NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1475498356|ref|WP_118839645|]
View 

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinibacter ruber]

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

CATH:  3.40.50.720
EC:  7.1.1.1
Gene Ontology:  GO:0070403|GO:0016491
PubMed:  17323922

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 3-366 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: 540.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATF-DADIIAKVAPPSD 81
Cdd:cd05304     1 MTIGVPKETAPGERRVALTPETVKKLVK--LGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  82 DEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLT 161
Cdd:cd05304    79 EEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 162 TAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEAdQDESGYAEQVEKEKQE 241
Cdd:cd05304   159 TAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDA-EGAGGYAKELSEEFLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 242 RQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLPA 321
Cdd:cd05304   238 KQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1475498356 322 EMPVHASELYAKTVAAMIEE-GLEADAFAPDFDDEIFAESCLTRDG 366
Cdd:cd05304   318 RLPTQASQLYAKNLLNFLELlVKDDGELTLDLEDEIVRGTLVTHDG 363
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 3-366 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: 540.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATF-DADIIAKVAPPSD 81
Cdd:cd05304     1 MTIGVPKETAPGERRVALTPETVKKLVK--LGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  82 DEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLT 161
Cdd:cd05304    79 EEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 162 TAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEAdQDESGYAEQVEKEKQE 241
Cdd:cd05304   159 TAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDA-EGAGGYAKELSEEFLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 242 RQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLPA 321
Cdd:cd05304   238 KQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1475498356 322 EMPVHASELYAKTVAAMIEE-GLEADAFAPDFDDEIFAESCLTRDG 366
Cdd:cd05304   318 RLPTQASQLYAKNLLNFLELlVKDDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
3-366 2.13e-163

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 462.16  E-value: 2.13e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDAtFDADIIAKVAPPSDD 82
Cdd:COG3288     1 MKIGVPKETAPGERRVALTPETVKKLVK--LGAEVLVESGAGLAAGFPDAAYEAAGAEIVDAEL-LGADIVLKVRPPSAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  83 EVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTT 162
Cdd:COG3288    78 ELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 163 AAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEAdqdESGYAEQVEKEKQER 242
Cdd:COG3288   158 AAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANG---AGGYAKELSEEEKAK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 243 QPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLPAE 322
Cdd:COG3288   235 QAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSR 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1475498356 323 MPVHASELYAKTVAAMIEEGLEADAFAPDFDDEIFAESCLTRDG 366
Cdd:COG3288   315 LPAHASQLYAKNLLNFLELLVKDGALALDLEDEIVAGTLLTHDG 358
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
3-368 1.40e-132

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


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 389.19  E-value: 1.40e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATFDADIIAKVAPPSDD 82
Cdd:PRK09424    1 MRIGIPRERLPGETRVAATPKTVEQLLKL--GFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  83 EVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTT 162
Cdd:PRK09424   79 EIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQIT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 163 AAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDiEADQDESGYAEQVEKEKQER 242
Cdd:PRK09424  159 AAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFE-EEGGSGDGYAKVMSEEFIKA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 243 QPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIV-AHNVQILGPTNLPA 321
Cdd:PRK09424  238 EMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTDLPS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1475498356 322 EMPVHASELYAKTVAAMIEE-GLEAD-AFAPDFDDEIFAESCLTRDGTV 368
Cdd:PRK09424  318 RLPTQSSQLYGTNLVNLLKLlCPEKDgNIVVDFDDVVIRGVTVVRDGEI 366
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 5-366 1.79e-102

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: 312.37  E-value: 1.79e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   5 IGVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATFDADIIAKVAPPSDDEV 84
Cdd:TIGR00561   2 IGIPRELLENESRVAATPKTVEQILKL--GFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  85 DRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTTAA 164
Cdd:TIGR00561  80 ALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 165 GTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEADQDEsGYAEQVEKEKQERQP 244
Cdd:TIGR00561 160 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGD-GYAKVMSDAFIKAAM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 245 ELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHN-VQILGPTNLPAEM 323
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENgVKVIGYTDFPGRL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1475498356 324 PVHASELYAKTVAAMIEEGL-EADA-FAPDFDDEIFAESCLTRDG 366
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCkEKDGnINIDFDDVVIRGVTVIRAG 363
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 145-368 2.68e-65

