGVQRVYTLQDL---LYQSDCVS 697
Cdd:cd12159   113 PAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVI--------AVNRSgrpvEGADETVPADRLdevWPDADHVV 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 698 LHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfsFAQG-PLKDAPNLICT 776
Cdd:cd12159   185 LAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALIT 262

                  ....
gi 2238827606 777 PHTA 780
Cdd:cd12159   263 PHVA 266
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
545-810 1.28e-18

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: 87.65  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 545 TREDLEKFKALRIIIRIGSGYDNIdIKAAGElGIAVCNipSAAVEE--TADSTLCHVLNLYRRNTWLYQALREG----TR 618
Cdd:cd12166    51 VLEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGLPRFVRAQARGrwepRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 619 VQSVEqirevasgaarirGETLGLIGFGRSGQAVAVRAKVFGFNVIfydpylqdGLERS----LGVQRVYTLQDLLYQSD 694
Cdd:cd12166   127 TPSLA-------------DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGIDELPALLPEAD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 695 CVSLHCNLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRgAALDVHETEPFSfAQGPLKDAPNLI 774
Cdd:cd12166   186 VVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEPLP-PGHPLWSAPGVL 263
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2238827606 775 CTPHTAWYSEQASLEMREAAATEIRRAITGRIPDSL 810
Cdd:cd12166   264 ITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
607-784 3.43e-17

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 83.86  E-value: 3.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 607 TWL-----YQALREGTRVQSVEQiREVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFY--------------- 666
Cdd:cd12163    99 TWLvlshhFLQYIELQKEQTWGR-RQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkddg 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 667 -------DPylqDGL--------ERSLGVQRVYTLQ-DLLyqsdCVSLhcNLNEHNHHLIN--DFTIKQMRqGAFLVNTA 728
Cdd:cd12163   178 yivpgtgDP---DGSipsawfsgTDKASLHEFLRQDlDLL----VVSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIA 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2238827606 729 RGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWYSE 784
Cdd:cd12163   248 RGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPLWSAPNVIITPHVSWQTQ 302
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
520-786 4.95e-16

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: 79.65  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 520 QSTQEIHEKVlNEAVGALMYHTITLTREDLEKFKALRIIIRIGSGYD----NIDIKAAGELGIAVCNIPS---AAVEETA 592
Cdd:cd12170    35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 593 DSTLCHVLNLYRRNTWLYQALRegtrvqsveqirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQD 672
Cdd:cd12170   114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 673 GLERSlGVqRVYTLQDLLYQSDCVSLHCNlneHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGrirGAAL 752
Cdd:cd12170   174 DAEAK-GI-RYLPLNELLKTVDVICTCLP---KNVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2238827606 753 DVHETEPfSFAQGPLKDAPNLICTPHTAWYSEQA 786
Cdd:cd12170   246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQA 278
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
548-773 2.40e-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: 68.80  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 548 DLEKFKALRIIIRIGSGYDNIDIK-AAGELGIAVcnipsAAVEETADSTLCHVLNLYRrntwlYQALREGTRVQSVeQIR 626
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTeALARAGLTA-----IAVEGVELPLLTSNSIGAG-----ELSVQFIARFLEV-QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 627 EVASGAARIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGL-ERSLGVQRVYTLQDLLYQSDCVSLHCNLNEH 705
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEqLEELGGKNVEELEEALAEADVIVTTTLLPGK 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 706 NHHLINDFT-IKQMRQGAFLVNTARG-GLVDEKALSQALKEGRIRGAALDVHETEPFSFAQGPLKDAPNL 773
Cdd:cd12154   230 RAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
553-817 4.00e-12

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 67.99  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 553 KALRIIIRIGSGYDNIDIKAAGElGIAVCNIPSA---AVEETADS-TLCHVLNLYRRNtwlyQALREGTRVQSVEQIrev 628
Cdd:PRK06436   48 KKTKMIQSLSAGVDHIDVSGIPE-NVVLCSNAGAysiSVAEHAFAlLLAWAKNICENN----YNMKNGNFKQSPTKL--- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 629 asgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQDGlerslGVQRVY-TLQDLLYQSDCVSLHCNLNEHNH 707
Cdd:PRK06436  120 ------LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTRSYVND-----GISSIYmEPEDIMKKSDFVLISLPLTDETR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 708 HLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSFAQGPlkdaPNLICTPHTAwysEQAS 787
Cdd:PRK06436  189 GMINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHVA---GGMS 261
                         250       260       270
                  ....*....|....*....|....*....|
gi 2238827606 788 LEMREAAATEIRRAITGRIPDSLRNCVNKE 817
Cdd:PRK06436  262 GEIMQPAVALAFENIKNFFEGKPKNIVRKE 291
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
536-806 1.92e-11

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 66.85  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 536 ALMYHTITLTREDLEKFKALRIIIRIGSGYDNIDIKAAGELGIAVCNIP---SAAVEETADSTLchvlnlyrrntwLYQA 612
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPgcnAIAVVEYVFSSL------------LMLA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 613 LREGTRvqsveqirevasgaarIRGETLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQD-GLERSLgvqrvYTLQDLLY 691
Cdd:PRK15438  108 ERDGFS----------------LHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADrGDEGDF-----RSLDELVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 692 QSDCVSLHCNLNEHNH----HLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPfSFAQGPL 767
Cdd:PRK15438  167 EADILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2238827606 768 KDAPnlICTPHTAWYseqaSLEMREAAATEIRRAITGRI 806
Cdd:PRK15438  246 KKVD--IGTPHIAGY----TLEGKARGTTQVFEAYSKFI 278
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
553-803 7.65e-09

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 58.27  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 553 KALRIIIRIGSGYDNIDIKAAGELGIAVCNIPSAAVEETA------DSTLCHVLNLYRRNTwLYQALREGTRVQSVEQIR 626
Cdd:PRK15469   55 RDLKAVFALGAGVDSILSKLQAHPEMLDPSVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-DYQALQNSSHWQPLPEYH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 627 evasgaariRGE-TLGLIGFGRSGQAVAVRAKVFGFNVIFYDPYLQD--GLERSLGVQRvytLQDLLYQSDC-VSLHCNL 702
Cdd:PRK15469  134 ---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGREE---LSAFLSQTRVlINLLPNT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 703 NEhNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALSQALKEGRIRGAALDVHETEPFSfAQGPLKDAPNLICTPHTAWY 782
Cdd:PRK15469  202 PE-TVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREPLP-PESPLWQHPRVAITPHVAAV 279
                         250       260
                  ....*....|....*....|.
gi 2238827606 783 SEQASlemreaAATEIRRAIT 803
Cdd:PRK15469  280 TRPAE------AVEYISRTIA 294
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
305-495 2.90e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 305 HLIQPPPSALQSVSPrmgeflgrrPSSAPSQHLLETTTYPAVRPIGGLPVSPGGYSTALPQP--RPLSMYNAHTGLAMSA 382
Cdd:pfam03154 165 QILQTQPPVLQAQSG---------AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPpnQTQSTAAPHTLIQQTP 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238827606 383 QQHPMNTPgvapktfsSTYSPMELMKRPPnlPPlsPAHSPHHSPQLLRKGAAPvesavlPASSTLQhqtvnpnnkltrrT 462
Cdd:pfam03154 236 TLHPQRLP--------SPHPPLQPMTQPP--PP--SQVSPQPLPQPSLHGQMP------PMPHSLQ-------------T 284
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2238827606 463 GPPVIVSTMASPDTSIRPQMVNGPMHPRPLVAL 495
Cdd:pfam03154 285 GPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317
 
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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