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Conserved domains on  [gi|1249030266|ref|XP_022539195|]
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C-terminal-binding protein 1 isoform X1 [Astyanax mexicanus]

Protein Classification

C-terminal binding protein( domain architecture ID 10143094)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 1.96e-148

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


:

Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 424.23  E-value: 1.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 104 NIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 184 RVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGVRVV-SLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1249030266 344 PDS 346
Cdd:cd05299   310 PRN 312
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 1.96e-148

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


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 424.23  E-value: 1.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 104 NIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 184 RVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGVRVV-SLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1249030266 344 PDS 346
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 5.01e-97

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


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 293.53  E-value: 5.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDI 107
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 108 KSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 187
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 188 AVALRAKAFGFNVIFYDPYLSDGMErALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 267
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 268 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 347
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1249030266 348 KNCVNK 353
Cdd:COG1052   311 PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 9.11e-82

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 254.52  E-value: 9.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 109 SAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 189 VALRAKAFGFNVIFYDPYLSDGMERALGLQRVNTLQDLLF---HSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 266 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1249030266 346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
80-358 3.10e-70

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 231.06  E-value: 3.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  80 TLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsv 159
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 160 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDgmERA--LGLQRVNTLQDLLFHSDCVTLHC 237
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 238 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAA 317
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1249030266 318 WYSEQASIEMREEAAREIRRAITGripDSLKNCVNKEFLTQ 358
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVNAPGIDA 317
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-356 3.84e-57

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 191.55  E-value: 3.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  60 QEIHEKVLNEAV---GALmyhtITLMRE--DLEKFKA---LRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADS 131
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLSEriDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 132 TLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGM 211
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 212 ERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:PRK13243  188 EKELGAEYR-PLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1249030266 292 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLkncVNKEFL 356
Cdd:PRK13243  267 FEEEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNREVV 326
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 1.96e-148

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


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 424.23  E-value: 1.96e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  28 PLVALLDGR--DCTVEMPILKDvATVAFCDAQS--TQEIHEKVlNEAVGALMYHTiTLMREDLEKFKALRIIVRIGSGFD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYA-PVTAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 104 NIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVeqirevASGAARIRGETLGIIGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTV------GGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 184 RVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVAALGGVRVV-SLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 264 TARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFsQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPPA-DSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1249030266 344 PDS 346
Cdd:cd05299   310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
30-337 1.50e-107

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


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 319.96  E-value: 1.50e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRDCTVEMPILKD-VATVAFCDAQSTQEIhEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:cd05198     2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 109 SAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRvqsveqIREVASGAARIRGETLGIIGLGRVGQA 188
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 189 VALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGG 268
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1249030266 269 LVDEKALAQALKEGRIRGAALDVHETEPFSFSqGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 337
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEPLPAD-HPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
30-353 5.01e-97

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


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 293.53  E-value: 5.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRDCTVE-MPILKDVA-TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDI 107
Cdd:COG1052     3 ILVLDPRTLPDEvLERLEAEHfEVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 108 KSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIrevasgAARIRGETLGIIGLGRVGQ 187
Cdd:COG1052    83 AAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSPGLL------GRDLSGKTLGIIGLGRIGQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 188 AVALRAKAFGFNVIFYDPYLSDGMErALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARG 267
Cdd:COG1052   157 AVARRAKGFGMKVLYYDRSPKPEVA-ELGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 268 GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdsl 347
Cdd:COG1052   235 GLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDH-PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP--- 310

                  ....*.
gi 1249030266 348 KNCVNK 353
Cdd:COG1052   311 PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
49-352 1.23e-95

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 290.17  E-value: 1.23e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  49 ATVAFCDAQSTQEIHEKvLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEET 128
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 129 ADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLS 208
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGRWDRSAFRGRE-------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 209 DGMERALGLQRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAA 288
Cdd:COG0111   175 PEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRLAGAA 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1249030266 289 LDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRipdSLKNCVN 352
Cdd:COG0111   255 LDVFEPEPLPADS-PLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGE---PLRNLVN 314
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
83-342 3.99e-87

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


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 267.74  E-value: 3.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGT----RVQS 158
Cdd:cd12173    54 AEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKwdrkKFMG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 159 VEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERALGlQRVNTLQDLLFHSDCVTLHCS 238
Cdd:cd12173   134 VE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISLHTP 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 239 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAW 318
Cdd:cd12173   202 LTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEPPP-ADSPLLGLPNVILTPHLGA 280
                         250       260
                  ....*....|....*....|....
gi 1249030266 319 YSEQASIEMREEAAREIRRAITGR 342
Cdd:cd12173   281 STEEAQERVAVDAAEQVLAVLAGE 304
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
58-338 4.92e-87

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


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 267.82  E-value: 4.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  58 STQEIHEKvLNEAVGAL-MYHTITlmREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHI 136
Cdd:cd12172    37 TEEELIEL-LKDADGVIaGLDPIT--EEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLM 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 137 LNLYRRTTWLHQALREG--TRVQSVEqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERA 214
Cdd:cd12172   114 LALARQIPQADREVRAGgwDRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 215 LGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:cd12172   183 HGVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEE 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1249030266 295 EPFSfSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 338
Cdd:cd12172   262 EPPP-ADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 9.11e-82

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


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 254.52  E-value: 9.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRdCTVEMPILKDvATVAFCDAQSTQEIHEKVlnEAVGALMYHTIT-LMREDLEKFKALRIIVRIGSGFDNIDIK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 109 SAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVasgaariRGETLGIIGLGRVGQA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLEL-------YGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 189 VALRAKAFGFNVIFYDPYLSDGMERALGLQRVNTLQDLLF---HSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLDlpeSDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 266 RGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPd 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDS--PLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1249030266 346 slKNCVN 352
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
83-352 8.49e-80

