|
Name |
Accession |
Description |
Interval |
E-value |
| PNTB |
pfam02233 |
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ... |
622-1079 |
0e+00 |
|
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.
Pssm-ID: 460502 Cd Length: 454 Bit Score: 714.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 622 IMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLGVLKPGPELLAQ-MSGAMALGGTIGLTIAKRIQISDLP 700
Cdd:pfam02233 1 AAYLVAAVLFILGLKGLSSPKTARRGNLLGAIGMALAIVATLLLGALADSLPYGlILIAIAIGGVIGLYIARRVKMTAMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 701 QLVAAFHSLVGLAAVLTCIAEYIIEYPHfaTDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLL 780
Cdd:pfam02233 81 QLVALFHSLGGLAAVLVAIAEYLAPEAF--GAGISAFHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSSKPLTLPGRHLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 781 NAGLLAASVGGIIPFMVDPSFTTgitcLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 860
Cdd:pfam02233 159 NLLLLLAIVVLGVLFVAAPSSPG----LWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVLGNPLLII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 861 VGALIGSSGAILSYIMCVAMNRSLANVILGGYG-TTSTAGGKPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAK 939
Cdd:pfam02233 235 AGALVGASGAILTYIMCKAMNRSLTNVLFGGFGaAASAGAAGAAAADGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 940 AQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQED 1019
Cdd:pfam02233 315 AQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVVNPAARTD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 1020 PNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAK 1079
Cdd:pfam02233 395 PGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEELVKA 454
|
|
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
57-587 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 688.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPmvnpt 136
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 137 lGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFT 216
Cdd:PRK09424 76 -SDDEIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 217 GQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEF 296
Cdd:PRK09424 155 GQITAAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 297 IEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYI-HKGITHIGYTD 375
Cdd:PRK09424 235 IKAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 376 LPSRMATQASTLYSNNITKLLKAISPDKD-NFYFDVKDDfdfgtmghVIRGTVVMKDGKVIFPAPTPKNIPQGAPVKQKT 454
Cdd:PRK09424 315 LPSRLPTQSSQLYGTNLVNLLKLLCPEKDgNIVVDFDDV--------VIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 455 VAELEAEKAAtitpfrKTMSTASAYTAGLTGILGLGIAAPNlAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAI 534
Cdd:PRK09424 387 AAKEEEKKPA------SPWRKYALMALAAALFGWLASVAPA-EFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAI 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034644404 535 SGLTAVGGLALMGGHlypSTTSQGLAALAAFISSVNIAGGFLVTQRMLDMFKR 587
Cdd:PRK09424 460 SGIIVVGALLQIGSG---SGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| PntB |
COG1282 |
NAD/NADP transhydrogenase beta subunit [Energy production and conversion]; |
618-1076 |
0e+00 |
|
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
Pssm-ID: 440893 Cd Length: 458 Bit Score: 630.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 618 NIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLgvLKPGPELLAQMSGAMALGGTIGLTIAKRIQIS 697
Cdd:COG1282 4 TLITLAYLVAAVLFILGLKGLSSPETARRGNLLGAVGMLIAVVATL--LLPGIVNYGLILAAIAIGGAIGAVLARKVEMT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 698 DLPQLVAAFHSLVGLAAVLTCIAEYIieYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGR 777
Cdd:COG1282 82 AMPQLVALFNGFGGLAAALVAAAELL--EPGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPITFPGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 778 HLLNAGLLAASVGGIIPFMVDPSfttGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNL 857
Cdd:COG1282 160 HLLNLLLLLAIVALGVLFVVSPG---SLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGNDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 858 LTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKpMEISGTHTEINLDNAIDMIREANSIIITPGYGLCA 937
Cdd:COG1282 237 LIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAAG-AAEQGEVKEISAEDAAILLAYASSVIIVPGYGMAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 938 AKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQ 1017
Cdd:COG1282 316 AQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAAR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644404 1018 EDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDAL 1076
Cdd:COG1282 396 TDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEEL 454
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
57-432 |
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: 583.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLA-SDLVVKVRAPMVnp 135
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAqADIVLKVRPPSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 136 tlgvHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFF 215
Cdd:cd05304 79 ----EEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 216 TGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKE 295
Cdd:cd05304 155 PMLMTAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 296 FIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTD 375
Cdd:cd05304 235 FLAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTN 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644404 376 LPSRMATQASTLYSNNITKLLKAISPDKDNFYFDVKDDfdfgtmghVIRGTVVMKDG 432
Cdd:cd05304 315 LPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDE--------IVRGTLVTHDG 363
|
|
| pntB |
PRK09444 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta; |
