|
Name |
Accession |
Description |
Interval |
E-value |
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
1-509 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 959.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVWQSDILLKVNAPLDEEV 80
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 81 ELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAA 160
Cdd:PRK09424 81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 161 GKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEMA 240
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 241 LFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTENGVKIIGYTDLPSRLS 320
Cdd:PRK09424 241 LFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 321 TQSSQLYGTNLVNLLKLLCKEKNGEIDIDFDDNVIRGVTVIKSGEITWPAPPIQVSaQPQQAKPAAAAVAQQDAKPASPW 400
Cdd:PRK09424 321 TQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVS-AAPAAAAAAPAAKEEEKKPASPW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 401 KKFIFIAIAIVLFGWLANVAPKEFLSHFTVFALSCVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGHGGW-VS 479
Cdd:PRK09424 400 RKYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGSGSGlVT 479
|
490 500 510
....*....|....*....|....*....|
gi 742462265 480 FFSFIAVLIASINIFGGFTVTQRMLKMFRK 509
Cdd:PRK09424 480 FLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
2-510 |
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: 841.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 2 RIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVWQSDILLKVNAPLDEEVE 81
Cdd:TIGR00561 1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 82 LTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAAG 161
Cdd:TIGR00561 81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 162 KVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEMAL 241
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAMEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 242 FAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTENGVKIIGYTDLPSRLST 321
Cdd:TIGR00561 241 FAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENGVKVIGYTDFPGRLPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 322 QSSQLYGTNLVNLLKLLCKEKNGEIDIDFDDNVIRGVTVIKSGEITWPAPPIQVSAQPQQAKPAAAAVAQQDAKPASPWK 401
Cdd:TIGR00561 321 QSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAAQKAAPEAEKEEKCPCDPRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 402 KFIFIAIAIVLFGWLANVAPKEFLSHFTVFALSCVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGHGG---WV 478
Cdd:TIGR00561 401 KYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQIGQGGgnlFI 480
|
490 500 510
....*....|....*....|....*....|..
gi 742462265 479 SFFSFIAVLIASINIFGGFTVTQRMLKMFRKN 510
Cdd:TIGR00561 481 DALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
1-364 |
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: 560.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA-VWQSDILLKVNAPLDEE 79
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEeLAQADIVLKVRPPSEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 80 VELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITA 159
Cdd:cd05304 81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 160 AGKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEM 239
Cdd:cd05304 161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAKQR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 240 ALFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTeNGVKIIGYTDLPSRL 319
Cdd:cd05304 241 ELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVT-NGVTIIGPTNLPSRL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 742462265 320 STQSSQLYGTNLVNLLKLLCKEKnGEIDIDFDDNVIRGVTVIKSG 364
Cdd:cd05304 320 PTQASQLYAKNLLNFLELLVKDD-GELTLDLEDEIVRGTLVTHDG 363
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
1-365 |
1.03e-158 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 455.23 E-value: 1.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDtAAVWQSDILLKVNAPLDEEV 80
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVD-AELLGADIVLKVRPPSAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 81 ELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAA 160
Cdd:COG3288 80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 161 GKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGaEFLELEFEEEAGSGdGYAKVMSEAFIKAEMA 240
Cdd:COG3288 160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLG-AKFVELAIDANGAG-GYAKELSEEEKAKQAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 241 LFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRvTVTENGVKIIGYTDLPSRLS 320
Cdd:COG3288 238 LLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGE-TVTKNGVTIIGPTNLPSRLP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 742462265 321 TQSSQLYGTNLVNLLKLLCKEknGEIDIDFDDNVIRGVTVIKSGE 365
Cdd:COG3288 317 AHASQLYAKNLLNFLELLVKD--GALALDLEDEIVAGTLLTHDGE 359
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
141-368 |
1.76e-69 |
|
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: 221.21 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 141 AIVEAAHEFGRFFTGQITAAGKVP---PAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMgaeflelefe 217
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 218 eeagSGDGYAKVmseafIKAEMALFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCE---L 294
Cdd:pfam01262 71 ----LGAKFVET-----LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsrP 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742462265 295 TVADRVTVTENGVKIIGYTDLPSRLSTQSSQLYGTNLVNLLKLLcKEKnGEIDIDFDDNVIRGVTVIKSGEITW 368
Cdd:pfam01262 142 TTHGEPVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL-ADK-GLKAALLEDEALRAGLNTHDGKITH 213
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
4-135 |
1.74e-64 |
|
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: 205.34 E-value: 1.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 4 GVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVW-QSDILLKVNAPLDEEVEL 82
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWaDADIILKVKEPSPEELAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 742462265 83 TRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMAN 135
Cdd:smart01003 81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
1-509 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 959.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVWQSDILLKVNAPLDEEV 80
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 81 ELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAA 160
Cdd:PRK09424 81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 161 GKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEMA 240
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 241 LFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTENGVKIIGYTDLPSRLS 320
Cdd:PRK09424 241 LFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 321 TQSSQLYGTNLVNLLKLLCKEKNGEIDIDFDDNVIRGVTVIKSGEITWPAPPIQVSaQPQQAKPAAAAVAQQDAKPASPW 400
Cdd:PRK09424 321 TQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVS-AAPAAAAAAPAAKEEEKKPASPW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 401 KKFIFIAIAIVLFGWLANVAPKEFLSHFTVFALSCVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGHGGW-VS 479
Cdd:PRK09424 400 RKYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGSGSGlVT 479
|
490 500 510
....*....|....*....|....*....|
gi 742462265 480 FFSFIAVLIASINIFGGFTVTQRMLKMFRK 509
Cdd:PRK09424 480 FLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
2-510 |
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: 841.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 2 RIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVWQSDILLKVNAPLDEEVE 81
Cdd:TIGR00561 1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 82 LTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAAG 161
Cdd:TIGR00561 81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 162 KVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEMAL 241
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAMEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 242 FAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTENGVKIIGYTDLPSRLST 321
Cdd:TIGR00561 241 FAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENGVKVIGYTDFPGRLPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 322 QSSQLYGTNLVNLLKLLCKEKNGEIDIDFDDNVIRGVTVIKSGEITWPAPPIQVSAQPQQAKPAAAAVAQQDAKPASPWK 401
Cdd:TIGR00561 321 QSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAAQKAAPEAEKEEKCPCDPRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 402 KFIFIAIAIVLFGWLANVAPKEFLSHFTVFALSCVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGHGG---WV 478
Cdd:TIGR00561 401 KYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQIGQGGgnlFI 480
|
490 500 510
....*....|....*....|....*....|..
gi 742462265 479 SFFSFIAVLIASINIFGGFTVTQRMLKMFRKN 510
Cdd:TIGR00561 481 DALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
1-364 |
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: 560.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA-VWQSDILLKVNAPLDEE 79
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEeLAQADIVLKVRPPSEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 80 VELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITA 159
Cdd:cd05304 81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 160 AGKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLELEFEEEAGSGDGYAKVMSEAFIKAEM 239
Cdd:cd05304 161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAKQR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 240 ALFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRVTVTeNGVKIIGYTDLPSRL 319
Cdd:cd05304 241 ELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVT-NGVTIIGPTNLPSRL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 742462265 320 STQSSQLYGTNLVNLLKLLCKEKnGEIDIDFDDNVIRGVTVIKSG 364
Cdd:cd05304 320 PTQASQLYAKNLLNFLELLVKDD-GELTLDLEDEIVRGTLVTHDG 363
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
1-365 |
1.03e-158 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 455.23 E-value: 1.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDtAAVWQSDILLKVNAPLDEEV 80
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVD-AELLGADIVLKVRPPSAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 81 ELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQITAA 160
Cdd:COG3288 80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 161 GKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGaEFLELEFEEEAGSGdGYAKVMSEAFIKAEMA 240
Cdd:COG3288 160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLG-AKFVELAIDANGAG-GYAKELSEEEKAKQAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 241 LFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCELTVADRvTVTENGVKIIGYTDLPSRLS 320
Cdd:COG3288 238 LLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGE-TVTKNGVTIIGPTNLPSRLP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 742462265 321 TQSSQLYGTNLVNLLKLLCKEknGEIDIDFDDNVIRGVTVIKSGE 365
Cdd:COG3288 317 AHASQLYAKNLLNFLELLVKD--GALALDLEDEIVAGTLLTHDGE 359
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
2-338 |
7.80e-74 |
|
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: 236.15 E-value: 7.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 2 RIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA--VWQSDILLKVNAPLDEE 79
Cdd:cd01620 1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAASkeAYSADIIVKLKEPEFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 80 VELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRaqsmDALSSMANIAGYRAIVEAAHEFGRFFTGQITA 159
Cdd:cd01620 81 YDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR----PRLAPNSNIAGYAGVQLGAYELARIQGGRMGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 160 AGKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEFLElefeeeagsgdgyaKVMSEAFIKAem 239
Cdd:cd01620 157 AGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLR--------------YSQKEELEKE-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 240 alfaaqAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCEL---TVADRVTVTENGVKIIGYTDLP 316
Cdd:cd01620 221 ------LKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETsipTTEGVPTYEVDGVVIYGVDNMP 294
|
330 340
....*....|....*....|..
gi 742462265 317 SRLSTQSSQLYGTNLVNLLKLL 338
Cdd:cd01620 295 SLVPREASELLSKNLLPYLVKL 316
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
141-368 |
1.76e-69 |
|
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: 221.21 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 141 AIVEAAHEFGRFFTGQITAAGKVP---PAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMgaeflelefe 217
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 218 eeagSGDGYAKVmseafIKAEMALFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCE---L 294
Cdd:pfam01262 71 ----LGAKFVET-----LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsrP 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742462265 295 TVADRVTVTENGVKIIGYTDLPSRLSTQSSQLYGTNLVNLLKLLcKEKnGEIDIDFDDNVIRGVTVIKSGEITW 368
Cdd:pfam01262 142 TTHGEPVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL-ADK-GLKAALLEDEALRAGLNTHDGKITH 213
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
4-135 |
1.74e-64 |
|
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: 205.34 E-value: 1.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 4 GVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVW-QSDILLKVNAPLDEEVEL 82
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWaDADIILKVKEPSPEELAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 742462265 83 TRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISRAQSMDALSSMAN 135
Cdd:smart01003 81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
4-137 |
1.32e-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: 200.73 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 4 GVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA-VW-QSDILLKVNAPLDEEVE 81
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVDTAAeVWaEADLILKVKEPQPEEYA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 742462265 82 LTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRiSRAQSMDALSSMANIA 137
Cdd:pfam05222 81 LLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANIA 135
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
1-370 |
1.34e-57 |
|
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: 195.32 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA-VW-QSDILLKVNAPLDE 78
Cdd:cd05305 1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIVPTAEeVWaKADLIVKVKEPLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 79 EVELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVprISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQ-- 156
Cdd:cd05305 81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETI--EDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGGRgv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 157 ----ITAagkVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAeflelefeeeagsGDGYAKVMSE 232
Cdd:cd05305 159 llggVPG---VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFG-------------GRVTTLYSNP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 233 AFIkaemalfAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCE---LTVADRVTVTENGVki 309
Cdd:cd05305 223 ANL-------EEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFEtsrPTTHDNPTYVVHGV-- 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742462265 310 IGY--TDLPSRLSTQSSQLYgTNlvNLLKLLCK--EKNGEIDIDFDDNVIRGVTVIKsGEITWPA 370
Cdd:cd05305 294 IHYcvPNMPGAVPRTSTLAL-TN--ATLPYLLKlaNKGLEEALLEDPGLAKGLNTYK-GKLTNKA 354
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
1-293 |
3.55e-50 |
|
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: 175.97 E-value: 3.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAA-VW-QSDILLKVNAPLDE 78
Cdd:COG0686 1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIVDTAEeVFaQADLIVKVKEPQPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 79 EVELTRAGSTIISFIWPAQNPALLETLAARQVTVLAMDSVprISRAQSMDALSSMANIAGYRAIVEAAHEFGRFFTGQit 158
Cdd:COG0686 81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETV--EDPDGSLPLLAPMSEIAGRMAIQIGAEYLEKPNGGR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 159 aaGK-------VPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKS-MGAEFLElefeeeagsgdgyakVM 230
Cdd:COG0686 157 --GVllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDiFGGRVTT---------------LY 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742462265 231 SEAFIKAEMALFAaqaqevDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCE 293
Cdd:COG0686 220 SNPANIEEALKEA------DLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFE 276
|
|
| PNTB_4TM |
pfam12769 |
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of ... |
428-509 |
2.85e-44 |
|
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: 150.68 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 428 FTVFALSCVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGHGG--WVSFFSFIAVLIASINIFGGFTVTQRMLK 505
Cdd:pfam12769 1 LTVFVLALFVGYEVIWKVPPALHTPLMSVTNAISGIIIVGALLAAGGGDttLATVLGFIAVVLATINVVGGFLVTDRMLD 80
|
....
gi 742462265 506 MFRK 509
Cdd:pfam12769 81 MFKK 84
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
146-311 |
1.24e-43 |
|
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: 151.12 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 146 AHEFGRFFTGQITAAGKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAeflelefeeeagsgdg 225
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLG---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 226 yAKVMSeafIKAEMALFAAQAQEVDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCEL---TVADRVTV 302
Cdd:smart01002 65 -ARFTT---LYSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETsrpTTHDDPTY 140
|
....*....
gi 742462265 303 TENGVKIIG 311
Cdd:smart01002 141 VVDGVVHYC 149
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
3-335 |
3.32e-38 |
|
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: 141.98 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 3 IGVPKERLANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTA-AVWQSDILLKVNAPL-DEEV 80
Cdd:cd12154 1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLAkALWSLDVVLKVKEPLtNAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 81 ELTR--AGSTIISFIWPAQNPALLETLAARQVTVLAMDSVPRISraqsmdaLSSMANIAGYRAIVEAAHEFGRFFTGQIT 158
Cdd:cd12154 81 ALIQklGDRLLFTYTIGADHRDLTEALARAGLTAIAVEGVELPL-------LTSNSIGAGELSVQFIARFLEVQQPGRLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 159 AAGKVPPAKVLIIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVKEQVKSMGAEflelefeeeagsgdgYAKVMSEAFIKAe 238
Cdd:cd12154 154 GAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGK---------------NVEELEEALAEA- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 239 malfaaqaqevDIIVTTALIPGKPAPRLITKEMVQGMKPGSVIVDLAAQTGGNCElTVADRVTVTENGVKIIGYTDLPSR 318
Cdd:cd12154 218 -----------DVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQ-ALHTQLLEEGHGVVHYGDVNMPGP 285
|
330 340
....*....|....*....|..
gi 742462265 319 LSTQ-----SSQLYGTNLVNLL 335
Cdd:cd12154 286 GCAMgvpwdATLRLAANTLPAL 307
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
1-307 |
6.23e-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: 63.40 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 1 MRIGVPKERLANEARVAATPKTVEQLlKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAVW-QSDILLKVnAPLDEE 79
Cdd:cd12181 1 KTGGFGISNKENEKRVPLLPADLERI-PLREQLYFEEGYGERLGISDEEYAALGAGIVSREEILaKCDVICDP-KPGDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 80 VELTRAGSTIISFIWPAQNPALLETLAARQVTVLA---MDSVPRISRaqsmDALSSMANIAGYRAIVEAAHEFGRFFTGQ 156
Cdd:cd12181 79 YLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAwedMFEWSKIGR----HVFYKNNELAGYAAVLHALQLYGITPYRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 157 ItaagkvppaKVLIIgagvaglaaigaagSLGAIVR-AFDTrpevkeqVKSMGAeflelefeeeagsgdgYAKVmseaFI 235
Cdd:cd12181 155 T---------KVAVL--------------GFGNTARgAIRA-------LKLGGA----------------DVTV----YT 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742462265 236 KAEMALFAAQAQEVDIIVTTALI-PGKPAPrLITKEMVQGMKPGSVIVDLAAQTGGNCEL---TVADRVTVTENGV 307
Cdd:cd12181 185 RRTEALFKEELSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFakpTTFDDPIYKVDGI 259
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
411-473 |
1.15e-08 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 56.93 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 411 VLFGWLANVAPKEFL-----SHFTVFAL------------------SCVVGYYVVWNVSHALHT--PLMSVTNAI---SG 462
Cdd:COG3288 87 VLIGFLDPLGNPELVkalaaAGLTVFALeliprisraqsmdalssqANFAGYKAVLLAAPALHTffPLMSTAAGTirpAG 166
|
90
....*....|.
gi 742462265 463 IIVVGALLQIG 473
Cdd:COG3288 167 VLVVGAGVAGL 177
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
11-77 |
1.33e-06 |
|
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: 50.31 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742462265 11 ANEARVAATPKTVEQLLKLGFEVAIERGAGKLasFEDEAYEQAGATILDTAAvWqsdillkVNAPLD 77
Cdd:cd12188 11 PLERRTALTPTTAKKLLDAGFKVTVERSPQRI--FPDEEYEAVGCELVPAGS-W-------VNAPKD 67
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
3-83 |
2.30e-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: 40.29 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742462265 3 IGVPKER-LANEARVAATPKTVEQLLKLGFEVAIERGAGKLASFEDEAYEQAGATILDTAAvwQSDILLKVnapldEEVE 81
Cdd:cd05199 2 IGIIREGkTPPDRRVPLTPEQCKELQAKYPGVEIFVQPSPVRCFKDEEYRAAGIEVVEDLS--DCDILLGV-----KEVP 74
|
..
gi 742462265 82 LT 83
Cdd:cd05199 75 IE 76
|
|
| |