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


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 249.46  E-value: 8.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsveqi 162
Cdd:cd12178    57 KEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRG--------- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 163 reVASGAAR-------IRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERALGLQRVnTLQDLLFHSDCVT 234
Cdd:cd12178   128 --GFLGWAPlfflgheLAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDFVS 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGpLKDAPNLICTP 314
Cdd:cd12178   205 LHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEP-EVSPE-LKKLDNVILTP 282
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1249030266 315 HAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVN 352
Cdd:cd12178   283 HIGNATVEARDAMAKEAADNIISFLEGKRP---KNIVN 317
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
81-344 1.79e-78

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


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 245.95  E-value: 1.79e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  81 LMREDLEK-FKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsv 159
Cdd:cd12175    54 VIDAELLAaAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAG------ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 160 EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERALGLQRVnTLQDLLFHSDCVTLHCS 238
Cdd:cd12175   128 RWGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLHVP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 239 LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAW 318
Cdd:cd12175   207 LTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEPLPPDD-PLLRLDNVILTPHIAG 285
                         250       260
                  ....*....|....*....|....*.
gi 1249030266 319 YSEQASIEMREEAAREIRRAITGRIP 344
Cdd:cd12175   286 VTDESYQRMAAIVAENIARLLRGEPP 311
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
92-341 1.87e-73

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: 233.21  E-value: 1.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  92 LRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEqirevASGAAR 171
Cdd:cd12168    77 LKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRGFLD-----LTLAHD 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 172 IRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERALGLqRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDF 250
Cdd:cd12168   152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALAT-YYVSLDELLAQSDVVSLNCPLTAATRHLINKK 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 251 TIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFsFSQGpLKDAPNLICTPHAAWYSEQASIEMREE 330
Cdd:cd12168   231 EFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPE-VNPG-LLKMPNVTLLPHMGTLTVETQEKMEEL 308
                         250
                  ....*....|.
gi 1249030266 331 AAREIRRAITG 341
Cdd:cd12168   309 VLENIEAFLET 319
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
83-329 2.34e-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: 227.34  E-value: 2.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQ- 161
Cdd:cd12162    57 AEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEWQKSPDFc 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 162 -----IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGmeraLGLQRVnTLQDLLFHSDCVTLH 236
Cdd:cd12162   137 fwdypIIELA-------GKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPP----LREGYV-SLDELLAQSDVISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 237 CSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsqgP------LKDAPNL 310
Cdd:cd12162   205 CPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplLKAAPNL 278
                         250
                  ....*....|....*....
gi 1249030266 311 ICTPHAAWyseqASIEMRE 329
Cdd:cd12162   279 IITPHIAW----ASREARQ 293
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
42-341 4.15e-71

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


Pssm-ID: 240626 [Multi-domain]  Cd Length: 309  Bit Score: 226.89  E-value: 4.15e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  42 MPILKDVATVAFCD---AQSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVC 118
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 119 NMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGF 198
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAG----EWKGWSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 199 NVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 278
Cdd:cd05301   169 KILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEA 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 279 LKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd05301   248 LKSGKIAGAGLDVFEPEPLPADH-PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLAVLAG 309
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
80-358 3.10e-70

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 231.06  E-value: 3.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  80 TLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsv 159
Cdd:TIGR01327  51 KVTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEG------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 160 EQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDgmERA--LGLQRVNTLQDLLFHSDCVTLHC 237
Cdd:TIGR01327 125 EWDRKAFMGT-ELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISP--ERAeqLGVELVDDLDELLARADFITVHT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 238 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSqgPLKDAPNLICTPHAA 317
Cdd:TIGR01327 202 PLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPTDN--PLFDLDNVIATPHLG 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1249030266 318 WYSEQASIEMREEAAREIRRAITGripDSLKNCVNKEFLTQ 358
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKG---LPVPNAVNAPGIDA 317
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
30-342 4.31e-70

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


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 224.49  E-value: 4.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGRDctVEMPILKDVA-----TVAFCDAQSTQEIHEKVLNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFDN 104
Cdd:cd01619     3 VLIYDYRD--DELEIEKEILkaggvDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 105 IDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGR 184
Cdd:cd01619    81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRE-------LEDQTVGVVGTGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 185 VGQAVALRAKAFGFNVIFYDPYLSDGMErALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNT 264
Cdd:cd01619   154 IGRAVAQRAKGFGMKVIAYDPFRNPELE-DKGVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 265 ARGGLVDEKALAQALKEGRIRGAALDVHETE-----------PFSFSQGP-LKDAPNLICTPHAAWYSEQASIEMREEAA 332
Cdd:cd01619   232 ARGSLVDTEALIEALDSGKIFGAGLDVLEDEtpdllkdlegeIFKDALNAlLGRRPNVIITPHTAFYTDDALKNMVEISC 311
                         330
                  ....*....|
gi 1249030266 333 REIRRAITGR 342
Cdd:cd01619   312 ENIVDFLEGE 321
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
133-317 2.90e-69

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: 217.36  E-value: 2.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 133 LCHILNLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGM 211
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRwASPDALLGRE-------LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 212 ERALGLQRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:pfam02826  74 EEEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDV 153
                         170       180
                  ....*....|....*....|....*.
gi 1249030266 292 HETEPFSFSQgPLKDAPNLICTPHAA 317
Cdd:pfam02826 154 FEPEPLPADH-PLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
83-315 6.44e-68

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: 218.18  E-value: 6.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsveQI 162
Cdd:cd05303    55 KEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLG-------KW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 163 REVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEH 242
Cdd:cd05303   128 NKKKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLHVPLTPE 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 243 NHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgpLKDAPNLICTPH 315
Cdd:cd05303   207 TKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPPGSK--LLELPNVSLTPH 277
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
83-352 7.14e-67

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: 215.89  E-value: 7.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRttwLHQALREGTRVQSVEQI 162
Cdd:cd12174    42 LHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRN---IIQAIKWVTNGDGDDIS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 163 REVASGAAR-----IRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDgmERALGL----QRVNTLQDLLFHSDCV 233
Cdd:cd12174   119 KGVEKGKKQfvgteLRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSV--EAAWKLsvevQRVTSLEELLATADYI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 234 TLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEpfsfsqgPLKDAPNLICT 313
Cdd:cd12174   197 TLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLPNVIAT 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1249030266 314 PHAAWYSEQASIEMREEAAREIRRAI-TGRIPdslkNCVN 352
Cdd:cd12174   270 PHLGASTEEAEENCAVMAARQIMDFLeTGNIT----NSVN 305
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-337 1.50e-64

