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Conserved domains on  [gi|501170175|ref|WP_012214104|]
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Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Burkholderia multivorans]

Protein Classification

NAD(P) transhydrogenase subunit alpha( domain architecture ID 10143114)

NAD(P) transhydrogenase subunit alpha is part of the enzyme complex that catalyzes the transhydrogenation between NADH and NADP which is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-374 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


:

Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 568.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAF-GADIVLKVQAPTDAE 79
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  80 LPSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAqNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDeerdaAQGVGGYARPMPPSW 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEED-----AEGAGGYAKELSEEF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 239 LARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIVHNGV 318
Cdd:cd05304  236 LAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQ--------GGNCELTVPGETVVTNGV 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 319 TIAGHTNLASMVASDASALYARNLLDFMKLIVTKEGVLNIDLADDIVAATLLCRDG 374
Cdd:cd05304  308 TIIGPTNLPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDEIVRGTLVTHDG 363
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-374 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 568.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAF-GADIVLKVQAPTDAE 79
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  80 LPSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAqNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDeerdaAQGVGGYARPMPPSW 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEED-----AEGAGGYAKELSEEF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 239 LARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIVHNGV 318
Cdd:cd05304  236 LAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQ--------GGNCELTVPGETVVTNGV 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 319 TIAGHTNLASMVASDASALYARNLLDFMKLIVTKEGVLNIDLADDIVAATLLCRDG 374
Cdd:cd05304  308 TIIGPTNLPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-375 1.10e-175

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 492.98  E-value: 1.10e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQsAAFGADIVLKVQAPTDAEL 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDA-ELLGADIVLKVRPPSAEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  81 PSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAA 159
Cdd:COG3288   80 AALKPGAVLIGFLDPLgNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 160 GTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPyetdeerDAAQGVGGYARPMPPSWL 239
Cdd:COG3288  160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELA-------IDANGAGGYAKELSEEEK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 240 ARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIVHNGVT 319
Cdd:COG3288  233 AKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQ--------GGNCELTVPGETVTKNGVT 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 320 IAGHTNLASMVASDASALYARNLLDFMKLIVtKEGVLNIDLADDIVAATLLCRDGE 375
Cdd:COG3288  305 IIGPTNLPSRLPAHASQLYAKNLLNFLELLV-KDGALALDLEDEIVAGTLLTHDGE 359
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-377 1.30e-149

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 432.33  E-value: 1.30e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFGADIVLKVQAPTDAEL 80
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  81 PSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAA 159
Cdd:PRK09424  81 ALLREGATLVSFIWPAqNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 160 GTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDEErdaaqGVGGYARPMPPSWL 239
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGG-----SGDGYAKVMSEEFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 240 ARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIV-HNGV 318
Cdd:PRK09424 236 KAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAEN--------GGNCELTVPGEVVVtDNGV 307

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 319 TIAGHTNLASMVASDASALYARNLLDFMKLIV-TKEGVLNIDLADDIVAATLLCRDGEVT 377
Cdd:PRK09424 308 TIIGYTDLPSRLPTQSSQLYGTNLVNLLKLLCpEKDGNIVVDFDDVVIRGVTVVRDGEIT 367
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 3-377 6.98e-110

NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of alpha 2 beta 2 tetramer that couples the proton transport across the membrane to the reversible transfer of hydride ion equivalents between NAD and NADP. An alternate name is pyridine nucleotide transhydrogenase alpha subunit. The N-terminal region is homologous to alanine dehydrogenase. In some species, such as Rhodospirillum rubrum, the alpha chain is replaced by two shorter chains, both with some homology to the full-length alpha chain modeled here. These score below the trusted cutoff. [Energy metabolism, Electron transport]


