|
Name |
Accession |
Description |
Interval |
E-value |
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
5-531 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 825.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAAnLWStSDIVFKVRAPSAEEV 84
Cdd:PRK09424 3 IGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAA-VWQ-SDIILKVNAPSDDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtLSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:PRK09424 81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPR-ISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAAQR 244
Cdd:PRK09424 160 AGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVK-HGVTIVGYTDLPSRL 323
Cdd:PRK09424 240 ALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTdNGVTIIGYTDLPSRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 324 PKQASTLYSTNLLRLTEELCKDAegkkttDGIINVNMEDEAIRGLTVIKEGNITWPPPPPKPVAAPAAKPAPAAAPAhgh 403
Cdd:PRK09424 320 PTQSSQLYGTNLVNLLKLLCPEK------DGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKE--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 404 gPSTTVSSPKRVVTMFVFATLLFALIGMGAPTAFLGHLTVFVLGCFIGYMVVWNVTPALHTPLMSVTNSISSIIVIGALV 483
Cdd:PRK09424 391 -EEKKPASPWRKYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1860583002 484 QVappladgmARPELLIKCLAAAGIALTAINMFGGFAVTRRMLDMFRK 531
Cdd:PRK09424 470 QI--------GSGSGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
5-532 |
0e+00 |
|
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: 606.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAAnLWStSDIVFKVRAPSAEEV 84
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAE-IWQ-SDIIFKVNAPLDDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtLSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:TIGR00561 80 ALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPR-ISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAAQR 244
Cdd:TIGR00561 159 AGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVV-VKHGVTIVGYTDLPSRL 323
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFtTENGVKVIGYTDFPGRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 324 PKQASTLYSTNLLRLTEELCKDaegkktTDGIINVNMEDEAIRGLTVIKEGNITWPPPPPKPVAAPAAKPAPAAAPAHGH 403
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCKE------KDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAAQKAAPEAEKEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 404 GPSTtvsSPKRVVTMFVFATLLFALIGMGAPTAFLGHLTVFVLGCFIGYMVVWNVTPALHTPLMSVTNSISSIIVIGALV 483
Cdd:TIGR00561 393 KCPC---DPRRKYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1860583002 484 QVAPPLADgmarpeLLIKCLAAAGIALTAINMFGGFAVTRRMLDMFRKN 532
Cdd:TIGR00561 470 QIGQGGGN------LFIDALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
3-374 |
0e+00 |
|
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.
Pssm-ID: 240629 [Multi-domain] Cd Length: 363 Bit Score: 575.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 3 LVIGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWStSDIVFKVRAPSAE 82
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAQ-ADIVLKVRPPSEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 83 EVGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQI 162
Cdd:cd05304 80 EVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRI-SRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 163 TAAGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAA 242
Cdd:cd05304 159 TAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 243 QREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVKHGVTIVGYTDLPSR 322
Cdd:cd05304 239 QRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1860583002 323 LPKQASTLYSTNLLRLTEELCKDaegkkttDGIINVNMEDEAIRGLTVIKEG 374
Cdd:cd05304 319 LPTQASQLYAKNLLNFLELLVKD-------DGELTLDLEDEIVRGTLVTHDG 363
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
5-374 |
1.46e-156 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 450.61 E-value: 1.46e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVqgAANLWStSDIVFKVRAPSAEEV 84
Cdd:COG3288 3 IGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIV--DAELLG-ADIVLKVRPPSAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:COG3288 80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRI-SRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGggYAKVMSEGFQAAQR 244
Cdd:COG3288 159 AGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANGAGG--YAKELSEEEKAKQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVKHGVTIVGYTDLPSRLP 324
Cdd:COG3288 237 ELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSRLP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1860583002 325 KQASTLYSTNLLRLTEELCKdaegkkttDGIINVNMEDEAIRGLTVIKEG 374
Cdd:COG3288 317 AHASQLYAKNLLNFLELLVK--------DGALALDLEDEIVAGTLLTHDG 358
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
146-378 |
7.95e-70 |
|
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: 222.76 E-value: 7.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 146 AVIEAANAFGRFFNGQITAAGKV---APAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVS-LGGEFVKVDY 221
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVETLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 222 deegsggggyakvmsegfqaAQREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCE--- 298
Cdd:pfam01262 81 --------------------SQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 299 LTEPGK-VVVKHGVTIVGYTDLPSRLPKQASTLYSTNLLRLTEELckdAEGkkttdGIINVNMEDEAIRGLTVIKEGNIT 377
Cdd:pfam01262 141 PTTHGEpVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADK-----GLKAALLEDEALRAGLNTHDGKIT 212
|
.