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: 209.70  E-value: 1.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  61 EIHEKVLNEAVGA--LMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILN 138
Cdd:cd12171    35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 139 LYRRTTWLHQALREGtrvqsveQIREVASGAAR----IRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERA 214
Cdd:cd12171   115 ETRNIARAHAALKDG-------EWRKDYYNYDGygpeLRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPEKIEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 215 LGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:cd12171   188 DGVKKV-SLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1249030266 295 EPFSfSQGPLKDAPNLICTPHAAWYSEQA---SIEMreeAAREIRR 337
Cdd:cd12171   267 EPLP-ADHPLLKLDNVTLTPHIAGATRDVaerSPEI---IAEELKR 308
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
31-349 3.77e-64

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: 209.10  E-value: 3.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  31 ALLDGRDCTVEMPILKDVATVAFCDAQSTqeIHEKVLNEAVGAlmYHTI------TLMREDLEKFKALRIIVRIGSGFDN 104
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEKLKG--YDIIiasvtpNFDKEFFEYNDGLKLIARHGIGYDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 105 IDIKSAGELGIAVCNMPSA----SVEETAdstLCHILNLYRRTTWLHQALREGtrvqsveQIREVASGAAR-IRGETLGI 179
Cdd:cd12177    83 VDLKAATEHGVIVTRVPGAverdAVAEHA---VALILTVLRKINQASEAVKEG-------KWTERANFVGHeLSGKTVGI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 180 IGLGRVGQAVA-LRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQG 258
Cdd:cd12177   153 IGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 259 AFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRA 338
Cdd:cd12177   232 VILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKADH-PLLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDF 310
                         330
                  ....*....|.
gi 1249030266 339 ITGRIPDSLKN 349
Cdd:cd12177   311 LAGKEPKGILN 321
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
58-341 2.58e-59

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


Pssm-ID: 240662  Cd Length: 329  Bit Score: 196.99  E-value: 2.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  58 STQEIHEKVLNEAVGA---LMYHTITLMREDLEKFKAL---RIIVRIgSGFDNIDIKSAGELGIAVCNMPSASVEETADS 131
Cdd:cd12186    30 TTELLTPETVDLAKGYdgvVVQQTLPYDEEVYEKLAEYgikQIALRS-AGVDMIDLDLAKENGLKITNVPAYSPRAIAEF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 132 TLCHILNLYRRTTWLHQALREGT-RVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDG 210
Cdd:cd12186   109 AVTQALNLLRNTPEIDRRVAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 211 MErALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALD 290
Cdd:cd12186   182 LE-KFLLYYD-SLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALD 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 291 VHETE----PFSFSQGPLKDA--------PNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12186   260 TYENEtgyfNKDWSGKEIEDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEG 322
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
43-341 1.58e-57

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: 191.57  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  43 PILKDVATV-AFCDaqstqeiHEKVLNEAVGALM-YHTITLMRED-------LEKFKALRIIVRIGSGFDNIDIKSAGEL 113
Cdd:cd12169    19 SKLDDRAEVtVFND-------HLLDEDALAERLApFDAIVLMRERtpfpaalLERLPNLKLLVTTGMRNASIDLAAAKER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 114 GIAVCNMPSaSVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVeqirevasgAARIRGETLGIIGLGRVGQAVALRA 193
Cdd:cd12169    92 GIVVCGTGG-GPTATAELTWALILALARNLPEEDAALRAGGWQTTL---------GTGLAGKTLGIVGLGRIGARVARIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 194 KAFGFNVIFYDPYLSDGMERALGLQRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEK 273
Cdd:cd12169   162 QAFGMRVIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEG 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1249030266 274 ALAQALKEGRIRGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12169   242 ALLAALRAGRIAGAALDVFDVEPLPADH-PLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLAG 308
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
42-332 2.53e-57

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: 191.28  E-value: 2.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  42 MPILKDVATVAFCDAQSTQEihEKVLNEAVGA--LMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCN 119
Cdd:cd12161    20 APLEEQGHEFVYYDTKTTDT--AELIERSKDAdiVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 120 MPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQiREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFN 199
Cdd:cd12161    98 AAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIG-RE-------LAGKTVGIVGTGAIGLRVARLFKAFGCK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 200 VIFYDPYLSDGMErALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQAL 279
Cdd:cd12161   170 VLAYSRSEKEEAK-ALGIEYV-SLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADAL 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 280 KEGRIRGAALDVHETEPFSFSQGPLKDAPNLICTPHAAWYSEQAsIEMREEAA 332
Cdd:cd12161   248 NEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVAFATEEA-MEKRAEIV 299
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
39-342 2.67e-57

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: 191.72  E-value: 2.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  39 TVEMPILKDVATVaFCDAqstqeihekvlnEAVGALMYHTITlmREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVC 118
Cdd:cd12187    26 FTSQELLDDNVEE-FKDA------------EVISVFVYSRLD--AEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 119 NMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGF 198
Cdd:cd12187    91 NVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFE-------LAGKTLGVVGTGRIGRRVARIARGFGM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 199 NVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQA 278
Cdd:cd12187   164 KVLAYDVVPDEELAERLGFRYV-SLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 279 LKEGRIRGAALDVHETEPF----------SFSQGPLKDA---------PNLICTPHAAWYSEQASIEMREEAAREIRRAI 339
Cdd:cd12187   243 LKEGKLAGAGLDVLEQEEVlreeaelfreDVSPEDLKKLladhallrkPNVIITPHVAYNTKEALERILDTTVENIKAFA 322

                  ...
gi 1249030266 340 TGR 342
Cdd:cd12187   323 AGQ 325
PRK13243 PRK13243
glyoxylate reductase; Reviewed
60-356 3.84e-57