Pssm-ID: 273140 [Multi-domain]  Cd Length: 512  Bit Score: 331.25  E-value: 6.98e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175    3 IGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFGADIVLKVQAPTDAELPS 82
Cdd:TIGR00561   2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   83 LKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAAGT 161
Cdd:TIGR00561  82 LKEGAALVSFIWPAqNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAGK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  162 VKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLdvpyETDEERDAAQGvGGYARPMPPSWLAR 241
Cdd:TIGR00561 162 VPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFL----EIDFKEEAGSG-DGYAKVMSDAFIKA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  242 QAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAgrgpevdgRKGGNCPLTVADQVI-VHNGVTI 320
Cdd:TIGR00561 237 AMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAA--------ANGGNCEYTQAGEIFtTENGVKV 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 501170175  321 AGHTNLASMVASDASALYARNLLDFMKLIVT-KEGVLNIDLADDIVAATLLCRDGEVT 377
Cdd:TIGR00561 309 IGYTDFPGRLPTQSSQLYGTNLVNLLKLLCKeKDGNINIDFDDVVIRGVTVIRAGEET 366
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-377 1.05e-72

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 225.45  E-value: 1.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  140 AVLVAASLYPRFLPMLMTAAGTV---KAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIES-LGAKFLDVpy 215
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  216 etdeerdaaqgvggyarpmppswLARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpe 295
Cdd:pfam01262  79 -----------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQ--- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  296 vdgrkGGNCP---LTVADQVIVH-NGVTIAGHTNLASMVASDASALYARNLLDFMKLIVTKeGVLNIDLADDIVAATLLC 371
Cdd:pfam01262 133 -----GGNVEtsrPTTHGEPVYVvDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADK-GLKAALLEDEALRAGLNT 206


                  ....*.
gi 501170175  372 RDGEVT 377
Cdd:pfam01262 207 HDGKIT 212
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-134 5.18e-53

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 172.21  E-value: 5.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175     4 GVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFG-ADIVLKVQAPTDAELPS 82
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWAdADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 501170175    83 LKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQAN 134
Cdd:smart01003  81 LREGQILFGYLHPAaNPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-374 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 568.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAF-GADIVLKVQAPTDAE 79
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  80 LPSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAqNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDeerdaAQGVGGYARPMPPSW 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEED-----AEGAGGYAKELSEEF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 239 LARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIVHNGV 318
Cdd:cd05304  236 LAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQ--------GGNCELTVPGETVVTNGV 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 319 TIAGHTNLASMVASDASALYARNLLDFMKLIVTKEGVLNIDLADDIVAATLLCRDG 374
Cdd:cd05304  308 TIIGPTNLPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-375 1.10e-175

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 492.98  E-value: 1.10e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQsAAFGADIVLKVQAPTDAEL 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDA-ELLGADIVLKVRPPSAEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  81 PSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAA 159
Cdd:COG3288   80 AALKPGAVLIGFLDPLgNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 160 GTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPyetdeerDAAQGVGGYARPMPPSWL 239
Cdd:COG3288  160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELA-------IDANGAGGYAKELSEEEK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 240 ARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIVHNGVT 319
Cdd:COG3288  233 AKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQ--------GGNCELTVPGETVTKNGVT 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 320 IAGHTNLASMVASDASALYARNLLDFMKLIVtKEGVLNIDLADDIVAATLLCRDGE 375
Cdd:COG3288  305 IIGPTNLPSRLPAHASQLYAKNLLNFLELLV-KDGALALDLEDEIVAGTLLTHDGE 359
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-377 1.30e-149

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 432.33  E-value: 1.30e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFGADIVLKVQAPTDAEL 80
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  81 PSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAA 159
Cdd:PRK09424  81 ALLREGATLVSFIWPAqNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 160 GTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDEErdaaqGVGGYARPMPPSWL 239
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGG-----SGDGYAKVMSEEFI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 240 ARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGNCPLTVADQVIV-HNGV 318
Cdd:PRK09424 236 KAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAEN--------GGNCELTVPGEVVVtDNGV 307

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 319 TIAGHTNLASMVASDASALYARNLLDFMKLIV-TKEGVLNIDLADDIVAATLLCRDGEVT 377
Cdd:PRK09424 308 TIIGYTDLPSRLPTQSSQLYGTNLVNLLKLLCpEKDGNIVVDFDDVVIRGVTVVRDGEIT 367
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 3-377 6.98e-110

NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of alpha 2 beta 2 tetramer that couples the proton transport across the membrane to the reversible transfer of hydride ion equivalents between NAD and NADP. An alternate name is pyridine nucleotide transhydrogenase alpha subunit. The N-terminal region is homologous to alanine dehydrogenase. In some species, such as Rhodospirillum rubrum, the alpha chain is replaced by two shorter chains, both with some homology to the full-length alpha chain modeled here. These score below the trusted cutoff. [Energy metabolism, Electron transport]


Pssm-ID: 273140 [Multi-domain]  Cd Length: 512  Bit Score: 331.25  E-value: 6.98e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175    3 IGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFGADIVLKVQAPTDAELPS 82
Cdd:TIGR00561   2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   83 LKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAAGT 161
Cdd:TIGR00561  82 LKEGAALVSFIWPAqNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAGK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  162 VKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLdvpyETDEERDAAQGvGGYARPMPPSWLAR 241
Cdd:TIGR00561 162 VPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFL----EIDFKEEAGSG-DGYAKVMSDAFIKA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  242 QAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAgrgpevdgRKGGNCPLTVADQVI-VHNGVTI 320
Cdd:TIGR00561 237 AMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAA--------ANGGNCEYTQAGEIFtTENGVKV 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 501170175  321 AGHTNLASMVASDASALYARNLLDFMKLIVT-KEGVLNIDLADDIVAATLLCRDGEVT 377
Cdd:TIGR00561 309 IGYTDFPGRLPTQSSQLYGTNLVNLLKLLCKeKDGNINIDFDDVVIRGVTVIRAGEET 366
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-377 1.05e-72

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 225.45  E-value: 1.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  140 AVLVAASLYPRFLPMLMTAAGTV---KAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIES-LGAKFLDVpy 215
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  216 etdeerdaaqgvggyarpmppswLARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpe 295
Cdd:pfam01262  79 -----------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQ--- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  296 vdgrkGGNCP---LTVADQVIVH-NGVTIAGHTNLASMVASDASALYARNLLDFMKLIVTKeGVLNIDLADDIVAATLLC 371
Cdd:pfam01262 133 -----GGNVEtsrPTTHGEPVYVvDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADK-GLKAALLEDEALRAGLNT 206


                  ....*.
gi 501170175  372 RDGEVT 377
Cdd:pfam01262 207 HDGKIT 212
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 3-349 8.63e-69

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 219.20  E-value: 8.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   3 IGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSA--AFGADIVLKVQAPTDAEL 80
Cdd:cd01620    2 LGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAASkeAYSADIIVKLKEPEFAEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  81 PSLKRGAVLVGMLE-PFNAEQAAKLAATGVTGFALEaaprTTRAQSLDVLSSQANIAGYKAVLVAASLYPRFLPMLMTAA 159
Cdd:cd01620   82 DLIKKGQLLVTFLHaATNRGVVEVLMRKKLTAYALE----DLENDFRPRLAPNSNIAGYAGVQLGAYELARIQGGRMGGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 160 GTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLdvpyetdeerdaaqgvggyarpmppswL 239
Cdd:cd01620  158 GGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRL---------------------------R 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 240 ARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAgrgpevdgRKGGNCPL---TVADQVIVHN 316
Cdd:cd01620  211 YSQKEELEKELKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAA--------DQGGNDETsipTTEGVPTYEV 282

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 501170175 317 -GVTIAGHTNLASMVASDASALYARNLLDFM-KLI 349
Cdd:cd01620  283 dGVVIYGVDNMPSLVPREASELLSKNLLPYLvKLA 317
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-134 5.18e-53

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 172.21  E-value: 5.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175     4 GVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAAFG-ADIVLKVQAPTDAELPS 82
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWAdADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 501170175    83 LKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRTTRAQSLDVLSSQAN 134
Cdd:smart01003  81 LREGQILFGYLHPAaNPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-289 3.31e-49