gi 1860583002 378 W 378
Cdd:pfam01262 213 H 213
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
6-140 |
1.05e-61 |
|
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: 198.79 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 6 GVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVqGAANLWSTSDIVFKVRAPSAEEVG 85
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIV-DTAEVWADADIILKVKEPSPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1860583002 86 LIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAG 140
Cdd:smart01003 80 LLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRI-SRAQSLDALSSMAE 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
5-531 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 825.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAAnLWStSDIVFKVRAPSAEEV 84
Cdd:PRK09424 3 IGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAA-VWQ-SDIILKVNAPSDDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtLSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:PRK09424 81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPR-ISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAAQR 244
Cdd:PRK09424 160 AGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVK-HGVTIVGYTDLPSRL 323
Cdd:PRK09424 240 ALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTdNGVTIIGYTDLPSRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 324 PKQASTLYSTNLLRLTEELCKDAegkkttDGIINVNMEDEAIRGLTVIKEGNITWPPPPPKPVAAPAAKPAPAAAPAhgh 403
Cdd:PRK09424 320 PTQSSQLYGTNLVNLLKLLCPEK------DGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKE--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 404 gPSTTVSSPKRVVTMFVFATLLFALIGMGAPTAFLGHLTVFVLGCFIGYMVVWNVTPALHTPLMSVTNSISSIIVIGALV 483
Cdd:PRK09424 391 -EEKKPASPWRKYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1860583002 484 QVappladgmARPELLIKCLAAAGIALTAINMFGGFAVTRRMLDMFRK 531
Cdd:PRK09424 470 QI--------GSGSGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
5-532 |
0e+00 |
|
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: 606.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAAnLWStSDIVFKVRAPSAEEV 84
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAE-IWQ-SDIIFKVNAPLDDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtLSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:TIGR00561 80 ALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPR-ISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAAQR 244
Cdd:TIGR00561 159 AGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVV-VKHGVTIVGYTDLPSRL 323
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFtTENGVKVIGYTDFPGRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 324 PKQASTLYSTNLLRLTEELCKDaegkktTDGIINVNMEDEAIRGLTVIKEGNITWPPPPPKPVAAPAAKPAPAAAPAHGH 403
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCKE------KDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAAQKAAPEAEKEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 404 GPSTtvsSPKRVVTMFVFATLLFALIGMGAPTAFLGHLTVFVLGCFIGYMVVWNVTPALHTPLMSVTNSISSIIVIGALV 483
Cdd:TIGR00561 393 KCPC---DPRRKYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1860583002 484 QVAPPLADgmarpeLLIKCLAAAGIALTAINMFGGFAVTRRMLDMFRKN 532
Cdd:TIGR00561 470 QIGQGGGN------LFIDALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
3-374 |
0e+00 |
|
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.
Pssm-ID: 240629 [Multi-domain] Cd Length: 363 Bit Score: 575.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 3 LVIGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWStSDIVFKVRAPSAE 82
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAQ-ADIVLKVRPPSEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 83 EVGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQI 162
Cdd:cd05304 80 EVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRI-SRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 163 TAAGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGGGYAKVMSEGFQAA 242
Cdd:cd05304 159 TAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 243 QREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVKHGVTIVGYTDLPSR 322
Cdd:cd05304 239 QRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1860583002 323 LPKQASTLYSTNLLRLTEELCKDaegkkttDGIINVNMEDEAIRGLTVIKEG 374
Cdd:cd05304 319 LPTQASQLYAKNLLNFLELLVKD-------DGELTLDLEDEIVRGTLVTHDG 363
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
5-374 |
1.46e-156 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 450.61 E-value: 1.46e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVqgAANLWStSDIVFKVRAPSAEEV 84
Cdd:COG3288 3 IGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIV--DAELLG-ADIVLKVRPPSAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:COG3288 80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRI-SRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYDEEGSGGggYAKVMSEGFQAAQR 244
Cdd:COG3288 159 AGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANGAGG--YAKELSEEEKAKQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVKHGVTIVGYTDLPSRLP 324
Cdd:COG3288 237 ELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSRLP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1860583002 325 KQASTLYSTNLLRLTEELCKdaegkkttDGIINVNMEDEAIRGLTVIKEG 374
Cdd:COG3288 317 AHASQLYAKNLLNFLELLVK--------DGALALDLEDEIVAGTLLTHDG 358
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
5-342 |
5.09e-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: 235.00 E-value: 5.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWSTSDIVFKVRAPSAEEV 84
Cdd:cd01620 2 LGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAASKEAYSADIIVKLKEPEFAEY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtlsraQKMDALTSTAGVSGYRAVIEAANAFGRFFNGQITA 164
Cdd:cd01620 82 DLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLEN-----DFRPRLAPNSNIAGYAGVQLGAYELARIQGGRMGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 165 AGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFvkvdydeegsggggyakvmsegFQAAQR 244
Cdd:cd01620 157 AGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSR----------------------LRYSQK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 245 EMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCEL----TEPGKVVVKHGVTIVGYTDLP 320
Cdd:cd01620 215 EELEKELKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETsiptTEGVPTYEVDGVVIYGVDNMP 294
|
330 340
....*....|....*....|..