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: 206.58  E-value: 2.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 145 AAIGAAERLPAFFPLLTTAAGTV---RPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVES-LGASFVELev 220
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 221 dieadqdesgyaeqvekekQERQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCA-- 298
Cdd:pfam01262  79 -------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEts 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475498356 299 -LTETGEEI-VAHNVQILGPTNLPAEMPVHASELYAKTVAAMIEEGLEADAFAPDFDDEIFAESCLTRDGTV 368
Cdd:pfam01262 140 rPTTHGEPVyVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADKGLKAALLEDEALRAGLNTHDGKI 211
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 150-304 5.49e-49

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: 162.29  E-value: 5.49e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  150 AERLPAFFPLLTTAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVES-LGASFVELevdieadqde 228
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTL---------- 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475498356  229 sgyaeqvekekqERQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGE 304
Cdd:smart01002  71 ------------YSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTT 134
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 3-366 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: 540.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATF-DADIIAKVAPPSD 81
Cdd:cd05304     1 MTIGVPKETAPGERRVALTPETVKKLVK--LGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELaQADIVLKVRPPSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  82 DEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLT 161
Cdd:cd05304    79 EEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 162 TAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEAdQDESGYAEQVEKEKQE 241
Cdd:cd05304   159 TAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDA-EGAGGYAKELSEEFLA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 242 RQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLPA 321
Cdd:cd05304   238 KQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1475498356 322 EMPVHASELYAKTVAAMIEE-GLEADAFAPDFDDEIFAESCLTRDG 366
Cdd:cd05304   318 RLPTQASQLYAKNLLNFLELlVKDDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
3-366 2.13e-163

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 462.16  E-value: 2.13e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDAtFDADIIAKVAPPSDD 82
Cdd:COG3288     1 MKIGVPKETAPGERRVALTPETVKKLVK--LGAEVLVESGAGLAAGFPDAAYEAAGAEIVDAEL-LGADIVLKVRPPSAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  83 EVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTT 162
Cdd:COG3288    78 ELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 163 AAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEAdqdESGYAEQVEKEKQER 242
Cdd:COG3288   158 AAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANG---AGGYAKELSEEEKAK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 243 QPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLPAE 322
Cdd:COG3288   235 QAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSR 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1475498356 323 MPVHASELYAKTVAAMIEEGLEADAFAPDFDDEIFAESCLTRDG 366
Cdd:COG3288   315 LPAHASQLYAKNLLNFLELLVKDGALALDLEDEIVAGTLLTHDG 358
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
3-368 1.40e-132

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


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 389.19  E-value: 1.40e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATFDADIIAKVAPPSDD 82
Cdd:PRK09424    1 MRIGIPRERLPGETRVAATPKTVEQLLKL--GFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  83 EVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTT 162
Cdd:PRK09424   79 EIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQIT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 163 AAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDiEADQDESGYAEQVEKEKQER 242
Cdd:PRK09424  159 AAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFE-EEGGSGDGYAKVMSEEFIKA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 243 QPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIV-AHNVQILGPTNLPA 321
Cdd:PRK09424  238 EMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTDLPS 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1475498356 322 EMPVHASELYAKTVAAMIEE-GLEAD-AFAPDFDDEIFAESCLTRDGTV 368
Cdd:PRK09424  318 RLPTQSSQLYGTNLVNLLKLlCPEKDgNIVVDFDDVVIRGVTVVRDGEI 366
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 5-366 1.79e-102