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 169.81  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSA-AFG-ADIVLKVQAPTDA 78
Cdd:COG0686    1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEeVFAqADLIVKVKEPQPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  79 ELPSLKRGAVLVGMLEpFNA--EQAAKLAATGVTGFALEAAprTTRAQSLDVLSSQANIAGYKAVLVAASlyprflpMLM 156
Cdd:COG0686   81 EYALLRPGQILFTYLH-LAAdpELTEALLEKGVTAIAYETV--EDPDGSLPLLAPMSEIAGRMAIQIGAE-------YLE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 157 TAAGT----------VKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLgakfldvpyetdeerdaaqg 226
Cdd:COG0686  151 KPNGGrgvllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDI-------------------- 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501170175 227 VGGYARPmppswLARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLA 289
Cdd:COG0686  211 FGGRVTT-----LYSNPANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVA 268
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 1-293 4.12e-49

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 169.12  E-value: 4.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELT-DQSAAFG-ADIVLKVQAPTDA 78
Cdd:cd05305    1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVpTAEEVWAkADLIVKVKEPLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  79 ELPSLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAprTTRAQSLDVLSSQANIAGYKAVLVAASLyprflpmLMT 157
Cdd:cd05305   81 EYDLLREGQILFTYLHLAaDKELTEALLEKKVTAIAYETI--EDEDGSLPLLAPMSEIAGRLAVQIGAEY-------LEK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 158 AAG----------TVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIES-LGAKFldvpyETdeerdaaqg 226
Cdd:cd05305  152 PNGgrgvllggvpGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDiFGGRV-----TT--------- 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501170175 227 vggyarpmppswLARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRG 293
Cdd:cd05305  218 ------------LYSNPANLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQG 272
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 145-322 3.15e-48

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 160.37  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   145 ASLYPRFLPMLMTAAGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIES-LGAKFLDvpyetdeerda 223
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTT----------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   224 aqgvggyarpmppswLARQAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRgpevdgrkGGN 303
Cdd:smart01002  70 ---------------LYSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQ--------GGC 126

                          170       180
                   ....*....|....*....|...
gi 501170175   304 C----PLTVADQVIVHNGVTIAG 322
Cdd:smart01002 127 IetsrPTTHDDPTYVVDGVVHYC 149
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 4-136 6.61e-48

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 158.74  E-value: 6.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175    4 GVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELTDQSAA--FGADIVLKVQAPTDAELP 81
Cdd:pfam05222   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVDTAAEvwAEADLILKVKEPQPEEYA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175   82 SLKRGAVLVGMLEPF-NAEQAAKLAATGVTGFALEAAPRtTRAQSLDVLSSQANIA 136
Cdd:pfam05222  81 LLREGQTLITFLHPAaNPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANIA 135
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 3-345 1.79e-40

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: 145.07  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   3 IGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGA-ELTDQSAAFGADIVLKVQAPTDAELP 81
Cdd:cd12154    1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAiVVTLAKALWSLDVVLKVKEPLTNAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  82 SLKRGAVLVGMLEPF----NAEQAAKLAATGVTGFALEAAPRTtraqsldVLSSQANIAGYKAVLVAASLYPRFLPMLMT 157
Cdd:cd12154   81 ALIQKLGDRLLFTYTigadHRDLTEALARAGLTAIAVEGVELP-------LLTSNSIGAGELSVQFIARFLEVQQPGRLG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 158 AAGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFldvpyetdeerdaaqgvggyarpmpps 237
Cdd:cd12154  154 GAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKN--------------------------- 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 238 wlarqAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGrgpevdgrKGGNCPLTVADQVIVHNG 317
Cdd:cd12154  207 -----VEELEEALAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVG--------AVGCVQALHTQLLEEGHG 273

                        330       340       350
                 ....*....|....*....|....*....|...
gi 501170175 318 VTIAGHTNL-----ASMVASDASALYARNLLDF 345
Cdd:cd12154  274 VVHYGDVNMpgpgcAMGVPWDATLRLAANTLPA 306
alaDH TIGR00518
alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes ...
 1-298 4.47e-34

alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129609 [Multi-domain]  Cd Length: 370  Bit Score: 129.65  E-value: 4.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175    1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAASYPDEAYAAAGAELT-DQSAAFGADIVLKVQAPTDAE 79
Cdd:TIGR00518   1 MRIGVPKEIKNNEFRVALTPAGVAELTSRGHEVLVEAGAGEGSGFTDAAYKAAGAELVaTAKQVWDAELVLKVKEPLPEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   80 LPSLKRGAVLVGMLE-PFNAEQAAKLAATGVTGFALEAAprTTRAQSLDVLSSQANIAGYKAVLVAASLYPRF---LPML 155
Cdd:TIGR00518  81 YGYLRHGQILFTYLHlAAERALTDALLDSGTTAIAYETV--QTADGALPLLAPMSEVAGRLAAQVGAYHLEKTqggRGVL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  156 MTAAGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETdeerdaaqgvggyarpmp 235
Cdd:TIGR00518 159 LGGVPGVEPGDVTIIGGGVVGTNAAKMANGLGATVTILDINIDRLRQLDAEFGGRIHTRYSN------------------ 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501170175  236 pswlarqAALVHERAKQADIVITTALIPGRPAPTLISAETVQAMKPGSVLVDLAAGRGPEVDG 298
Cdd:TIGR00518 221 -------AYEIEDAVKRADLLIGAVLIPGAKAPKLVSNSLVAQMKPGAVIVDVAIDQGGCVET 276
SDH cd12188
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ...
 1-81 8.72e-10

Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure.


Pssm-ID: 240664 [Multi-domain]  Cd Length: 351  Bit Score: 59.55  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVSVAKGAGTAasYPDEAYAAAGAELtdqsAAFGAdivlKVQAPTDA-- 78
Cdd:cd12188    1 THLWLRAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRI--FPDEEYEAVGCEL----VPAGS----WVNAPKDAii 70


                 ....*..
gi 501170175  79 ----ELP 81
Cdd:cd12188   71 lglkELP 77
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 1-319 1.19e-08

N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase.


Pssm-ID: 240658 [Multi-domain]  Cd Length: 295  Bit Score: 55.70  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   1 MHIGVPAETRANEARVAATPETVKKYAAAGHRVsVAKGAGTAASYPDEAYAAAGAE-LTDQSAAFGADIVLKVqAPTDAE 79
Cdd:cd12181    1 KTGGFGISNKENEKRVPLLPADLERIPLREQLY-FEEGYGERLGISDEEYAALGAGiVSREEILAKCDVICDP-KPGDAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175  80 LPSLKRGAVLVGMLEPFNAEQAAKLA-ATGVTGFALEA------APRttraqslDVLSSQANIAGYKAVLVAASLYPRFl 152
Cdd:cd12181   79 YLEILEGQILWGWVHCVQDKEITQLAiDKKLTLIAWEDmfewskIGR-------HVFYKNNELAGYAAVLHALQLYGIT- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 153 PMLMTaagtvkaaRVLVLGAGvaglqaiATAKrlGAVieasdvrpavkeQIESLGAKFLDVpyetdeerdaaqgvggYAR 232
Cdd:cd12181  151 PYRQT--------KVAVLGFG-------NTAR--GAI------------RALKLGGADVTV----------------YTR 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 233 pmppswlaRQAALVHERAKQADIVITTALI-PGRPAPtLISAETVQAMKPGSVLVDLAAGRGPEVDGRKggncPLTVADQ 311
Cdd:cd12181  186 --------RTEALFKEELSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFAK----PTTFDDP 252


                 ....*...
gi 501170175 312 VIVHNGVT 319
Cdd:cd12181  253 IYKVDGID 260
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 155-230 2.03e-05

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 46.09  E-value: 2.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501170175 155 LMTAAGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDEERDAAQGVGGY 230
Cdd:cd08254  157 VVRAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGLGGG 232
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 154-231 6.65e-05

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 44.23  E-value: 6.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501170175 154 MLMTAAGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLDVPYETDEERDAAQGVGGYA 231
Cdd:cd05188  125 ALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGA 202
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 159-228 1.06e-03