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 191.55  E-value: 3.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  60 QEIHEKVLNEAV---GALmyhtITLMRE--DLEKFKA---LRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADS 131
Cdd:PRK13243   32 REIPREVLLEKVrdvDAL----VTMLSEriDCEVFEAaprLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 132 TLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGM 211
Cdd:PRK13243  108 AWALLLATARRLVEADHFVRSGEWKRRGVAWHPLMFLGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 212 ERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV 291
Cdd:PRK13243  188 EKELGAEYR-PLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1249030266 292 HETEPfsFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLkncVNKEFL 356
Cdd:PRK13243  267 FEEEP--YYNEELFSLKNVVLAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNREVV 326
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 6.10e-57

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 190.20  E-value: 6.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  30 VALLDGR---DCTVEmpILKDVATVAFCDAQSTQEIHEKVLNEAVgaLMYHTITLMREDLEKFKALRIIVRIGSGFDNID 106
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 107 IKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSvEQIREVASGAARIRGETLGIIGLGRVG 186
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSES-PIFTHISRPLGEIKGKKWGIIGLGTIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 187 QAVALRAKAFGFNVIFYDPylsDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTAR 266
Cdd:PRK08410  158 KRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1249030266 267 GGLVDEKALAQALKEGRIrGAALDVHETEPFSfSQGPL---KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:PRK08410  234 GGIVNEKDLAKALDEKDI-YAGLDVLEKEPME-KNHPLlsiKNKEKLLITPHIAWASKEARKTLIEKVKENIKDFLEG 309
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
88-323 6.50e-54

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: 182.64  E-value: 6.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  88 KFKALRIivrigSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTtwlHQALregtrvqsveqirevas 167
Cdd:cd12183    70 KLIALRC-----AGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKI---HRAY----------------- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 168 gaARIR---------------GETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMErALGLQRVnTLQDLLFHSDC 232
Cdd:cd12183   125 --NRVRegnfsldgllgfdlhGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYPNPELA-KLGVEYV-DLDELLAESDI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 233 VTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSF----SQGPLKDA- 307
Cdd:cd12183   201 ISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFfedhSDEIIQDDv 280
                         250       260
                  ....*....|....*....|...
gi 1249030266 308 -------PNLICTPHAAWYSEQA 323
Cdd:cd12183   281 larllsfPNVLITGHQAFFTKEA 303
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
55-342 1.93e-53

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 181.05  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  55 DAQSTQEIHEKvLNEAVGALMyHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLC 134
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 135 HILNLYRRTTWLHQALREGtRVQSVEQ-------IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFNVIfydpyL 207
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-RWQQSSQfclldfpIVELE-------GKTLGLLGHGELGGAVARLAEAFGMRVL-----I 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 208 SDGMERALGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGA 287
Cdd:PRK06487  177 GQLPGRPARPDRL-PLDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1249030266 288 ALDVHETEPfSFSQGPL--KDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGR 342
Cdd:PRK06487  256 ATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
51-336 1.74e-49

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 170.85  E-value: 1.74e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  51 VAFCDAQSTQE-IHEKVLNEAVGALmyHTITLMREDLEKFKAL-------RIIvrigsGFDNIDIKSAGELGIAVCNM-- 120
Cdd:cd12185    27 VTLTKEPLTLEnAHLAEGYDGISIL--GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVty 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 121 PSASVeetADSTLCHILNLYRRTTW-LHQALREGTRVQSVeQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFN 199
Cdd:cd12185   100 SPNSV---ADYTVMLMLMALRKYKQiMKRAEVNDYSLGGL-QGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 200 VIFYDPYLSDGMERalGLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQAL 279
Cdd:cd12185   169 ILAYDPYPNEEVKK--YAEYV-DLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGL 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1249030266 280 KEGRIRGAALDVHETEPFSFSQ------------GPLKDAPNLICTPHAAWYSEQASIEMREEAAREIR 336
Cdd:cd12185   246 ESGKIGGAALDVIEGEDGIYYNdrkgdilsnrelAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLV 314
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
80-360 8.90e-48

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


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 166.58  E-value: 8.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  80 TLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQsv 159
Cdd:cd12167    61 PLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWG-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 160 eqiREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVnTLQDLLFHSDCVTLHCSL 239
Cdd:cd12167   139 ---WPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSLHAPL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 240 NEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPFSFSQgPLKDAPNLICTPHAAWY 319
Cdd:cd12167   215 TPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEPLPPDS-PLRTLPNVLLTPHIAGS 292
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1249030266 320 SEQASIEMREEAAREIRRAITGRIPdslKNCVNKEFLTQTT 360
Cdd:cd12167   293 TGDERRRLGDYALDELERFLAGEPL---LHEVTPERLARMA 330
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
101-337 4.00e-47

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


Pssm-ID: 240653  Cd Length: 304  Bit Score: 164.29  E-value: 4.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 101 GFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsveQIREVASGAARIRGETLGII 180
Cdd:cd12176    74 GTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG-------IWNKSATGSHEVRGKTLGII 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 181 GLGRVGQAVALRAKAFGFNVIFYDPylsdgmERALGL---QRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQ 257
Cdd:cd12176   147 GYGHIGSQLSVLAEALGMRVIFYDI------AEKLPLgnaRQVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKK 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 258 GAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFS----FSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAR 333
Cdd:cd12176   221 GAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngepFSS-PLQGLPNVILTPHIGGSTEEAQENIGLEVAG 299

                  ....
gi 1249030266 334 EIRR 337
Cdd:cd12176   300 KLVK 303
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
81-335 1.20e-46

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 163.05  E-value: 1.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  81 LMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNL-YRRTTWLHQALreGTRVQSV 159
Cdd:PRK06932   55 FTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALkHSLMGWYRDQL--SDRWATC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 160 EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDpylsdgmERALGLQRVNTL--QDLLFHSDCVTLHC 237
Cdd:PRK06932  133 KQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREGYTpfEEVLKQADIVTLHC 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 238 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPL----KDAPNLICT 313
Cdd:PRK06932  206 PLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPPE-KDNPLiqaaKRLPNLLIT 284
                         250       260
                  ....*....|....*....|..
gi 1249030266 314 PHAAWYSEQASIEMREEAAREI 335
Cdd:PRK06932  285 PHIAWASDSAVTTLVNKVAQNI 306
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
86-329 1.85e-46