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: 312.37  E-value: 1.79e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   5 IGVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATFDADIIAKVAPPSDDEV 84
Cdd:TIGR00561   2 IGIPRELLENESRVAATPKTVEQILKL--GFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  85 DRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFPLLTTAA 164
Cdd:TIGR00561  80 ALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 165 GTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDIEADQDEsGYAEQVEKEKQERQP 244
Cdd:TIGR00561 160 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGD-GYAKVMSDAFIKAAM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 245 ELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHN-VQILGPTNLPAEM 323
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENgVKVIGYTDFPGRL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1475498356 324 PVHASELYAKTVAAMIEEGL-EADA-FAPDFDDEIFAESCLTRDG 366
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCkEKDGnINIDFDDVVIRGVTVIRAG 363
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 4-341 4.49e-73

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: 230.37  E-value: 4.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   4 TIGVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVV--GRDATFDADIIAKVAPPSD 81
Cdd:cd01620     1 TLGFPKETKNNEFRVALTPSFVKKLVA--NGFKVYIETGAGSGAGFSDEDYLQAGAQIVpaASKEAYSADIIVKLKEPEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  82 DEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRaqklDALSAMSSIGGYRAAIGAAERLPAFFPLLT 161
Cdd:cd01620    79 AEYDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR----PRLAPNSNIAGYAGVQLGAYELARIQGGRM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 162 TAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVElEVDIEADQDEsgyaeqvekekqe 241
Cdd:cd01620   155 GGAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLR-YSQKEELEKE------------- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 242 rqpellqphLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCAL----TETGEEIVAHNVQILGPT 317
Cdd:cd01620   221 ---------LKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETsiptTEGVPTYEVDGVVIYGVD 291

                         330       340
                  ....*....|....*....|....
gi 1475498356 318 NLPAEMPVHASELYAKTVAAMIEE 341
Cdd:cd01620   292 NMPSLVPREASELLSKNLLPYLVK 315
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 145-368 2.68e-65

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: 206.58  E-value: 2.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 145 AAIGAAERLPAFFPLLTTAAGTV---RPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVES-LGASFVELev 220
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 221 dieadqdesgyaeqvekekQERQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCA-- 298
Cdd:pfam01262  79 -------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEts 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475498356 299 -LTETGEEI-VAHNVQILGPTNLPAEMPVHASELYAKTVAAMIEEGLEADAFAPDFDDEIFAESCLTRDGTV 368
Cdd:pfam01262 140 rPTTHGEPVyVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADKGLKAALLEDEALRAGLNTHDGKI 211
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 3-300 1.65e-54

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: 183.38  E-value: 1.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLlatVDD-LDIRVEEGAGQGAYHTDADYDAAGCSVVG--RDATFDADIIAKVAPP 79
Cdd:cd05305     1 MKIGIPKEIKNQENRVALTPAGVAEL---VAAgHEVLVEKGAGLGSGFSDEEYSEAGAEIVPtaEEVWAKADLIVKVKEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  80 SDDEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVprISRAQKLDALSAMSSIGGYRAAIGAAERLPAFFP- 158
Cdd:cd05305    78 LPEEYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETI--EDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 159 ---LLTTAAGtVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVDieadqdesgyaeqv 235
Cdd:cd05305   156 rgvLLGGVPG-VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTTLYS-------------- 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475498356 236 ekekqerQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGnCALT 300
Cdd:cd05305   221 -------NPANLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGG-CFET 277
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 150-304 5.49e-49

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: 162.29  E-value: 5.49e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  150 AERLPAFFPLLTTAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVES-LGASFVELevdieadqde 228
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTL---------- 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475498356  229 sgyaeqvekekqERQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGE 304
Cdd:smart01002  71 ------------YSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTT 134
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 3-295 3.45e-48