624-1076 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
Pssm-ID: 236520 Cd Length: 462 Bit Score: 559.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 624 YLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATlgVLKPGPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLV 703
Cdd:PRK09444 10 YIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIAT--IFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEMTEMPELV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 704 AAFHSLVGLAAVLTCIAEYIiEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLLNAG 783
Cdd:PRK09444 88 AILHSFVGLAAVLVGFNSYL-DHDAGMAPVLVNIHLTEVFLGIFIGAVTFTGSIVAFGKLRGKISSKPLMLPHRHKLNLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 784 LLAASVGGIIPFMVDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGA 863
Cdd:PRK09444 167 ALVVSFLLLIVFVRTDSVGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 864 LIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEIsGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYP 943
Cdd:PRK09444 247 LVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEV-GEHRETTAEEVAEMLKNSHSVIITPGYGMAVAQAQYP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 944 IADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDPNSI 1023
Cdd:PRK09444 326 VAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAQEDPNSP 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034644404 1024 IAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDAL 1076
Cdd:PRK09444 406 IAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAI 458
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
59-587 |
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: 551.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 59 VGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPMVNptlg 138
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 139 vhEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQ 218
Cdd:TIGR00561 78 --EIALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 219 ITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIE 298
Cdd:TIGR00561 156 ITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 299 AEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELY-IHKGITHIGYTDLP 377
Cdd:TIGR00561 236 AAMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFtTENGVKVIGYTDFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 378 SRMATQASTLYSNNITKLLKAISPDKDNfyfDVKDDFDfgtmGHVIRGTVVMKDGKVIFPAPtPKNIPQGAPVKQKTVAE 457
Cdd:TIGR00561 316 GRLPTQSSQLYGTNLVNLLKLLCKEKDG---NINIDFD----DVVIRGVTVIRAGEETIPAA-PIQVSAQPKAAQKAAPE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 458 LEAEKAATITPFRKTMSTAsaytagLTGILGLGIA--APNlAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAIS 535
Cdd:TIGR00561 388 AEKEEKCPCDPRRKYALMA------GAGILFGWLAsvAPA-AFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAIS 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034644404 536 GLTAVGGLALM---GGHLYPSTtsqgLAALAAFISSVNIAGGFLVTQRMLDMFKR 587
Cdd:TIGR00561 461 GIIIVGALLQIgqgGGNLFIDA----LAFIAILIASINIFGGFRVTQRMLAMFRK 511
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
57-433 |
2.15e-138 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 421.33 E-value: 2.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIqGAKEVLASDLVVKVRAPmvnpt 136
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEI-VDAELLGADIVLKVRPP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 137 lGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFT 216
Cdd:COG3288 75 -SAEELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 217 GQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLkeSGEGQGGYAKEMSKEF 296
Cdd:COG3288 154 LMSTAAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAI--DANGAGGYAKELSEEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 297 IEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTDL 376
Cdd:COG3288 232 KAKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644404 377 PSRMATQASTLYSNNITKLLKAISPDKdNFYFDVKDDfdfgtmghVIRGTVVMKDGK 433
Cdd:COG3288 312 PSRLPAHASQLYAKNLLNFLELLVKDG-ALALDLEDE--------IVAGTLLTHDGE 359
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
203-436 |
4.22e-71 |
|
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: 235.47 E-value: 4.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 203 AVVLAANHFGRFFTGQITAAGKVP---PAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKS-LGAEPLEVdl 278
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 279 kesgegqggyakemskefIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFET-- 356
Cdd:pfam01262 79 ------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 357 -TKPGEL-YIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAIspdKDNFYFDV-KDDfdfgtmgHVIRGTVVMKDGK 433
Cdd:pfam01262 141 pTTHGEPvYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADKGLKAAlLED-------EALRAGLNTHDGK 210
|
...
gi 1034644404 434 VIF 436
Cdd:pfam01262 211 ITH 213
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
208-372 |
8.13e-52 |
|
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: 178.47 E-value: 8.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 208 ANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKS-LGAEPLEvdlkesgegqg 286
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 287 gyakemskefIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPG----EL 362
Cdd:smart01002 70 ----------LYSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTthddPT 139
|
170
....*....|
gi 1034644404 363 YIHKGITHIG 372
Cdd:smart01002 140 YVVDGVVHYC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PNTB |
pfam02233 |
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ... |
622-1079 |
0e+00 |
|
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.
Pssm-ID: 460502 Cd Length: 454 Bit Score: 714.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 622 IMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLGVLKPGPELLAQ-MSGAMALGGTIGLTIAKRIQISDLP 700
Cdd:pfam02233 1 AAYLVAAVLFILGLKGLSSPKTARRGNLLGAIGMALAIVATLLLGALADSLPYGlILIAIAIGGVIGLYIARRVKMTAMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 701 QLVAAFHSLVGLAAVLTCIAEYIIEYPHfaTDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLL 780
Cdd:pfam02233 81 QLVALFHSLGGLAAVLVAIAEYLAPEAF--GAGISAFHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSSKPLTLPGRHLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 781 NAGLLAASVGGIIPFMVDPSFTTgitcLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 860
Cdd:pfam02233 159 NLLLLLAIVVLGVLFVAAPSSPG----LWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVLGNPLLII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 861 VGALIGSSGAILSYIMCVAMNRSLANVILGGYG-TTSTAGGKPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAK 939
Cdd:pfam02233 235 AGALVGASGAILTYIMCKAMNRSLTNVLFGGFGaAASAGAAGAAAADGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 940 AQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQED 1019
Cdd:pfam02233 315 AQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVVNPAARTD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 1020 PNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAK 1079
Cdd:pfam02233 395 PGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEELVKA 454
|
|
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
57-587 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 688.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPmvnpt 136
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 137 lGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFT 216
Cdd:PRK09424 76 -SDDEIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 217 GQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEF 296
Cdd:PRK09424 155 GQITAAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 297 IEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYI-HKGITHIGYTD 375
Cdd:PRK09424 235 IKAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 376 LPSRMATQASTLYSNNITKLLKAISPDKD-NFYFDVKDDfdfgtmghVIRGTVVMKDGKVIFPAPTPKNIPQGAPVKQKT 454
Cdd:PRK09424 315 LPSRLPTQSSQLYGTNLVNLLKLLCPEKDgNIVVDFDDV--------VIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 455 VAELEAEKAAtitpfrKTMSTASAYTAGLTGILGLGIAAPNlAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAI 534
Cdd:PRK09424 387 AAKEEEKKPA------SPWRKYALMALAAALFGWLASVAPA-EFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAI 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034644404 535 SGLTAVGGLALMGGHlypSTTSQGLAALAAFISSVNIAGGFLVTQRMLDMFKR 587
Cdd:PRK09424 460 SGIIVVGALLQIGSG---SGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| PntB |
COG1282 |
NAD/NADP transhydrogenase beta subunit [Energy production and conversion]; |
618-1076 |
0e+00 |
|
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
Pssm-ID: 440893 Cd Length: 458 Bit Score: 630.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 618 NIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLgvLKPGPELLAQMSGAMALGGTIGLTIAKRIQIS 697
Cdd:COG1282 4 TLITLAYLVAAVLFILGLKGLSSPETARRGNLLGAVGMLIAVVATL--LLPGIVNYGLILAAIAIGGAIGAVLARKVEMT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 698 DLPQLVAAFHSLVGLAAVLTCIAEYIieYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGR 777
Cdd:COG1282 82 AMPQLVALFNGFGGLAAALVAAAELL--EPGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPITFPGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 778 HLLNAGLLAASVGGIIPFMVDPSfttGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNL 857
Cdd:COG1282 160 HLLNLLLLLAIVALGVLFVVSPG---SLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGNDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 858 LTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKpMEISGTHTEINLDNAIDMIREANSIIITPGYGLCA 937
Cdd:COG1282 237 LIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAAG-AAEQGEVKEISAEDAAILLAYASSVIIVPGYGMAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 938 AKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQ 1017
Cdd:COG1282 316 AQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAAR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644404 1018 EDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDAL 1076
Cdd:COG1282 396 TDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEEL 454
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
57-432 |
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: 583.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLA-SDLVVKVRAPMVnp 135
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVSDAEELAqADIVLKVRPPSE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 136 tlgvHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFF 215
Cdd:cd05304 79 ----EEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 216 TGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKE 295
Cdd:cd05304 155 PMLMTAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 296 FIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTD 375
Cdd:cd05304 235 FLAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTN 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644404 376 LPSRMATQASTLYSNNITKLLKAISPDKDNFYFDVKDDfdfgtmghVIRGTVVMKDG 432
Cdd:cd05304 315 LPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDE--------IVRGTLVTHDG 363
|
|
| pntB |
PRK09444 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta; |
624-1076 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
Pssm-ID: 236520 Cd Length: 462 Bit Score: 559.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 624 YLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATlgVLKPGPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLV 703
Cdd:PRK09444 10 YIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIAT--IFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEMTEMPELV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 704 AAFHSLVGLAAVLTCIAEYIiEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLLNAG 783
Cdd:PRK09444 88 AILHSFVGLAAVLVGFNSYL-DHDAGMAPVLVNIHLTEVFLGIFIGAVTFTGSIVAFGKLRGKISSKPLMLPHRHKLNLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 784 LLAASVGGIIPFMVDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGA 863
Cdd:PRK09444 167 ALVVSFLLLIVFVRTDSVGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 864 LIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEIsGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYP 943
Cdd:PRK09444 247 LVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEV-GEHRETTAEEVAEMLKNSHSVIITPGYGMAVAQAQYP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 944 IADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDPNSI 1023
Cdd:PRK09444 326 VAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAQEDPNSP 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034644404 1024 IAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDAL 1076
Cdd:PRK09444 406 IAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAI 458
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
59-587 |
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: 551.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 59 VGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPMVNptlg 138
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 139 vhEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQ 218
Cdd:TIGR00561 78 --EIALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 219 ITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIE 298
Cdd:TIGR00561 156 ITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 299 AEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELY-IHKGITHIGYTDLP 377
Cdd:TIGR00561 236 AAMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFtTENGVKVIGYTDFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 378 SRMATQASTLYSNNITKLLKAISPDKDNfyfDVKDDFDfgtmGHVIRGTVVMKDGKVIFPAPtPKNIPQGAPVKQKTVAE 457
Cdd:TIGR00561 316 GRLPTQSSQLYGTNLVNLLKLLCKEKDG---NINIDFD----DVVIRGVTVIRAGEETIPAA-PIQVSAQPKAAQKAAPE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 458 LEAEKAATITPFRKTMSTAsaytagLTGILGLGIA--APNlAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAIS 535
Cdd:TIGR00561 388 AEKEEKCPCDPRRKYALMA------GAGILFGWLAsvAPA-AFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAIS 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034644404 536 GLTAVGGLALM---GGHLYPSTtsqgLAALAAFISSVNIAGGFLVTQRMLDMFKR 587
Cdd:TIGR00561 461 GIIIVGALLQIgqgGGNLFIDA----LAFIAILIASINIFGGFRVTQRMLAMFRK 511
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
57-433 |
2.15e-138 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 421.33 E-value: 2.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIqGAKEVLASDLVVKVRAPmvnpt 136
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEI-VDAELLGADIVLKVRPP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 137 lGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFT 216
Cdd:COG3288 75 -SAEELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 217 GQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLkeSGEGQGGYAKEMSKEF 296
Cdd:COG3288 154 LMSTAAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAI--DANGAGGYAKELSEEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 297 IEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTDL 376
Cdd:COG3288 232 KAKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644404 377 PSRMATQASTLYSNNITKLLKAISPDKdNFYFDVKDDfdfgtmghVIRGTVVMKDGK 433
Cdd:COG3288 312 PSRLPAHASQLYAKNLLNFLELLVKDG-ALALDLEDE--------IVAGTLLTHDGE 359
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
58-396 |
4.07e-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: 245.40 E-value: 4.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 58 TVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQI--QGAKEVLASDLVVKVRAPMVNp 135
Cdd:cd01620 1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIvpAASKEAYSADIIVKLKEPEFA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 136 tlgvhEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIaqgyDALSSMANIAGYKAVVLAANHFGRFF 215
Cdd:cd01620 80 -----EYDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR----PRLAPNSNIAGYAGVQLGAYELARIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 216 TGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKEsgegqggyakEMSKE 295
Cdd:cd01620 151 GGRMGGAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKE----------ELEKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 296 FieaemklfaqqcKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFE----TTKPGELYIHKGITHI 371
Cdd:cd01620 221 L------------KQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDEtsipTTEGVPTYEVDGVVIY 288
|
330 340
....*....|....*....|....*
gi 1034644404 372 GYTDLPSRMATQASTLYSNNITKLL 396
Cdd:cd01620 289 GVDNMPSLVPREASELLSKNLLPYL 313
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
203-436 |
4.22e-71 |
|
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: 235.47 E-value: 4.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 203 AVVLAANHFGRFFTGQITAAGKVP---PAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKS-LGAEPLEVdl 278
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 279 kesgegqggyakemskefIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFET-- 356
Cdd:pfam01262 79 ------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 357 -TKPGEL-YIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAIspdKDNFYFDV-KDDfdfgtmgHVIRGTVVMKDGK 433
Cdd:pfam01262 141 pTTHGEPvYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADKGLKAAlLED-------EALRAGLNTHDGK 210
|
...
gi 1034644404 434 VIF 436
Cdd:pfam01262 211 ITH 213
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
57-399 |
7.37e-67 |
|
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: 229.21 E-value: 7.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQI-QGAKEV-LASDLVVKVRAPMvn 134
Cdd:cd05305 1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIvPTAEEVwAKADLIVKVKEPL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 135 ptlgVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDqvprvTIAQGYDA---LSSMANIAGYKAVVLAANHF 211
Cdd:cd05305 79 ----PEEYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYE-----TIEDEDGSlplLAPMSEIAGRLAVQIGAEYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 212 GRFFTGQ------ITAagkVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVdlkesgegq 285
Cdd:cd05305 150 EKPNGGRgvllggVPG---VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTT--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 286 ggyakEMSKEfieaemKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGEL--- 362
Cdd:cd05305 218 -----LYSNP------ANLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRPTTHdnp 286
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034644404 363 -YIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAI 399
Cdd:cd05305 287 tYVVHGVIHYCVPNMPGAVPRTSTLALTNATLPYLLKL 324
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
57-393 |
4.09e-59 |
|
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: 207.56 E-value: 4.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 57 LTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQI-QGAKEV-LASDLVVKVRAPMvn 134
Cdd:COG0686 1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIvDTAEEVfAQADLIVKVKEPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 135 ptlgVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQvprVTIAQG-YDALSSMANIAGYKAVVLAANHFGR 213
Cdd:COG0686 79 ----PEEYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYET---VEDPDGsLPLLAPMSEIAGRMAIQIGAEYLEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 214 FFTGQitaaGK-------VPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVdlkesgegqg 286
Cdd:COG0686 152 PNGGR----GVllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTT---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 287 gyakEMSKEfieaemKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKP---GE-L 362
Cdd:COG0686 218 ----LYSNP------ANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRPtthDDpT 287
|
330 340 350
....*....|....*....|....*....|.
gi 1034644404 363 YIHKGITHIGYTDLPSRMAtQASTLYSNNIT 393
Cdd:COG0686 288 YVVHGVVHYCVANMPGAVP-RTSTYALTNAT 317
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
208-372 |
8.13e-52 |
|
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: 178.47 E-value: 8.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 208 ANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKS-LGAEPLEvdlkesgegqg 286
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 287 gyakemskefIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPG----EL 362
Cdd:smart01002 70 ----------LYSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTthddPT 139
|
170
....*....|
gi 1034644404 363 YIHKGITHIG 372
Cdd:smart01002 140 YVVDGVVHYC 149
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
60-199 |
3.78e-51 |
|
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: 176.08 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 60 GVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQ-GAKEVLA-SDLVVKVRAPMvnptl 137
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVdTAAEVWAeADLILKVKEPQ----- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644404 138 gVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRvTIAQGYDALSSMANIA 199
Cdd:pfam05222 76 -PEEYALLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANIA 135
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
60-197 |
1.63e-50 |
|
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: 174.14 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 60 GVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLA-SDLVVKVRAPMVNptlg 138
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWAdADIILKVKEPSPE---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644404 139 vhEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMAN 197
Cdd:smart01003 77 --ELALLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
59-392 |
9.13e-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: 155.85 E-value: 9.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 59 VGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLAS-DLVVKVRAPMVNPtl 137
Cdd:cd12154 1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLAKALWSlDVVLKVKEPLTNA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 138 gvhEADLLKTSGT--LISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTiaqgydaLSSMANIAGYKAVVLAANHFGRFF 215
Cdd:cd12154 79 ---EYALIQKLGDrlLFTYTIGADHRDLTEALARAGLTAIAVEGVELPL-------LTSNSIGAGELSVQFIARFLEVQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 216 TGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAeplevdlkesgegqggyakemsKE 295
Cdd:cd12154 149 PGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGG----------------------KN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 296 FIEAEmklfaQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTD 375
Cdd:cd12154 207 VEELE-----EALAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDVN 281
|
330 340
....*....|....*....|..
gi 1034644404 376 LPSRMATQ-----ASTLYSNNI 392
Cdd:cd12154 282 MPGPGCAMgvpwdATLRLAANT 303
|
|
| PNTB_4TM |
pfam12769 |
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of ... |
502-587 |
2.89e-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: 137.20 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 502 VTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLALMGGHLypSTTSQGLAALAAFISSVNIAGGFLVTQRM 581
Cdd:pfam12769 1 LTVFVLALFVGYEVIWKVPPALHTPLMSVTNAISGIIIVGALLAAGGGD--TTLATVLGFIAVVLATINVVGGFLVTDRM 78
|
....*.
gi 1034644404 582 LDMFKR 587
Cdd:pfam12769 79 LDMFKK 84
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
58-413 |
1.05e-17 |
|
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: 84.97 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 58 TVGVPKEIFQNEKRVALSPAGVQNLvKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPMvnptl 137
Cdd:cd12181 2 TGGFGISNKENEKRVPLLPADLERI-PLREQLYFEEGYGERLGISDEEYAALGAGIVSREEILAKCDVICDPKPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 138 gvhEADL--LKTSGTLISFIYPAQNPELLNKLSQRKTTVLA---M---DQVPRVTIaqgYDAlssmANIAGYKAVVLAAN 209
Cdd:cd12181 76 ---DADYleILEGQILWGWVHCVQDKEITQLAIDKKLTLIAwedMfewSKIGRHVF---YKN----NELAGYAAVLHALQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 210 HFGRFFTGQItaagkvppaKILIVGggvaglasagaaksMGAIVRGfdtraaALEQFKSLGAeplEVDLkesgegqggya 289
Cdd:cd12181 146 LYGITPYRQT---------KVAVLG--------------FGNTARG------AIRALKLGGA---DVTV----------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 290 kemskeFIEAEMKLFAQQCKEVDILISTALI-PGKKAPVLfNKEMIESMKEGSVVVDLAAEAGGNFETTKPGEL----YI 364
Cdd:cd12181 183 ------YTRRTEALFKEELSEYDIIVNCILQdTDRPDHII-YEEDLKRLKPGALIIDVSCDEGMGIEFAKPTTFddpiYK 255
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034644404 365 HKGITHIGYTDLPSrmatqastLYSNNITKLL-KAISPdkdnfYFDVKDD 413
Cdd:cd12181 256 VDGIDYYAVDHTPS--------LFYRSASRSIsKALAP-----YLDTVIE 292
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
58-357 |
5.33e-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: 49.54 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 58 TVGVPKE--IFQnEKRVALSPAGVQNLVKQGFNV--VVESGAGEAskFSDDHYRVAGAQIQ----------GAKEVLASD 123
Cdd:cd05199 1 KIGIIREgkTPP-DRRVPLTPEQCKELQAKYPGVeiFVQPSPVRC--FKDEEYRAAGIEVVedlsdcdillGVKEVPIEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 124 LVVKvrapmvnptlgvheadllKT----SGTlisfiYPAQ--NPELLNKLSQRKTT-----VLAMDQVPRVtIAQGYdal 192
Cdd:cd05199 78 LIPN------------------KTyfffSHT-----IKKQpyNRKLLQTILEKNITlidyeVLVDEQGKRV-IAFGR--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 193 ssMANIAG-YKAVVLAANHFGRF----------FTGQITAAGKV--PPAKILIVGGGVAGLasagaaksmgaivrgfdtr 259
Cdd:cd05199 131 --YAGIVGaYNGLRAYGKKTGLFdlkrahecsdLEELIAELKKVglPPPKIVITGSGRVGS------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 260 aAALEQFKSLGAEPLEVDlkesgegqggyakemskEFIEAemklfaqqckeVDILISTALIpGKKAPVLFNKEMIEsmKE 339
Cdd:cd05199 190 -GAAEVLKALGIKEVSPE-----------------DFLTV-----------ADILINGHYW-DKRAPRLFTKEDLK--KP 237
|
330 340
....*....|....*....|.
gi 1034644404 340 G---SVVVDLAAEAGGNFETT 357
Cdd:cd05199 238 DfkiRVIADVTCDIHGSIPST 258
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|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
42-113 |
1.55e-05 |
|
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: 48.38 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644404 42 LWCKAPVKPgipykqltvgvpkeifqNEKRVALSPAGVQNLVKQGFNVVVESGAGEAskFSDDHYRVAGAQI 113
Cdd:cd12188 3 LWLRAETKP-----------------LERRTALTPTTAKKLLDAGFKVTVERSPQRI--FPDEEYEAVGCEL 55
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|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
229-278 |
6.97e-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: 43.53 E-value: 6.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1034644404 229 KILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDL 278
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVVL 55
|
|
| MDR_TM0436_like |
cd08231 |
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ... |
190-285 |
2.32e-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: 41.48 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 190 DALSSMANIAGykAVVLAAnhfgrfftgqITAAGKVPPAK-ILIVGGGVAGLASAGAAKSMGAI-VRGFDTRAAALEQFK 267
Cdd:cd08231 152 DEVAAPANCAL--ATVLAA----------LDRAGPVGAGDtVVVQGAGPLGLYAVAAAKLAGARrVIVIDGSPERLELAR 219
|
90
....*....|....*...
gi 1034644404 268 SLGAEPLeVDLKESGEGQ 285
Cdd:cd08231 220 EFGADAT-IDIDELPDPQ 236
|
|
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
69-124 |
6.24e-03 |
|
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase 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. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.
Pssm-ID: 240665 [Multi-domain] Cd Length: 433 Bit Score: 40.23 E-value: 6.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644404 69 EKRVALSPAGVQNLVKQ-GFNVVVESGAGEAskFSDDHYRVAGAQIQ----------GAKEVLASDL 124
Cdd:cd12189 13 ERRAPLTPSHVRELVKKpGVKVLVQPSNRRA--FPDQEYEAAGAIIQedlsdadlilGVKEPPIDKL 77
|
|
| PRK08306 |
PRK08306 |
dipicolinate synthase subunit DpsA; |
228-355 |
6.93e-03 |
|
dipicolinate synthase subunit DpsA;
Pssm-ID: 181371 [Multi-domain] Cd Length: 296 Bit Score: 39.82 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644404 228 AKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDlkesgegqggyakEMSKEFieaemklfaqq 307
Cdd:PRK08306 153 SNVLVLGFGRTGMTLARTLKALGANVTVGARKSAHLARITEMGLSPFHLS-------------ELAEEV----------- 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034644404 308 cKEVDILISTalIPgkkAPVLfNKEMIESMKEGSVVVDLAAEAGG-NFE 355
Cdd:PRK08306 209 -GKIDIIFNT--IP---ALVL-TKEVLSKMPPEALIIDLASKPGGtDFE 250
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
220-287 |
7.88e-03 |
|
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: 39.61 E-value: 7.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644404 220 TAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGA----EPLEVDLKESGEGQGG 287
Cdd:cd05188 128 RAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGAdhviDYKEEDLEEELRLTGG 199
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