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


Pssm-ID: 240633 [Multi-domain]  Cd Length: 301  Bit Score: 162.25  E-value: 1.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  86 LEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtrvqsvEQIREV 165
Cdd:cd12156    59 IAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAG------RWPKGA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 166 ASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGmeraLGLQRVNTLQDLLFHSDCVTLHCSLNEHNHH 245
Cdd:cd12156   133 FPLTRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPD----VPYRYYASLLELAAESDVLVVACPGGPATRH 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGP--LKDAPNLICTPHAAWYSEQA 323
Cdd:cd12156   209 LVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP----NVPaaLLDLDNVVLTPHIASATVET 284

                  ....*.
gi 1249030266 324 SIEMRE 329
Cdd:cd12156   285 RRAMGD 290
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
76-315 8.43e-46

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


Pssm-ID: 240627  Cd Length: 348  Bit Score: 161.73  E-value: 8.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  76 YHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTR 155
Cdd:cd05302    69 FHPAYMTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 156 vqsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERALGLQRVNTLQDLLFHSDCVT 234
Cdd:cd05302   149 -----NVADVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDVVT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDAPNLICTP 314
Cdd:cd05302   224 INCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP-APKDHPWRTMPNNAMTP 302

                  .
gi 1249030266 315 H 315
Cdd:cd05302   303 H 303
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
58-341 1.99e-45

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


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 160.15  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  58 STQEIHEKVLN-EAVGALMYHTITlmREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHI 136
Cdd:cd12157    34 SREELLRRCKDaDGLMAFMPDRID--ADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 137 LNLYRRTTWLHQALREGTRvqsvEQIREVASGAArIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERAL 215
Cdd:cd12157   112 IGLGRHILAGDRFVRSGKF----GGWRPKFYGTG-LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHpLDQAEEQAL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 216 GLQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE 295
Cdd:cd12157   187 NLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 296 -------PFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITG 341
Cdd:cd12157   266 dwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
57-321 9.23e-45

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


Pssm-ID: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 157.84  E-value: 9.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  57 QSTQEIHEKVlnEAVGALMYHTITLM-REDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCH 135
Cdd:cd12179    29 ISREEILAII--PQYDGLIIRSRFPIdKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 136 ILNLyrrttwLHQALREGTRVQSVEQIREVASGAaRIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERAl 215
Cdd:cd12179   107 LLAL------FNKLNRADQEVRNGIWDREGNRGV-ELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAYA- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 216 glQRVnTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE 295
Cdd:cd12179   179 --EQV-SLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYE 255
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1249030266 296 PFSF---SQGP-----LKDAPNLICTPH-AAWYSE 321
Cdd:cd12179   256 KASFesiFNQPeafeyLIKSPKVILTPHiAGWTFE 290
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
83-329 1.28e-43

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


Pssm-ID: 240660  Cd Length: 330  Bit Score: 155.53  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRI---IVRIgSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTT-WLHQALREGTRVQS 158
Cdd:cd12184    58 KENLEIYKEYGIkyvFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAyTASRTANKNFKVDP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 159 VEQIREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQrvnTLQDLLFHSDCVTLHCS 238
Cdd:cd12184   137 FMFSKE-------IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVVTFV---SLDELLKKSDIISLHVP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 239 -LNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV--HETEPF--SFSQGPLKDA------ 307
Cdd:cd12184   207 yIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVlnNEKEIFfkDFDGDKIEDPvvekll 286
                         250       260
                  ....*....|....*....|....*
gi 1249030266 308 ---PNLICTPHAAWYSEQASIEMRE 329
Cdd:cd12184   287 dlyPRVLLTPHIGSYTDEALSNMIE 311
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
81-335 2.11e-42

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 153.68  E-value: 2.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  81 LMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAV-----CNmpSASVEETADSTlchILNLYRRTTWLHQALREGTR 155
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVaevtgSN--SISVAEHVVMM---ILALVRNYEPSHRQAVEGGW 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 156 vqsveQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPY-LSDGMERALGLQRVNTLQDLLFHSDCVT 234
Cdd:PRK07574  179 -----NIADCVSRSYDLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDVVT 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 235 LHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHetepfsFSQGPLKD-----APN 309
Cdd:PRK07574  254 IHCPLHPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVW------FPQPAPADhpwrtMPR 327
                         250       260
                  ....*....|....*....|....*...
gi 1249030266 310 LICTPHAAW--YSEQASIemrEEAAREI 335
Cdd:PRK07574  328 NGMTPHISGttLSAQARY---AAGTREI 352
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
64-345 5.77e-41

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: 148.16  E-value: 5.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  64 EKVLNEAvGALMYHTITLmREDLEKFKALRIIVRIGSGFDNIDIKSAGElGIAVCNMP--SASVEETAdstLCHILNLYR 141
Cdd:cd12165    35 EEALEDA-DVLVGGRLTK-EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHgnSPAVAEHA---LALILALAK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 142 RTTWLHQALREGTRVQSVEQIREVASgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYdpylSDGMERALGLQRVN 221
Cdd:cd12165   109 RIVEYDNDLRRGIWHGRAGEEPESKE----LRGKTVGILGYGHIGREIARLLKAFGMRVIGV----SRSPKEDEGADFVG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 222 TLQDL---LFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV------- 291
Cdd:cd12165   181 TLSDLdeaLEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwrypsr 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1249030266 292 -HETEPFSFsqgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPD 345
Cdd:cd12165   261 gDPVAPSRY---PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPLL 312
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
105-315 2.00e-40

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 148.79  E-value: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 105 IDIKSAGELGIAVCNMP---SASVEETAdstLCHILNLYRRTTWLHQALREGTRVQSveqirevASGAARIRGETLGIIG 181
Cdd:PRK11790   89 VDLDAAAKRGIPVFNAPfsnTRSVAELV---IGEIILLLRGIPEKNAKAHRGGWNKS-------AAGSFEVRGKTLGIVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 182 LGRVGQAVALRAKAFGFNVIFYDPylsdgMER-ALG-LQRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGA 259
Cdd:PRK11790  159 YGHIGTQLSVLAESLGMRVYFYDI-----EDKlPLGnARQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1249030266 260 FLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQG---PLKDAPNLICTPH 315
Cdd:PRK11790  234 ILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfesPLRGLDNVILTPH 292
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
92-323 6.20e-39