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: 167.50  E-value: 3.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   3 LTIGVPRETEPGETRVALVPDVADRLLA---TVddldiRVEEGAGQGAYHTDADYDAAGCSVVGR--DATFDADIIAKVA 77
Cdd:COG0686     1 MIIGVPKEIKNNENRVALTPAGVRELVAaghEV-----LVETGAGLGSGFSDEDYSAAGAEIVDTaeEVFAQADLIVKVK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  78 PPSDDEVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVprISRAQKLDALSAMSSIGGYRAAIGAAErlpaff 157
Cdd:COG0686    76 EPQPEEYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETV--EDPDGSLPLLAPMSEIAGRMAIQIGAE------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 158 pLLTTAAGT----------VRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEVdieadqd 227
Cdd:COG0686   148 -YLEKPNGGrgvllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTTLY------- 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475498356 228 eSgyaeqvekekqerQPELLQPHLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGG 295
Cdd:COG0686   220 -S-------------NPANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGG 273
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 6-138 8.50e-48

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: 158.73  E-value: 8.50e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356    6 GVPRETEPGETRVALVPDVADRLLAtvDDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDATF-DADIIAKVAPPSDDEV 84
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVK--LGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWaDADIILKVKEPSPEEL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1475498356   85 DRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRISRAQKLDALSAMS 138
Cdd:smart01003  79 ALLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMA 132
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 6-140 1.16e-44

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: 150.65  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   6 GVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVVGRDAT--FDADIIAKVAPPSDDE 83
Cdd:pfam05222   1 GVPKEIKPGERRVALTPAGVKKLVKL--GHEVLVESGAGLGAGFSDEAYEAAGAEIVDTAAEvwAEADLILKVKEPQPEE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475498356  84 VDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVPRiSRAQKLDALSAMSSI 140
Cdd:pfam05222  79 YALLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANI 134
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 5-341 1.82e-42

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: 150.84  E-value: 1.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   5 IGVPRETEPGETRVALVPDVADRLLATvdDLDIRVEEGAGQGAYHTDADYDAAGCSVV-GRDATFDADIIAKVA-PPSDD 82
Cdd:cd12154     1 IAGPKEIKNEEFRVGLSPSVVATLVEA--GHEVRVETGAGIGAGFADQAYVQAGAIVVtLAKALWSLDVVLKVKePLTNA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  83 EVDRLGE--GQVLVGFLSPLERPETAQALADRGVTALAMELVPRISraqkldaLSAMSSIGGYRAAIGAAERLPAFFPLL 160
Cdd:cd12154    79 EYALIQKlgDRLLFTYTIGADHRDLTEALARAGLTAIAVEGVELPL-------LTSNSIGAGELSVQFIARFLEVQQPGR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 161 TTAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVElevdieadqdesgyaeQVEKEkq 240
Cdd:cd12154   152 LGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVE----------------ELEEA-- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 241 erqpellqphLAEADVVISTALIPGQPAPLLINEEAVAAMDPGSVIVDLAAPNGGNCALTETGEEIVAHNVQILGPTNLP 320
Cdd:cd12154   214 ----------LAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDVNMP 283

                         330       340
                  ....*....|....*....|....*.
gi 1475498356 321 -----AEMPVHASELYAKTVAAMIEE 341
Cdd:cd12154   284 gpgcaMGVPWDATLRLAANTLPALVK 309
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 4-295 4.75e-11

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: 63.02  E-value: 4.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356   4 TIGVPRETEPGETRVALVPdvadrllATVDDLDIR----VEEGAGQGAYHTDADYDAAGCSVVGRDATF-DADIIAKVAP 78
Cdd:cd12181     2 TGGFGISNKENEKRVPLLP-------ADLERIPLReqlyFEEGYGERLGISDEEYAALGAGIVSREEILaKCDVICDPKP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356  79 PSDDeVDRLGEGQVLVGFLSPLERPETAQALADRGVTALAMELVpRISRAQKLDALSAMSSIGGYrAAIGAAERLPAFFP 158
Cdd:cd12181    75 GDAD-YLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAWEDM-FEWSKIGRHVFYKNNELAGY-AAVLHALQLYGITP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 159 LLTTaagtvrpaRVLVLGAGvaglqaiATAKrlGA----KVFGYDIREPTReeveslgasfvelevdieadqdesgyaeq 234
Cdd:cd12181   152 YRQT--------KVAVLGFG-------NTAR--GAiralKLGGADVTVYTR----------------------------- 185