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 40.68  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGAV-IEASDVRPAVKEQIESLGAKFLDVPYETD--EERDAAQGVG 228
Cdd:cd05281  159 AGDVSGKSVLITGCGPIGLMAIAVAKAAGASlVIASDPNPYRLELAKKMGADVVINPREEDvvEVKSVTDGTG 231
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 159-236 1.12e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 40.75  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGA-VIEASDVRPAVKEQIESLGAKFLDVPYETDEERDAAQGVGGYARPMPP 236
Cdd:cd08262  157 ARLTPGEVALVIGCGPIGLAVIAALKARGVgPIVASDFSPERRALALAMGADIVVDPAADSPFAAWAAELARAGGPKPA 235
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 159-208 1.94e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 39.74  E-value: 1.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGA--VIeASDVRPAVKEQIESLGA 208
Cdd:COG1063  157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAarVI-VVDRNPERLELARELGA 207
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
240-297 2.48e-03

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 39.78  E-value: 2.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501170175 240 ARQAALVHERAKQADIVitTALIPGRPAPT-LISAETVQAMKPGSVLVDLAagRGPEVD 297
Cdd:PRK11790 191 ARQVGSLEELLAQSDVV--SLHVPETPSTKnMIGAEELALMKPGAILINAS--RGTVVD 245
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 247-297 3.61e-03

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: 39.04  E-value: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501170175 247 HERAKQADIVITTAliPGRPApT--LISAETVQAMKPGSVLVDLaaGRGPEVD 297
Cdd:cd05300  184 DELLPEADYVVNAL--PLTPE-TrgLFNAERFAAMKPGAVLINV--GRGSVVD 231
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 159-325 4.53e-03

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 38.55  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 159 AGTVKAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPAVKEQIESLGAKFLdVPYETDEERDAAQGVGGyarpmppsw 238
Cdd:COG1064  158 AGVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHV-VNSSDEDPVEAVRELTG--------- 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 239 larqaalvherakqADIVITTAlipgrPAPTLIsAETVQAMKPGSVLVdlAAGRGPEvdgrkggncPLTVADQVIVHNGV 318
Cdd:COG1064  228 --------------ADVVIDTV-----GAPATV-NAALALLRRGGRLV--LVGLPGG---------PIPLPPFDLILKER 276


                 ....*..
gi 501170175 319 TIAGHTN 325
Cdd:COG1064  277 SIRGSLI 283
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 166-197 5.51e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 38.32  E-value: 5.51e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 501170175 166 RVLVLGAGVAGLQAIATAKRLGAVIEASDVRP 197
Cdd:cd08261  162 TVLVVGAGPIGLGVIQVAKARGARVIVVDIDD 193
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 158-225 7.65e-03

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 38.01  E-value: 7.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501170175 158 AAGTVKAAR-VLVLGAGVAGLQAIATAKRLGA----VIEASDVRpavKEQIESLGAKFLDVPYETDEERDAAQ 225
Cdd:cd08231  171 RAGPVGAGDtVVVQGAGPLGLYAVAAAKLAGArrviVIDGSPER---LELAREFGADATIDIDELPDPQRRAI 240
SDH_like cd05199
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ...
 2-81 7.94e-03

Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.


Pssm-ID: 240623 [Multi-domain]  Cd Length: 319  Bit Score: 37.98  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175   2 HIGVPAETRAN-EARVAATPETVKKYAA--AGHRVSVAKGAGTAasYPDEAYAAAGAELTDQSAAfgADIVLKV-QAPTD 77
Cdd:cd05199    1 KIGIIREGKTPpDRRVPLTPEQCKELQAkyPGVEIFVQPSPVRC--FKDEEYRAAGIEVVEDLSD--CDILLGVkEVPIE 76


                 ....
gi 501170175  78 AELP 81
Cdd:cd05199   77 QLIP 80
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 163-210 8.41e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 38.14  E-value: 8.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501170175 163 KAARVLVLGAGVAGLQAIATAKRLGAVIEASDVRPA---VKEQIESLGAKF 210
Cdd:COG0771    3 KGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPApelAAAELEAPGVEV 53
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
 232-297 8.53e-03

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: 37.91  E-value: 8.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501170175 232 RPMPP---SWLARQAALVHERAKQADIVITTAliPGRPAPT-LISAETVQAMKPGSVLVDLAagRGPEVD 297
Cdd:cd12168  186 SRLPEeleKALATYYVSLDELLAQSDVVSLNC--PLTAATRhLINKKEFAKMKDGVIIVNTA--RGAVID 251
 
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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