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 142.96  E-value: 6.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  92 LRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREgtrvqsvEQIREVASGAAR 171
Cdd:PRK08605   70 IKQIAQRSAGFDTYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVRE-------HDFRWEPPILSR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 172 -IRGETLGIIGLGRVGQAVA-LRAKAFGFNVIFYDPYLSDGMerALGLQRVNTLQDLLFHSDCVTLHCSLNEHNHHLIND 249
Cdd:PRK08605  143 sIKDLKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDPFPNAKA--ATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 250 FTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICTPHAA 317
Cdd:PRK08605  221 DLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIA 300

                  ....*.
gi 1249030266 318 WYSEQA 323
Cdd:PRK08605  301 FYTDAA 306
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
98-320 5.61e-38

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: 140.74  E-value: 5.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  98 IGS---GFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLhqalregtrvqsveqirevasgaarIRG 174
Cdd:cd12158    61 VGTatiGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFS-------------------------LKG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 175 ETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLsdgmERALGLQRVNTLQDLLFHSDCVTLHCSLNEH----NHHLINDF 250
Cdd:cd12158   116 KTVGIVGVGNVGSRLARRLEALGMNVLLCDPPR----AEAEGDPGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDED 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 251 TIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDApnLICTPHAAWYS 320
Cdd:cd12158   192 FLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP-EIDLELLDKV--DIATPHIAGYS 258
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
59-356 6.14e-37

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 137.58  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  59 TQEIHEKVLNEAVGaLMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILN 138
Cdd:PRK15409   35 TVEQHAAAFAEAEG-LLGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 139 LYRRttwlhqALREGTRVQSVEQIREVASG--AARIRGETLGIIGLGRVGQAVALRAKaFGFN--VIFYDPYLSDGMERA 214
Cdd:PRK15409  114 TARR------VVEVAERVKAGEWTASIGPDwfGTDVHHKTLGIVGMGRIGMALAQRAH-FGFNmpILYNARRHHKEAEER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 215 LGLQRVNtLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHET 294
Cdd:PRK15409  187 FNARYCD-LDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQ 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1249030266 295 EPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPdslKNCVNKEFL 356
Cdd:PRK15409  266 EPLSVDS-PLLSLPNVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVE---KNCVNPQVA 323
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
82-354 8.72e-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: 136.88  E-value: 8.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  82 MREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGtRVQSVEQ 161
Cdd:cd05300    50 LPELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAER-RWQRRGP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 162 IREvasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVI-------FYDPYLSD--GMERalglqrvntLQDLLFHSDC 232
Cdd:cd05300   129 VRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVIgvrrsgrPAPPVVDEvyTPDE---------LDELLPEADY 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 233 VTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLIC 312
Cdd:cd05300   193 VVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEEPLP-ADSPLWDLPNVII 271
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1249030266 313 TPHAAWYSEqasiEMREEAA----REIRRAITGRipdSLKNCVNKE 354
Cdd:cd05300   272 TPHISGDSP----SYPERVVeiflENLRRYLAGE---PLLNVVDKD 310
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
85-322 1.30e-35

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


Pssm-ID: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 133.48  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  85 DLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRttwLHQALRegtrvQSVEQIRE 164
Cdd:cd12155    54 DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKG---LKKAYK-----NQKEKKWK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 165 VASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIfydpylsdGMER----ALGLQRVNTLQDL---LFHSDCVTLHC 237
Cdd:cd12155   126 MDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTsgrdVEYFDKCYPLEELdevLKEADIVVNVL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 238 SLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAA 317
Cdd:cd12155   198 PLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLP-KDSPLWDLDNVLITPHIS 276

                  ....*
gi 1249030266 318 WYSEQ 322
Cdd:cd12155   277 GVSEH 281
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
170-342 3.03e-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: 127.07  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 170 ARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPylSDGMERALGLQRVNTLQDLLFHSDCVTLHCSLNEHNHHLIND 249
Cdd:cd12180   131 GSLAGSTLGIVGFGAIGQALARRALALGMRVLALRR--SGRPSDVPGVEAAADLAELFARSDHLVLAAPLTPETRHLINA 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 250 FTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLICTPHAAWYSEQASIEMRE 329
Cdd:cd12180   209 DVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPEPLP-EGHPLYTHPRVRLSPHTSAIAPDGRRNLAD 287
                         170
                  ....*....|...
gi 1249030266 330 EAAREIRRAITGR 342
Cdd:cd12180   288 RFLENLARYRAGQ 300
PLN02928 PLN02928
oxidoreductase family protein
82-348 3.16e-32

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 125.18  E-value: 3.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  82 MRED---LEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSA---SVEETADSTLCHILNLYRRttwlHQALRegtr 155
Cdd:PLN02928   70 MRLDadiIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRK----QNEMQ---- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 156 vQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERALGLQRVNT------------L 223
Cdd:PLN02928  142 -ISLKARRLGEPIGDTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPNGDVddlvdekgghedI 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 224 QDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQgP 303
Cdd:PLN02928  221 YEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDD-P 299
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1249030266 304 LKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLK 348
Cdd:PLN02928  300 ILKHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPLTGIE 344
PLN02306 PLN02306
hydroxypyruvate reductase
101-341 8.13e-31

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 122.27  E-value: 8.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 101 GFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREvasgAARIRGETLGII 180
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEGWLPHLFV----GNLLKGQTVGVI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 181 GLGRVGQAVA-LRAKAFGFNVIFYDPYLSDGME----------RALGLQ-----RVNTLQDLLFHSDCVTLHCSLNEHNH 244
Cdd:PLN02306  172 GAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEkfvtaygqflKANGEQpvtwkRASSMEEVLREADVISLHPVLDKTTY 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 245 HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsFSQGPLKDAPNLICTPHAAWYSEQAS 324
Cdd:PLN02306  252 HLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEP--YMKPGLADMKNAVVVPHIASASKWTR 329
                         250
                  ....*....|....*..
gi 1249030266 325 IEMREEAAREIRRAITG 341
Cdd:PLN02306  330 EGMATLAALNVLGKLKG 346
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
86-323 4.76e-29

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 116.17  E-value: 4.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  86 LEKFKALRIIVRIgSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWLHQalregtRVQSVEQIREV 165
Cdd:PRK12480   65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIER------RVQAHDFTWQA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 166 ASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERalgLQRVNTLQDLLFHSDCVTLHCSLNEHNHH 245
Cdd:PRK12480  138 EIMSKPVKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAYPNKDLDF---LTYKDSVKEAIKDADIISLHVPANKESYH 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETE----PFSFSQGPLKDA--------PNLICT 313
Cdd:PRK12480  215 LFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaayfTNDWTNKDIDDKtlleliehERILVT 294
                         250
                  ....*....|
gi 1249030266 314 PHAAWYSEQA 323
Cdd:PRK12480  295 PHIAFFSDEA 304
PLN03139 PLN03139
formate dehydrogenase; Provisional
76-315 1.18e-28

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 116.10  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  76 YHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRR--TTWlHQALREG 153
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNflPGY-HQVVSGE 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 154 TRVQsveqirEVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDG-MERALGLQRVNTLQDLLFHSDC 232
Cdd:PLN03139  185 WNVA------GIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDPeLEKETGAKFEEDLDAMLPKCDV 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 233 VTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAPNLIC 312
Cdd:PLN03139  259 VVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPAP-KDHPWRYMPNHAM 337

                  ...
gi 1249030266 313 TPH 315
Cdd:PLN03139  338 TPH 340
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
84-339 2.03e-26

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: 108.35  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  84 EDLEKFKALRIIVRIGSGFDNIDiKSAGELGIAVCNMPSASVEET-ADSTLCHILNLYRRTTwlhqALREGTRVQSVEQI 162
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLVDPGLAQGmAEYVLAAVLRLHRDMD----RYAAQQRRGVWKPL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 163 REVASGAARIrgetlGIIGLGRVGQAVALRAKAFGFNVI--------------FYDPylsDGMERALGlqRVNTLQDLLf 228
Cdd:cd12164   126 PQRPAAERRV-----GVLGLGELGAAVARRLAALGFPVSgwsrspkdiegvtcFHGE---EGLDAFLA--QTDILVCLL- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 229 hsdcvtlhcSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPLKDAP 308
Cdd:cd12164   195 ---------PLTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLP-ADHPLWRHP 264
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1249030266 309 NLICTPHAawyseqASIEMREEAAREIRRAI 339
Cdd:cd12164   265 RVTVTPHI------AAITDPDSAAAQVAENI 289
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
101-340 1.17e-22

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 98.95  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 101 GFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLyrrttwlhqALREGtrvqsveqirevasgaARIRGETLGII 180
Cdd:PRK00257   68 GTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTL---------AEREG----------------VDLAERTYGVV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 181 GLGRVGQAVALRAKAFGFNVIFYDPYLSDgmerALGLQRVNTLQDLLFHSDCVTLHCSLN-EHNH---HLINDFTIKQMR 256
Cdd:PRK00257  123 GAGHVGGRLVRVLRGLGWKVLVCDPPRQE----AEGDGDFVSLERILEECDVISLHTPLTkEGEHptrHLLDEAFLASLR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 257 QGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfsfsQGPLKDAPN-LICTPHAAWYseqaSIEMREEAAREI 335
Cdd:PRK00257  199 PGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEP----QIDLELADLcTIATPHIAGY----SLDGKARGTAQI 270

                  ....*
gi 1249030266 336 RRAIT 340
Cdd:PRK00257  271 YQALC 275
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
129-342 7.82e-22

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 95.52  E-value: 7.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 129 ADSTLCHILNLYRRTTWLHQALREGTRVQSV--EQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIfydPY 206
Cdd:cd12160    96 AEHTLALILAAVRRLDEMREAQREHRWAGELggLQPLRPAGRLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT---GV 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 207 LSDGMERAlGLQRV--NTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRI 284
Cdd:cd12160   173 ARSAGERA-GFPVVaeDELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRL 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1249030266 285 RGAALDVHETEPFSFSQgPLKDAPNLICTPHAAWYSEQASIEMreeAAREIRRAITGR 342
Cdd:cd12160   252 GGAALDVTATEPLPASS-PLWDAPNLILTPHAAGGRPQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
129-317 1.10e-21

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 94.64  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 129 ADSTLCHILNLYRRttwLHQALREGTRVQSveqirEVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYD--PY 206
Cdd:cd12159    88 AEHALALLLAGLRQ---LPARARATTWDPA-----EEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNrsGR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 207 LSDGMERALglqRVNTLQDLLFHSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRG 286
Cdd:cd12159   160 PVEGADETV---PADRLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAG 236
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1249030266 287 AALDVHETEPfsFSQG-PLKDAPNLICTPHAA 317
Cdd:cd12159   237 AALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
83-347 1.17e-20

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 91.88  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  83 REDLEKFKALRIIVRIGSGFDNIdIKSAGElGIAVCNMPSASVEETADSTLCHILNLYRRttwLHQALREGTRVQ-SVEQ 161
Cdd:cd12166    52 LEALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCNARGVHDASTAELAVALILASLRG---LPRFVRAQARGRwEPRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 162 IREVAsgaarirGETLGIIGLGRVGQAVALRAKAFGFNVIfydpylsdgmeralglqRVNT-------------LQDLLF 228
Cdd:cd12166   127 TPSLA-------DRRVLIVGYGSIGRAIERRLAPFEVRVT-----------------RVARtarpgeqvhgideLPALLP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 229 HSDCVTLHCSLNEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRgAALDVHETEPfsFSQG-PLKDA 307
Cdd:cd12166   183 EADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEP--LPPGhPLWSA 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1249030266 308 PNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSL 347
Cdd:cd12166   260 PGVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLENV 299
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
173-321 4.41e-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: 240640  Cd Length: 334  Bit Score: 85.02  E-value: 4.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 173 RGETLGIIGLGRVGQAVALRAKAFGFNVIFY-------------DPYLSDGMERALGL-----------QRVNTL--QDL 226
Cdd:cd12163   132 VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkdDGYIVPGTGDPDGSipsawfsgtdkASLHEFlrQDL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 227 lfhsDCVTLHCSLNEHNHHLIN--DFTIKQMRqGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSfSQGPL 304
Cdd:cd12163   212 ----DLLVVSLPLTPATKHLLGaeEFEILAKR-KTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPLP-ADHPL 285
                         170
                  ....*....|....*..
gi 1249030266 305 KDAPNLICTPHAAWYSE 321
Cdd:cd12163   286 WSAPNVIITPHVSWQTQ 302
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
73-320 1.78e-15