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475498356 235 vekekqeRQPELLQPHLAEADVVISTALI-PGQPAPlLINEEAVAAMDPGSVIVDLAAPNGG 295
Cdd:cd12181   186 -------RTEALFKEELSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGM 239
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 171-287 1.02e-06

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: 48.65  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 171 RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELEvdieadqdesgyaeqvekekqerqpELlqph 250
Cdd:pfam02826  38 TVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLD-------------------------EL---- 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1475498356 251 LAEADVVISTalipgqpAPL------LINEEAVAAMDPGSVIV 287
Cdd:pfam02826  89 LAESDVVSLH-------LPLtpetrhLINAERLALMKPGAILI 124
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 167-322 1.07e-06

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 50.11  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 167 VRPA-RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVeleVDIEAdqdesgyAEQVEKEKQERQpe 245
Cdd:COG1064   160 VGPGdRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHV---VNSSD-------EDPVEAVRELTG-- 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475498356 246 llqphlaeADVVISTAlipgqPAPLLINeEAVAAMDPGSVIVDLAAPNGgncALTETGEEIVAHNVQILGPTNLPAE 322
Cdd:COG1064   228 --------ADVVIDTV-----GAPATVN-AALALLRRGGRLVLVGLPGG---PIPLPPFDLILKERSIRGSLIGTRA 287
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 160-315 4.15e-06

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: 47.70  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 160 LTTAAGTVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVeleVDIEADQDESgyaeqvekek 239
Cdd:cd05188   126 LRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHV---IDYKEEDLEE---------- 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475498356 240 qerqpELLQPHLAEADVVISTAlipGQPAPLlinEEAVAAMDPGSVIVDLAAPNGGNcaLTETGEEIVAHNVQILG 315
Cdd:cd05188   193 -----ELRLTGGGGADVVIDAV---GGPETL---AQALRLLRPGGRIVVVGGTSGGP--PLDDLRRLLFKELTIIG 255
SDH_like cd05199
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ...
 4-73 4.27e-06

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: 48.00  E-value: 4.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475498356   4 TIGVPRETE-PGETRVALVPDVADRLLATVDDLDIRVEEGAGQgaYHTDADYDAAGCSVVgRDATfDADII 73
Cdd:cd05199     1 KIGIIREGKtPPDRRVPLTPEQCKELQAKYPGVEIFVQPSPVR--CFKDEEYRAAGIEVV-EDLS-DCDIL 67
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 164-216 1.79e-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: 1.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1475498356 164 AGTVRPA-RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFV 216
Cdd:cd08254   160 AGEVKPGeTVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEV 213
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 171-342 2.20e-05

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: 46.03  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 171 RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVelevdIEAdqdesgyaeqvekeKQERQPELLQPH 250
Cdd:cd08261   162 TVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDT-----INV--------------GDEDVAARLREL 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 251 LAE--ADVVISTAlipGQPAPLlinEEAVAAMDPGSVIVDLAapnggncaltetgeeIVAHNVQILGPTNLPAEMPVHAS 328
Cdd:cd08261   223 TDGegADVVIDAT---GNPASM---EEAVELVAHGGRVVLVG---------------LSKGPVTFPDPEFHKKELTILGS 281

                         170
                  ....*....|....*...
gi 1475498356 329 ELYAK----TVAAMIEEG 342
Cdd:cd08261   282 RNATRedfpDVIDLLESG 299
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 164-287 6.65e-05