gi 1860583002 321 SRLPKQASTLYSTNLLRLTEEL 342
Cdd:cd01620 295 SLVPREASELLSKNLLPYLVKL 316
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
146-378 |
7.95e-70 |
|
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: 222.76 E-value: 7.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 146 AVIEAANAFGRFFNGQITAAGKV---APAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVS-LGGEFVKVDY 221
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVpgvAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVETLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 222 deegsggggyakvmsegfqaAQREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCE--- 298
Cdd:pfam01262 81 --------------------SQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 299 LTEPGK-VVVKHGVTIVGYTDLPSRLPKQASTLYSTNLLRLTEELckdAEGkkttdGIINVNMEDEAIRGLTVIKEGNIT 377
Cdd:pfam01262 141 PTTHGEpVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADK-----GLKAALLEDEALRAGLNTHDGKIT 212
|
.
gi 1860583002 378 W 378
Cdd:pfam01262 213 H 213
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
6-141 |
7.65e-62 |
|
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: 199.19 E-value: 7.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 6 GVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWSTSDIVFKVRAPSAEEVG 85
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVDTAAEVWAEADLILKVKEPQPEEYA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860583002 86 LIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRtlSRAQKMDALTSTAGV 141
Cdd:pfam05222 81 LLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR--SRGQSLDALSSMANI 134
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
6-140 |
1.05e-61 |
|
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: 198.79 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 6 GVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVqGAANLWSTSDIVFKVRAPSAEEVG 85
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIV-DTAEVWADADIILKVKEPSPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1860583002 86 LIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLPRTlSRAQKMDALTSTAG 140
Cdd:smart01003 80 LLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRI-SRAQSLDALSSMAE 133
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
3-377 |
2.26e-60 |
|
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: 203.02 E-value: 2.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 3 LVIGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWSTSDIVFKVRAPSAE 82
Cdd:cd05305 1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVPTAEEVWAKADLIVKVKEPLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 83 EVGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMD-------SLPrtlsraqkmdALTSTAGVSGYRAVIEAANAFG 155
Cdd:cd05305 81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYEtiededgSLP----------LLAPMSEIAGRLAVQIGAEYLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 156 RFFNGQ------ITAagkVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVKVDYdeegsggg 229
Cdd:cd05305 151 KPNGGRgvllggVPG---VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTTLY-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 230 gyakvmsegfqaAQREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGK----V 305
Cdd:cd05305 220 ------------SNPANLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRPTThdnpT 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860583002 306 VVKHGVTIVGYTDLPSRLPKQASTLYSTNLLRLTEELCKdaegkkttDGIINVNMEDEAIR-GLTVIKeGNIT 377
Cdd:cd05305 288 YVVHGVIHYCVPNMPGAVPRTSTLALTNATLPYLLKLAN--------KGLEEALLEDPGLAkGLNTYK-GKLT 351
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
3-377 |
6.11e-53 |
|
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: 183.67 E-value: 6.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 3 LVIGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWSTSDIVFKVRAPSAE 82
Cdd:COG0686 1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEEVFAQADLIVKVKEPQPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 83 EVGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMD-------SLPrtlsraqkmdALTSTAGVSGYRAVIEAANAFG 155
Cdd:COG0686 81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYEtvedpdgSLP----------LLAPMSEIAGRMAIQIGAEYLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 156 RFFNGQitaaGK-------VAPAKVFIAGAGVAGLAAIGTAASLGAIVRA---NDTRAEVADQVvsLGGEfVKVdydeeg 225
Cdd:COG0686 151 KPNGGR----GVllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVldiNLDRLRRLDDI--FGGR-VTT------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 226 sggggyakVMSegfqaaQREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEP--- 302
Cdd:COG0686 218 --------LYS------NPANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRPtth 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860583002 303 -GKVVVKHGVTIVGYTDLPSRLPKQASTLYSTNLLRLTEELckdAEgkkttDGIINVNMEDEAIR-GLTVIKeGNIT 377
Cdd:COG0686 284 dDPTYVVHGVVHYCVANMPGAVPRTSTYALTNATLPYLLAL---AD-----KGWEQALREDPGLAkGLNTYK-GKLT 351
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
151-315 |
1.41e-42 |
|
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: 148.81 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 151 ANAFGRFFNGQITAAGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVS-LGGEFVKVdydeegsggg 229
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 230 gyakvmsegfqAAQREMYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGK----V 305
Cdd:smart01002 71 -----------YSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTThddpT 139
|
170
....*....|
gi 1860583002 306 VVKHGVTIVG 315
Cdd:smart01002 140 YVVDGVVHYC 149
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
5-342 |
1.49e-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: 154.31 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 5 IGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWSTSDIVFKVRAPSAEEV 84
Cdd:cd12154 1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLAKALWSLDVVLKVKEPLTNAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 85 GLIRE------GSTLIGfiwpAQNPELMQQLAAKRVTVLAMDSLPRTLsraqkmdaLTSTAGVSGYRAVIEAANAFGRFF 158
Cdd:cd12154 81 ALIQKlgdrllFTYTIG----ADHRDLTEALARAGLTAIAVEGVELPL--------LTSNSIGAGELSVQFIARFLEVQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 159 NGQITAAGKVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAEVADQVVSLGGEFVkVDYDEEgsggggyakvmseg 238
Cdd:cd12154 149 PGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNV-EELEEA-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 239 fqaaqremyaqqAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGKVVVKHGVTIVGYTD 318
Cdd:cd12154 214 ------------LAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDVN 281
|
330 340
....*....|....*....|....*....
gi 1860583002 319 LPSR-----LPKQASTLYSTNLLRLTEEL 342
Cdd:cd12154 282 MPGPgcamgVPWDATLRLAANTLPALVKL 310
|
|
| PNTB_4TM |
pfam12769 |
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of ... |
441-531 |
1.98e-38 |
|
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of family PNTB, pfam02233, that carries four of this transporters transmembrane regions. PNTB is the beta-subunit of pyridine nucleotide transhydrogenase. This family forms part of the Proton-translocating Transhydrogenase (PTH) Family.
Pssm-ID: 463694 [Multi-domain] Cd Length: 84 Bit Score: 135.27 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 441 LTVFVLGCFIGYMVVWNVTPALHTPLMSVTNSISSIIVIGALVQVAPPLAdgmarpeLLIKCLAAAGIALTAINMFGGFA 520
Cdd:pfam12769 1 LTVFVLALFVGYEVIWKVPPALHTPLMSVTNAISGIIIVGALLAAGGGDT-------TLATVLGFIAVVLATINVVGGFL 73
|
90
....*....|.
gi 1860583002 521 VTRRMLDMFRK 531
Cdd:pfam12769 74 VTDRMLDMFKK 84
|
|
| alaDH |
TIGR00518 |
alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes ... |
3-342 |
5.01e-35 |
|
alanine dehydrogenase; The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP. [Energy metabolism, Amino acids and amines]
Pssm-ID: 129609 [Multi-domain] Cd Length: 370 Bit Score: 135.04 E-value: 5.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 3 LVIGVPRESFPGEKRVATVPEVVEKLIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQGAANLWStSDIVFKVRAPSAE 82
Cdd:TIGR00518 1 MRIGVPKEIKNNEFRVALTPAGVAELTSRGHEVLVEAGAGEGSGFTDAAYKAAGAELVATAKQVWD-AELVLKVKEPLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 83 EVGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLAMDSLprTLSRAQkMDALTSTAGVSGYRAVIEAANAFGRFFNGQ- 161
Cdd:TIGR00518 80 EYGYLRHGQILFTYLHLAAERALTDALLDSGTTAIAYETV--QTADGA-LPLLAPMSEVAGRLAAQVGAYHLEKTQGGRg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 162 ITAAG--KVAPAKVFIAGAGVAGLAAIGTAASLGAIVRANDTRAevaDQVVSLGGEFvkvdydeegsgGGGYAKVMSEGF 239
Cdd:TIGR00518 157 VLLGGvpGVEPGDVTIIGGGVVGTNAAKMANGLGATVTILDINI---DRLRQLDAEF-----------GGRIHTRYSNAY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 240 QaaqremYAQQAKECDIIITTALIPGKPAPKLITAEMVQSMKPGSVIVDMAAEQGGNCELTEPGK----VVVKHGVTIVG 315
Cdd:TIGR00518 223 E------IEDAVKRADLLIGAVLIPGAKAPKLVSNSLVAQMKPGAVIVDVAIDQGGCVETSRPTThdqpTYAVHDVVHYC 296
|
330 340
....*....|....*....|....*..
gi 1860583002 316 YTDLPSRLPKQASTLYSTNLLRLTEEL 342
Cdd:TIGR00518 297 VANMPGAVPKTSTYALTNATMPYVLEL 323
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
4-302 |
2.04e-15 |
|
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: 76.89 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 4 VIGVPRESFPGEKRVATVPEVVEKlIKLGFSVSVESGAGDEANFSDDTYRAAGAQIVQgAANLWSTSDIVFKVRaPSAEE 83
Cdd:cd12181 2 TGGFGISNKENEKRVPLLPADLER-IPLREQLYFEEGYGERLGISDEEYAALGAGIVS-REEILAKCDVICDPK-PGDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 84 VGLIREGSTLIGFIWPAQNPELMQQLAAKRVTVLA---M---DSLPR-TLSRAQKMdaltstagvSGYRAVIEAANAFGR 156
Cdd:cd12181 79 YLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAwedMfewSKIGRhVFYKNNEL---------AGYAAVLHALQLYGI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 157 FFNGQITAAgkvapakVFiagagvaglaaigtaaSLGAIVRAndtraevADQVVSLGGEFVKVDYdeegsggggyakvms 236
Cdd:cd12181 150 TPYRQTKVA-------VL----------------GFGNTARG-------AIRALKLGGADVTVYT--------------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860583002 237 egfqaaQREMYAQQA--KECDIIITTALI-PGKPAPkLITAEMVQSMKPGSVIVDMAAEQGGNCELTEP 302
Cdd:cd12181 185 ------RRTEALFKEelSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFAKP 246
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
448-531 |
4.04e-07 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 52.31 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 448 CFIGYMVVWNVTPALHT--PLMSVTNSI---SSIIVIGALVQVAPPLA-------------------------------- 490
Cdd:COG3288 134 NFAGYKAVLLAAPALHTffPLMSTAAGTirpAGVLVVGAGVAGLQAIAtakrlgavveaydvrpavkeqveslgakfvel 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860583002 491 -------DGMARP----------ELLIKCLAAAGIALTAINMFGG---FAVTRRMLDMFRK 531
Cdd:COG3288 214 aidangaGGYAKElseeekakqaELLAEHIAKADIVITTALIPGRpapFLVTERMLAMMKP 274
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
10-69 |
7.72e-07 |
|
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: 51.08 E-value: 7.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860583002 10 ESFPGEKRVATVPEVVEKLIKLGFSVSVESGAgdEANFSDDTYRAAGAQIVqgAANLWST 69
Cdd:cd12188 8 ETKPLERRTALTPTTAKKLLDAGFKVTVERSP--QRIFPDEEYEAVGCELV--PAGSWVN 63
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
4-77 |
1.20e-03 |
|
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.
Pssm-ID: 240623 [Multi-domain] Cd Length: 319 Bit Score: 41.07 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860583002 4 VIGVPRES-FPGEKRVATVPEVVEKLIK--LGFSVSVESGagDEANFSDDTYRAAGAQIVQGAanlwSTSDIVFKVR 77
Cdd:cd05199 1 KIGIIREGkTPPDRRVPLTPEQCKELQAkyPGVEIFVQPS--PVRCFKDEEYRAAGIEVVEDL----SDCDILLGVK 71
|
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