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 77.64  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  73 ALMYHTITLMREDLEKFKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETADSTLCHILNLYRRTTWlhqALRE 152
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGF---SLHD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 153 gtrvqsveqirevasgaarirgETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSDGMERAlglqRVNTLQDLLFHSDC 232
Cdd:PRK15438  117 ----------------------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEG----DFRSLDELVQEADI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 233 VTLHCSLNEHNH----HLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPfSFSQGPLKDAP 308
Cdd:PRK15438  171 LTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLKKVD 249
                         250
                  ....*....|..
gi 1249030266 309 nlICTPHAAWYS 320
Cdd:PRK15438  250 --IGTPHIAGYT 259
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
57-337 3.51e-15

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


Pssm-ID: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 75.80  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  57 QSTQEIHEKVlNEAVGALMYHTITLMREDLEKFKALRIIVRIGSGFD----NIDIKSAGELGIAVCNMPS---ASVEETA 129
Cdd:cd12170    35 ESDEEIIERI-GDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDygdEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 130 DSTLCHILNLYRRTTWLHQALRegtrvqsveqirevasgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSD 209
Cdd:cd12170   114 ISELIRLLHGFGGKQWKEEPRE--------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 210 GMERALGlqRVNTLQDLLFHSDCVTLHcsLNEhNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGrirGAAL 289
Cdd:cd12170   174 DAEAKGI--RYLPLNELLKTVDVICTC--LPK-NVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLKAS---GYNI 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1249030266 290 DVHETEPfSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRR 337
Cdd:cd12170   246 FDCDTAG-ALGDEELLRYPNVICTNKSAGWTRQAFERLSQKVLANLEE 292
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
90-354 2.65e-14

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 73.38  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  90 KALRIIVRIGSGFDNIDIKSAGElGIAVCNMPSA---SVEETADSTLchiLNLYRRTTWLHQALREGTRVQSVEQIreva 166
Cdd:PRK06436   48 KKTKMIQSLSAGVDHIDVSGIPE-NVVLCSNAGAysiSVAEHAFALL---LAWAKNICENNYNMKNGNFKQSPTKL---- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 167 sgaarIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYD-PYLSDGMERAlglqrVNTLQDLLFHSDCVTLHCSLNEHNHH 245
Cdd:PRK06436  120 -----LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTrSYVNDGISSI-----YMEPEDIMKKSDFVLISLPLTDETRG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 246 LINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPlkdaPNLICTPH-AAWYSEQAS 324
Cdd:PRK06436  190 MINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPIITETNP----DNVILSPHvAGGMSGEIM 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 1249030266 325 IEMREEAAREIRRAITGRiPdslKNCVNKE 354
Cdd:PRK06436  266 QPAVALAFENIKNFFEGK-P---KNIVRKE 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
85-310 8.78e-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: 65.71  E-value: 8.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  85 DLEKFKALRIIVRIGSGFDNIDIKSA-GELGIAVCNMPSASVEETADStlchiLNLYRRttwlhQALREGTRVQSVeQIR 163
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTEAlARAGLTAIAVEGVELPLLTSN-----SIGAGE-----LSVQFIARFLEV-QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 164 EVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVIFYD-PYLSDGMERALGLQRVNTLQDLLFHSDCVTLHCSLNEH 242
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDiNVEALEQLEELGGKNVEELEEALAEADVIVTTTLLPGK 229
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 243 NHHLINDFT-IKQMRQGAFLVNTARG-GLVDEKALAQALKEGRIRGAALDVHETEPFSFSQGPLKDAPNL 310
Cdd:cd12154   230 RAGILVPEElVEQMKPGSVIVNVAVGaVGCVQALHTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
73-340 2.81e-09

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 58.27  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266  73 ALMYHTITLMREDlekfKALRIIVRIGSGFDNIDIKSAGELGIAVCNMPSASVEETA------DSTLCHILNLYRRTTwL 146
Cdd:PRK15469   42 ALVWHPPVEMLAG----RDLKAVFALGAGVDSILSKLQAHPEMLDPSVPLFRLEDTGmgeqmqEYAVSQVLHWFRRFD-D 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 147 HQALREGTRVQSVEQIRevasgaariRGE-TLGIIGLGRVGQAVALRAKAFGFNVIFYDPYLSD--GMERALG------- 216
Cdd:PRK15469  117 YQALQNSSHWQPLPEYH---------REDfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKSwpGVQSFAGreelsaf 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249030266 217 LQRVNTLQDLLFHSdcvtlhcslnEHNHHLINDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHETEP 296
Cdd:PRK15469  188 LSQTRVLINLLPNT----------PETVGIINQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREP 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1249030266 297 FSfSQGPLKDAPNLICTPHAawyseqASIEMREEAAREIRRAIT 340
Cdd:PRK15469  258 LP-PESPLWQHPRVAITPHV------AAVTRPAEAVEYISRTIA 294
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
177-227 7.02e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 38.19  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1249030266 177 LGIIGLGRVGQAVALRAKAFGFNVIFYD--PYLSDGMERAlGLQRVNTLQDLL 227
Cdd:PRK09599    3 LGMIGLGRMGGNMARRLLRGGHEVVGYDrnPEAVEALAEE-GATGADSLEELV 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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