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: 44.36  E-value: 6.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 164 AGTVRPARVLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGASFVelevdIEADQDEsgYAEQVEKEKQER 242
Cdd:COG1063   157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLELARELGADAV-----VNPREED--LVEAVRELTGGR 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1475498356 243 qpellqphlaEADVVISTAlipGQPAPLlinEEAVAAMDPGSVIV 287
Cdd:COG1063   230 ----------GADVVIEAV---GAPAAL---EQALDLVRPGGTVV 258
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 166-356 8.32e-05

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. 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-Rossman 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: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 44.13  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 166 TVRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREE---VESLGASFVELEVDIEADQDESGyaeqvekekqer 242
Cdd:cd08230   170 TWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNRRDPPDPKadiVEELGATYVNSSKTPVAEVKLVG------------ 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 243 qpellqphlaEADVVISTAlipGQPApllINEEAVAAMDPGSVIVDLAAPNGGNCALTETGE---EIVAHNVQILGPTN- 318
Cdd:cd08230   238 ----------EFDLIIEAT---GVPP---LAFEALPALAPNGVVILFGVPGGGREFEVDGGElnrDLVLGNKALVGSVNa 301

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1475498356 319 ------LPAEMPVHASELYAKTVAAMI------EEglEADAFAPDFDDEI 356
Cdd:cd08230   302 nkrhfeQAVEDLAQWKYRWPGVLERLItrrvplEE--FAEALTEKPDGEI 349
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 167-290 2.04e-04

(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: 43.05  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 167 VRPARVLVLGAGVAGLQAIATAKRLGAKVFGYDIReptreeveslgasfvelevdieadqdESGYAEQVekEKQERQPEL 246
Cdd:cd12184   143 IRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIY--------------------------PSDAAKDV--VTFVSLDEL 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1475498356 247 lqphLAEADVV-ISTALIPGQPAPlLINEEAVAAMDPGSVIVDLA 290
Cdd:cd12184   195 ----LKKSDIIsLHVPYIKGKNDK-LINKEFISKMKDGAILINTA 234
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 171-218 2.49e-04

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 43.04  E-value: 2.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1475498356 171 RVLVLGAGVAGLQAIATAKRLGAKVFGYDI--REPTREEVESLGASFVEL 218
Cdd:PRK14106    7 KVLVVGAGVSGLALAKFLKKLGAKVILTDEkeEDQLKEALEELGELGIEL 56
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 171-219 3.58e-04

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: 42.38  E-value: 3.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1475498356 171 RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVELE 219
Cdd:COG0771     6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVV 54
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 174-290 4.33e-04

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: 41.88  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 174 VLGAGVAGLQAIATAKRLGAKVFGYDIRePTREEVESLGASFVELEvdieadqdesgyaeqvekekqerqpELLQphlaE 253
Cdd:cd12187   144 VVGTGRIGRRVARIARGFGMKVLAYDVV-PDEELAERLGFRYVSLE-------------------------ELLQ----E 193

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1475498356 254 ADVVisTALIPGQPAPL-LINEEAVAAMDPGSVIVDLA 290
Cdd:cd12187   194 SDII--SLHVPYTPQTHhLINRENFALMKPGAVLINTA 229
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 160-216 5.42e-04

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 41.73  E-value: 5.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1475498356 160 LTTAAGTVRP-ARVLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGASFV 216
Cdd:cd08265   194 LFIRGGGFRPgAYVVVYGAGPIGLAAIALAKAAGAsKVIAFEISEERRNLAKEMGADYV 252
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 172-290 6.90e-04

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: 41.08  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 172 VLVLGAGVAGLQAIATAKRLGAKVFGYDiREPTREEVESLGASFVELEvdieadqdesgyaeqvekekqerqpELlqphL 251
Cdd:cd05198   143 VGIVGLGRIGQRVAKRLQAFGMKVLYYD-RTRKPEPEEDLGFRVVSLD-------------------------EL----L 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1475498356 252 AEADvVISTALipgqpaPL------LINEEAVAAMDPGSVIVDLA 290
Cdd:cd05198   193 AQSD-VVVLHL------PLtpetrhLINEEELALMKPGAVLVNTA 230
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 160-221 7.20e-04

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. 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.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 41.09  E-value: 7.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1475498356 160 LTTAAGTVRPAR------VLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGASFVELEVD 221
Cdd:cd08284   153 LPTGYFGAKRAQvrpgdtVAVIGCGPVGLCAVLSAQVLGAaRVFAVDPVPERLERAAALGAEPINFEDA 221
SDH cd12188
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ...
 10-73 1.25e-03

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: 40.68  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475498356  10 ETEPGETRVALVPDVADRLLATVddLDIRVEEgAGQGAYhTDADYDAAGCSVVG----RDATFDADII 73
Cdd:cd12188     8 ETKPLERRTALTPTTAKKLLDAG--FKVTVER-SPQRIF-PDEEYEAVGCELVPagswVNAPKDAIIL 71
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 165-214 1.42e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. 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 has 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: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 40.28  E-value: 1.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1475498356 165 GTVRPA-RVLVLGAGVAGLQAIATAKRLGAKVFGYDIREPTREEVESLGAS 214
Cdd:cd08260   161 ARVKPGeWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAV 211
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 178-287 2.09e-03

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: 39.69  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 178 GVAGLQAI--ATAKRL---GAKVFGYDIREptREEVESLGASFVELEvdieadqdesgyaeqvekekqerqpELLqphlA 252
Cdd:COG1052   147 GIIGLGRIgqAVARRAkgfGMKVLYYDRSP--KPEVAELGAEYVSLD-------------------------ELL----A 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1475498356 253 EADVVISTAlipgqpaPL------LINEEAVAAMDPGSVIV 287
Cdd:COG1052   196 ESDIVSLHC-------PLtpetrhLINAEELALMKPGAILI 229
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 178-290 2.18e-03

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: 39.48  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 178 GVAGLQAI--ATAKRL---GAKVFGYDIREPTREEVESLGASFVELevdieadqdesgyaeqvekekqerqPELlqphLA 252
Cdd:cd12175   146 GIVGLGNIgrAVARRLrgfGVEVIYYDRFRDPEAEEKDLGVRYVEL-------------------------DEL----LA 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1475498356 253 EADVViSTALipgqpaPL------LINEEAVAAMDPGSVIVDLA 290
Cdd:cd12175   197 ESDVV-SLHV------PLtpetrhLIGAEELAAMKPGAILINTA 233
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 161-216 2.97e-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: 39.14  E-value: 2.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475498356 161 TTAAGTVRPARVLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGASFV 216
Cdd:cd05281   156 TVLAGDVSGKSVLITGCGPIGLMAIAVAKAAGAsLVIASDPNPYRLELAKKMGADVV 212
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 172-290 3.69e-03

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: 39.06  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 172 VLVLGAGVAGLQAIATAKRLGAKVFGYDIREptREEVESLGASFVELEvdieadqdesgyaeqvekekqerqpELlqphL 251
Cdd:cd12186   148 VGIIGTGRIGSAAAKIFKGFGAKVIAYDPYP--NPELEKFLLYYDSLE-------------------------DL----L 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1475498356 252 AEADVVisTALIPGQPAPL-LINEEAVAAMDPGSVIVDLA 290
Cdd:cd12186   197 KQADII--SLHVPLTKENHhLINAEAFAKMKDGAILVNAA 234
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 163-318 5.80e-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: 38.39  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 163 AAGTVRPAR-VLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGASFVeleVDIEADQDEsgyaeqvekEKQ 240
Cdd:cd08231   171 RAGPVGAGDtVVVQGAGPLGLYAVAAAKLAGArRVIVIDGSPERLELAREFGADAT---IDIDELPDP---------QRR 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 241 ERQPELLQPHlaEADVVISTAlipGQPAPLlinEEAVAAMDPGS--VIVDLAAPNGgncALTETGEEIVAHNVQILGPTN 318
Cdd:cd08231   239 AIVRDITGGR--GADVVIEAS---GHPAAV---PEGLELLRRGGtyVLVGSVAPAG---TVPLDPERIVRKNLTIIGVHN 307
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 171-290 6.34e-03

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: 38.25  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 171 RVLVLGAGVAGLQAIATAKRLGAKVFGYDiREPTREEVESLGASFV-ELEvdieadqdesgyaeqvekekqerqpELlqp 249
Cdd:COG0111   142 TVGIVGLGRIGRAVARRLRAFGMRVLAYD-PSPKPEEAADLGVGLVdSLD-------------------------EL--- 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1475498356 250 hLAEADVVISTalipgqpAPL------LINEEAVAAMDPGSVIVDLA 290
Cdd:COG0111   193 -LAEADVVSLH-------LPLtpetrgLIGAEELAAMKPGAILINTA 231
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
181-315 8.56e-03

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 36.05  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 181 GLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVeleVDIEADQDESGYAEQVEKEKqerqpellqphlaeADVVIST 260
Cdd:pfam00107   3 GLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHV---INPKETDLVEEIKELTGGKG--------------VDVVFDC 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1475498356 261 AlipGQPAPLlinEEAVAAMDPGSVIVDLAAPNGGncaLTETGEEIVAHNVQILG 315
Cdd:pfam00107  66 V---GSPATL---EQALKLLRPGGRVVVVGLPGGP---LPLPLAPLLLKELTILG 111
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 155-301 9.04e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. 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.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 37.64  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 155 AFFPLLTTAAGTVRPA------RVLVLGAGVAGLQAIATAKRLGAK-VFGYDIREPTREEVESLGAsfveLEVDIEADQD 227
Cdd:cd08255    78 ALTALAATALNGVRDAeprlgeRVAVVGLGLVGLLAAQLAKAAGAReVVGVDPDAARRELAEALGP----ADPVAADTAD 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475498356 228 ESGYaeqvekekqerqpellqphlAEADVVISTAlipGQPAPLlinEEAVAAMDPGSVIVDLAAPNGGNCALTE 301
Cdd:cd08255   154 EIGG--------------------RGADVVIEAS---GSPSAL---ETALRLLRDRGRVVLVGWYGLKPLLLGE 201
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 171-342 9.17e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.82  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 171 RVLVLGA--GVaGLQAIATAKRLGAKVFGYDIREPTREEVESLGASFVelevdieADQDESGYAEQVEKEKQERQpellq 248
Cdd:COG0604   142 TVLVHGAagGV-GSAAVQLAKALGARVIATASSPEKAELLRALGADHV-------IDYREEDFAERVRALTGGRG----- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 249 phlaeADVVISTalIPGQPApllinEEAVAAMDPGSVIVDLAAPNGGNCALTETgeEIVAHNVQILGPTNLPAEMPVHAS 328
Cdd:COG0604   209 -----VDVVLDT--VGGDTL-----ARSLRALAPGGRLVSIGAASGAPPPLDLA--PLLLKGLTLTGFTLFARDPAERRA 274

                         170
                  ....*....|....
gi 1475498356 329 ELyaKTVAAMIEEG 342
Cdd:COG0604   275 AL--AELARLLAAG 286
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 164-286 9.52e-03

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. 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.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 37.64  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475498356 164 AGTVRPARVLVLGAGVAGLQAIATAKRLGA-KVFGYDIREPTREEVESLGAsfvelevDIEADQDESGYAEQVEKEKQER 242
Cdd:cd05278   163 AGIKPGSTVAVIGAGPVGLCAVAGARLLGAaRIIAVDSNPERLDLAKEAGA-------TDIINPKNGDIVEQILELTGGR 235

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1475498356 243 qpellqphlaEADVVISTAlipGQPAPLlinEEAVAAMDPGSVI 286
Cdd:cd05278   236 ----------GVDCVIEAV---GFEETF---EQAVKVVRPGGTI 263
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH