|
Name |
Accession |
Description |
Interval |
E-value |
| PNTB |
pfam02233 |
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ... |
618-1072 |
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: 704.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 618 MMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATFGVLKPSPELMAQ-MSAAMAVGGTAGLTIAKKIQISDLP 696
Cdd:pfam02233 1 AAYLVAAVLFILGLKGLSSPKTARRGNLLGAIGMALAIVATLLLGALADSLPYGlILIAIAIGGVIGLYIARRVKMTAMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 697 QLVAAFHSLVGLAAVLTCVAEYMVEYPHfaTDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGRHAL 776
Cdd:pfam02233 81 QLVALFHSLGGLAAVLVAIAEYLAPEAF--GAGISAFHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSSKPLTLPGRHLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 777 NATLMAASVGGMIPYMLDPSYTTgitcLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 856
Cdd:pfam02233 159 NLLLLLAIVVLGVLFVAAPSSPG----LWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVLGNPLLII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 857 VGALIGSSGAILSYIMCVAMNRSLANVILGGYG-TSSTGTGKPMEITGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCAAK 935
Cdd:pfam02233 235 AGALVGASGAILTYIMCKAMNRSLTNVLFGGFGaAASAGAAGAAAADGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 936 AQYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQED 1015
Cdd:pfam02233 315 AQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVVNPAARTD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 1016 PNSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:pfam02233 395 PGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEEL 451
|
|
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
53-583 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 666.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFSSDVLLKVRAPmlnpt 132
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 133 lGVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFT 212
Cdd:PRK09424 76 -SDDEIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 213 GQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKEF 292
Cdd:PRK09424 155 GQITAAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 293 IEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSV-HKGVIHVGYTD 371
Cdd:PRK09424 235 IKAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 372 IPSRLPTQASTLYSNNITKLIRAISPDKetfyfDVKNEFDFGtmDHVIRGSVVMQDGKVLFPAPQPQnvpVAAPPKQKTV 451
Cdd:PRK09424 315 LPSRLPTQSSQLYGTNLVNLLKLLCPEK-----DGNIVVDFD--DVVIRGVTVVRDGEITWPPPPIQ---VSAAPAAAAA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 452 QELQKEKASAVSPFRATLTTAGVYTGGLGtaiGLGLCAPnAAFTQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAIS 531
Cdd:PRK09424 385 APAAKEEEKKPASPWRKYALMALAAALFG---WLASVAP-AEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAIS 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 47550793 532 GLTAVGGLSLMGGGylpSSTAETLAVLAAFISSVNIAGGFLVTQRMLDMFKR 583
Cdd:PRK09424 461 GIIVVGALLQIGSG---SGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| PntB |
COG1282 |
NAD/NADP transhydrogenase beta subunit [Energy production and conversion]; |
614-1072 |
0e+00 |
|
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
Pssm-ID: 440893 Cd Length: 458 Bit Score: 617.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 614 NIEQMMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATFgvLKPSPELMAQMSAAMAVGGTAGLTIAKKIQIS 693
Cdd:COG1282 4 TLITLAYLVAAVLFILGLKGLSSPETARRGNLLGAVGMLIAVVATL--LLPGIVNYGLILAAIAIGGAIGAVLARKVEMT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 694 DLPQLVAAFHSLVGLAAVLTCVAEYMVeyPHFATDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGR 773
Cdd:COG1282 82 AMPQLVALFNGFGGLAAALVAAAELLE--PGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPITFPGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 774 HALNATLMAASVGGMIPYMLDPSyttGITCLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNL 853
Cdd:COG1282 160 HLLNLLLLLAIVALGVLFVVSPG---SLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGNDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 854 LTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTSSTGTGKpMEITGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCA 933
Cdd:COG1282 237 LIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAAG-AAEQGEVKEISAEDAAILLAYASSVIIVPGYGMAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 934 AKAQYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQ 1013
Cdd:COG1282 316 AQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAAR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 47550793 1014 EDPNSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:COG1282 396 TDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEEL 454
|
|
| pntB |
PRK09444 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta; |
617-1072 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
Pssm-ID: 236520 Cd Length: 462 Bit Score: 560.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 617 QMMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATfgVLKPSPELMAQMSAAMAVGGTAGLTIAKKIQISDLP 696
Cdd:PRK09444 7 TAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIAT--IFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEMTEMP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 697 QLVAAFHSLVGLAAVLTCVAEYMvEYPHFATDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGRHAL 776
Cdd:PRK09444 85 ELVAILHSFVGLAAVLVGFNSYL-DHDAGMAPVLVNIHLTEVFLGIFIGAVTFTGSIVAFGKLRGKISSKPLMLPHRHKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 777 NATLMAASVGGMIPYMLDPSYTTGITCLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 856
Cdd:PRK09444 164 NLAALVVSFLLLIVFVRTDSVGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 857 VGALIGSSGAILSYIMCVAMNRSLANVILGGYGTSSTGTGKPMEItGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCAAKA 936
Cdd:PRK09444 244 TGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEV-GEHRETTAEEVAEMLKNSHSVIITPGYGMAVAQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 937 QYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQEDP 1016
Cdd:PRK09444 323 QYPVAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAQEDP 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 47550793 1017 NSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:PRK09444 403 NSPIAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAI 458
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
53-428 |
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: 549.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATI-RDVKDVFSSDVLLKVRAPMlnp 131
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIvSDAEELAQADIVLKVRPPS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 132 tlgVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFF 211
Cdd:cd05304 78 ---EEEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 212 TGQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKE 291
Cdd:cd05304 155 PMLMTAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 292 FIEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSVHKGVIHVGYTD 371
Cdd:cd05304 235 FLAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTN 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 372 IPSRLPTQASTLYSNNITKLIRAISPDKETFYFDVKNEfdfgtmdhVIRGSVVMQDG 428
Cdd:cd05304 315 LPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDE--------IVRGTLVTHDG 363
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
55-583 |
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: 541.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 55 VGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFSSDVLLKVRAPMLNptlg 134
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 135 vhEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFTGQ 214
Cdd:TIGR00561 78 --EIALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 215 ITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKEFIE 294
Cdd:TIGR00561 156 ITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 295 AEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGEL-SVHKGVIHVGYTDIP 373
Cdd:TIGR00561 236 AAMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIfTTENGVKVIGYTDFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 374 SRLPTQASTLYSNNITKLIRAISPDKETfyfDVKNEFDfgtmDHVIRGSVVMQDGKVLFPAPQPQnvpVAAPPK--QKTV 451
Cdd:TIGR00561 316 GRLPTQSSQLYGTNLVNLLKLLCKEKDG---NINIDFD----DVVIRGVTVIRAGEETIPAAPIQ---VSAQPKaaQKAA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 452 QELQKEKASAVSPFR--ATLTTAGVYTGGLGTAiglglcAPnAAFTQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNA 529
Cdd:TIGR00561 386 PEAEKEEKCPCDPRRkyALMAGAGILFGWLASV------AP-AAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNA 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 47550793 530 ISGLTAVGGLSLMGGGyLPSSTAETLAVLAAFISSVNIAGGFLVTQRMLDMFKR 583
Cdd:TIGR00561 459 ISGIIIVGALLQIGQG-GGNLFIDALAFIAILIASINIFGGFRVTQRMLAMFRK 511
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
53-429 |
2.73e-131 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 402.46 E-value: 2.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDvKDVFSSDVLLKVRAPmlnpt 132
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVD-AELLGADIVLKVRPP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 133 lGVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFT 212
Cdd:COG3288 75 -SAEELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 213 GQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIkeSGEGQGGYAKEMSKEF 292
Cdd:COG3288 154 LMSTAAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAI--DANGAGGYAKELSEEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 293 IEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSVHKGVIHVGYTDI 372
Cdd:COG3288 232 KAKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 373 PSRLPTQASTLYSNNITKLIRAISPDKetfyfdvknEFDFGTMDHVIRGSVVMQDGK 429
Cdd:COG3288 312 PSRLPAHASQLYAKNLLNFLELLVKDG---------ALALDLEDEIVAGTLLTHDGE 359
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
199-432 |
1.70e-61 |
|
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: 208.50 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 199 AVVLAANNFGRFFTGQITAAGKVP---PAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKS-LGAEPLEVdi 274
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 275 kesgegqggyakemskefIEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIET-- 352
Cdd:pfam01262 79 ------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 353 -TVPGELSVHK-GVIHVGYTDIPSRLPTQASTLYSNNITKLIRAIspdKETFYFDVKNEfdfgtmDHVIRGSVVMQDGKV 430
Cdd:pfam01262 141 pTTHGEPVYVVdGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADKGLKAALLE------DEALRAGLNTHDGKI 211
|
..
gi 47550793 431 LF 432
Cdd:pfam01262 212 TH 213
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
56-193 |
1.61e-54 |
|
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: 185.70 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 56 GVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFS-SDVLLKVRAPMLNptlg 134
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWAdADIILKVKEPSPE---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 47550793 135 vhEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMAN 193
Cdd:smart01003 77 --ELALLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PNTB |
pfam02233 |
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ... |
618-1072 |
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: 704.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 618 MMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATFGVLKPSPELMAQ-MSAAMAVGGTAGLTIAKKIQISDLP 696
Cdd:pfam02233 1 AAYLVAAVLFILGLKGLSSPKTARRGNLLGAIGMALAIVATLLLGALADSLPYGlILIAIAIGGVIGLYIARRVKMTAMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 697 QLVAAFHSLVGLAAVLTCVAEYMVEYPHfaTDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGRHAL 776
Cdd:pfam02233 81 QLVALFHSLGGLAAVLVAIAEYLAPEAF--GAGISAFHLVEIVLGVLIGAVTFTGSLIAFGKLQGLLSSKPLTLPGRHLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 777 NATLMAASVGGMIPYMLDPSYTTgitcLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 856
Cdd:pfam02233 159 NLLLLLAIVVLGVLFVAAPSSPG----LWLLTALALLLGVLLVLPIGGADMPVVISLLNSYSGWAAAAAGFVLGNPLLII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 857 VGALIGSSGAILSYIMCVAMNRSLANVILGGYG-TSSTGTGKPMEITGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCAAK 935
Cdd:pfam02233 235 AGALVGASGAILTYIMCKAMNRSLTNVLFGGFGaAASAGAAGAAAADGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 936 AQYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQED 1015
Cdd:pfam02233 315 AQHAVAELADLLEERGVEVRFAIHPVAGRMPGHMNVLLAEADVPYDIVLEMDEINDDFADTDVALVIGANDVVNPAARTD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 1016 PNSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:pfam02233 395 PGSPIYGMPILEVWKAKTVIVIKRSMGPGYAGVDNPLFYKDNTRMLFGDAKKSLEEL 451
|
|
| pntA |
PRK09424 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha; |
53-583 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
Pssm-ID: 236507 [Multi-domain] Cd Length: 509 Bit Score: 666.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFSSDVLLKVRAPmlnpt 132
Cdd:PRK09424 1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 133 lGVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFT 212
Cdd:PRK09424 76 -SDDEIALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 213 GQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKEF 292
Cdd:PRK09424 155 GQITAAGKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 293 IEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSV-HKGVIHVGYTD 371
Cdd:PRK09424 235 IKAEMALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVtDNGVTIIGYTD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 372 IPSRLPTQASTLYSNNITKLIRAISPDKetfyfDVKNEFDFGtmDHVIRGSVVMQDGKVLFPAPQPQnvpVAAPPKQKTV 451
Cdd:PRK09424 315 LPSRLPTQSSQLYGTNLVNLLKLLCPEK-----DGNIVVDFD--DVVIRGVTVVRDGEITWPPPPIQ---VSAAPAAAAA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 452 QELQKEKASAVSPFRATLTTAGVYTGGLGtaiGLGLCAPnAAFTQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAIS 531
Cdd:PRK09424 385 APAAKEEEKKPASPWRKYALMALAAALFG---WLASVAP-AEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAIS 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 47550793 532 GLTAVGGLSLMGGGylpSSTAETLAVLAAFISSVNIAGGFLVTQRMLDMFKR 583
Cdd:PRK09424 461 GIIVVGALLQIGSG---SGLVTFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
|
|
| PntB |
COG1282 |
NAD/NADP transhydrogenase beta subunit [Energy production and conversion]; |
614-1072 |
0e+00 |
|
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
Pssm-ID: 440893 Cd Length: 458 Bit Score: 617.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 614 NIEQMMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATFgvLKPSPELMAQMSAAMAVGGTAGLTIAKKIQIS 693
Cdd:COG1282 4 TLITLAYLVAAVLFILGLKGLSSPETARRGNLLGAVGMLIAVVATL--LLPGIVNYGLILAAIAIGGAIGAVLARKVEMT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 694 DLPQLVAAFHSLVGLAAVLTCVAEYMVeyPHFATDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGR 773
Cdd:COG1282 82 AMPQLVALFNGFGGLAAALVAAAELLE--PGALAGALPAIHLIEIVLGVLIGAVTFTGSLIAFGKLQGLISGKPITFPGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 774 HALNATLMAASVGGMIPYMLDPSyttGITCLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNL 853
Cdd:COG1282 160 HLLNLLLLLAIVALGVLFVVSPG---SLLLLLLLTVLALLLGVLLVLPIGGADMPVVISLLNSYSGLAAAAAGFVLGNDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 854 LTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTSSTGTGKpMEITGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCA 933
Cdd:COG1282 237 LIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAAG-AAEQGEVKEISAEDAAILLAYASSVIIVPGYGMAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 934 AKAQYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQ 1013
Cdd:COG1282 316 AQAQHAVRELADLLEERGVEVKFAIHPVAGRMPGHMNVLLAEANVPYDQLLEMDEINPEFAQTDVALVIGANDVVNPAAR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 47550793 1014 EDPNSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:COG1282 396 TDPGSPIYGMPILEVDKAKTVIVIKRSMGPGYAGVENPLFYKDNTRMLFGDAKKSVEEL 454
|
|
| pntB |
PRK09444 |
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta; |
617-1072 |
0e+00 |
|
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
Pssm-ID: 236520 Cd Length: 462 Bit Score: 560.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 617 QMMYLGSGLCCVGALGGLSTQSTARLGNALGMIGVAGGIAATfgVLKPSPELMAQMSAAMAVGGTAGLTIAKKIQISDLP 696
Cdd:PRK09444 7 TAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIAT--IFGPDTGNVGWIIIAMVIGGAIGIRLAKKVEMTEMP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 697 QLVAAFHSLVGLAAVLTCVAEYMvEYPHFATDPAANLTKIVAYLGTYIGGVTFSGSLVAYGKLQGLLNSAPLMLPGRHAL 776
Cdd:PRK09444 85 ELVAILHSFVGLAAVLVGFNSYL-DHDAGMAPVLVNIHLTEVFLGIFIGAVTFTGSIVAFGKLRGKISSKPLMLPHRHKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 777 NATLMAASVGGMIPYMLDPSYTTGITCLGSVSALSAVMGLTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTI 856
Cdd:PRK09444 164 NLAALVVSFLLLIVFVRTDSVGLQVFALLLMTLIALAFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 857 VGALIGSSGAILSYIMCVAMNRSLANVILGGYGTSSTGTGKPMEItGTHTEVNVDQTVDLIKEAHNIIIVPGYGLCAAKA 936
Cdd:PRK09444 244 TGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEV-GEHRETTAEEVAEMLKNSHSVIITPGYGMAVAQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 937 QYPIADLVKSLTDQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDVVLEMDEINEDFPETDLVLVIGANDTVNSAAQEDP 1016
Cdd:PRK09444 323 QYPVAEITEKLRARGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAQEDP 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 47550793 1017 NSIIAGMPVLEVWKSKQVVVMKRSLGVGYAAVDNPIFYKPNTSMLLGDAKKTCDAL 1072
Cdd:PRK09444 403 NSPIAGMPVLEVWKAQNVIVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKASVDAI 458
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
53-428 |
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: 549.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATI-RDVKDVFSSDVLLKVRAPMlnp 131
Cdd:cd05304 1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIvSDAEELAQADIVLKVRPPS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 132 tlgVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFF 211
Cdd:cd05304 78 ---EEEVALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 212 TGQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKE 291
Cdd:cd05304 155 PMLMTAAGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 292 FIEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSVHKGVIHVGYTD 371
Cdd:cd05304 235 FLAKQRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTN 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 372 IPSRLPTQASTLYSNNITKLIRAISPDKETFYFDVKNEfdfgtmdhVIRGSVVMQDG 428
Cdd:cd05304 315 LPSRLPTQASQLYAKNLLNFLELLVKDDGELTLDLEDE--------IVRGTLVTHDG 363
|
|
| pntA |
TIGR00561 |
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ... |
55-583 |
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: 541.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 55 VGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFSSDVLLKVRAPMLNptlg 134
Cdd:TIGR00561 2 IGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 135 vhEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFTGQ 214
Cdd:TIGR00561 78 --EIALLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 215 ITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKESGEGQGGYAKEMSKEFIE 294
Cdd:TIGR00561 156 ITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 295 AEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGEL-SVHKGVIHVGYTDIP 373
Cdd:TIGR00561 236 AAMELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIfTTENGVKVIGYTDFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 374 SRLPTQASTLYSNNITKLIRAISPDKETfyfDVKNEFDfgtmDHVIRGSVVMQDGKVLFPAPQPQnvpVAAPPK--QKTV 451
Cdd:TIGR00561 316 GRLPTQSSQLYGTNLVNLLKLLCKEKDG---NINIDFD----DVVIRGVTVIRAGEETIPAAPIQ---VSAQPKaaQKAA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 452 QELQKEKASAVSPFR--ATLTTAGVYTGGLGTAiglglcAPnAAFTQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNA 529
Cdd:TIGR00561 386 PEAEKEEKCPCDPRRkyALMAGAGILFGWLASV------AP-AAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNA 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 47550793 530 ISGLTAVGGLSLMGGGyLPSSTAETLAVLAAFISSVNIAGGFLVTQRMLDMFKR 583
Cdd:TIGR00561 459 ISGIIIVGALLQIGQG-GGNLFIDALAFIAILIASINIFGGFRVTQRMLAMFRK 511
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
53-429 |
2.73e-131 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 402.46 E-value: 2.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDvKDVFSSDVLLKVRAPmlnpt 132
Cdd:COG3288 1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVD-AELLGADIVLKVRPP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 133 lGVHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANNFGRFFT 212
Cdd:COG3288 75 -SAEELAALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 213 GQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIkeSGEGQGGYAKEMSKEF 292
Cdd:COG3288 154 LMSTAAGTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAI--DANGAGGYAKELSEEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 293 IEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSVHKGVIHVGYTDI 372
Cdd:COG3288 232 KAKQAELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 47550793 373 PSRLPTQASTLYSNNITKLIRAISPDKetfyfdvknEFDFGTMDHVIRGSVVMQDGK 429
Cdd:COG3288 312 PSRLPAHASQLYAKNLLNFLELLVKDG---------ALALDLEDEIVAGTLLTHDGE 359
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
54-392 |
1.60e-66 |
|
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: 226.91 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 54 TVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDV--KDVFSSDVLLKVRAPMLNp 131
Cdd:cd01620 1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAasKEAYSADIIVKLKEPEFA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 132 tlgvhEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIaqgyDALSSMANIAGYKAVVLAANNFGRFF 211
Cdd:cd01620 80 -----EYDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR----PRLAPNSNIAGYAGVQLGAYELARIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 212 TGQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIKEsgegqggyakEMSKE 291
Cdd:cd01620 151 GGRMGGAGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKE----------ELEKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 292 FIEAemklfakqcldvDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIE----TTVPGELSVHKGVIHV 367
Cdd:cd01620 221 LKQT------------DILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDEtsipTTEGVPTYEVDGVVIY 288
|
330 340
....*....|....*....|....*....
gi 47550793 368 GYTDIPSRLPTQASTLYSNN----ITKLI 392
Cdd:cd01620 289 GVDNMPSLVPREASELLSKNllpyLVKLA 317
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
199-432 |
1.70e-61 |
|
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: 208.50 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 199 AVVLAANNFGRFFTGQITAAGKVP---PAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKS-LGAEPLEVdi 274
Cdd:pfam01262 1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 275 kesgegqggyakemskefIEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIET-- 352
Cdd:pfam01262 79 ------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVETsr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 353 -TVPGELSVHK-GVIHVGYTDIPSRLPTQASTLYSNNITKLIRAIspdKETFYFDVKNEfdfgtmDHVIRGSVVMQDGKV 430
Cdd:pfam01262 141 pTTHGEPVYVVdGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL---ADKGLKAALLE------DEALRAGLNTHDGKI 211
|
..
gi 47550793 431 LF 432
Cdd:pfam01262 212 TH 213
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
53-395 |
1.37e-58 |
|
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: 205.72 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATI-RDVKDVFS-SDVLLKVRAPMLn 130
Cdd:cd05305 1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIvPTAEEVWAkADLIVKVKEPLP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 131 ptlgvHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDqvprvTIAQGYDA---LSSMANIAGYKAVVLAANNF 207
Cdd:cd05305 80 -----EEYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYE-----TIEDEDGSlplLAPMSEIAGRLAVQIGAEYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 208 GRFFTGQ------ITAagkVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIkesgegq 281
Cdd:cd05305 150 EKPNGGRgvllggVPG---VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTTLY------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 282 ggyakeMSKEFIEAEMKlfakqclDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELS-- 359
Cdd:cd05305 220 ------SNPANLEEALK-------EADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRPTTHDnp 286
|
330 340 350
....*....|....*....|....*....|....*....
gi 47550793 360 ---VHkGVIHVGYTDIPSRLPTQASTLYSNNITKLIRAI 395
Cdd:cd05305 287 tyvVH-GVIHYCVPNMPGAVPRTSTLALTNATLPYLLKL 324
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
56-193 |
1.61e-54 |
|
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: 185.70 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 56 GVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFS-SDVLLKVRAPMLNptlg 134
Cdd:smart01003 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWAdADIILKVKEPSPE---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 47550793 135 vhEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTIAQGYDALSSMAN 193
Cdd:smart01003 77 --ELALLREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
56-195 |
1.62e-52 |
|
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: 179.93 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 56 GVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDV-KDVFS-SDVLLKVRAPMLnptl 133
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVDTaAEVWAeADLILKVKEPQP---- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47550793 134 gvHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRvTIAQGYDALSSMANIA 195
Cdd:pfam05222 77 --EEYALLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANIA 135
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
53-395 |
4.18e-51 |
|
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: 184.83 E-value: 4.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 53 LTVGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATI-RDVKDVFS-SDVLLKVRAPMLn 130
Cdd:COG0686 1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIvDTAEEVFAqADLIVKVKEPQP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 131 ptlgvHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQvprVTIAQG-YDALSSMANIAGYKAVVLAA----- 204
Cdd:COG0686 80 -----EEYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYET---VEDPDGsLPLLAPMSEIAGRMAIQIGAeylek 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 205 NNFGR--FFTGqitAAGkVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGAEPLEVDIkesgegqg 282
Cdd:COG0686 152 PNGGRgvLLGG---VPG-VPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGRVTTLY-------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 283 gyakeMSKEFIEaemklfaKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELS--- 359
Cdd:COG0686 220 -----SNPANIE-------EALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRPTTHDdpt 287
|
330 340 350
....*....|....*....|....*....|....*...
gi 47550793 360 --VHkGVIHVGYTDIPSRLPTQASTLYSNNITKLIRAI 395
Cdd:COG0686 288 yvVH-GVVHYCVANMPGAVPRTSTYALTNATLPYLLAL 324
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
204-368 |
3.06e-40 |
|
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: 145.34 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 204 ANNFGRFFTGQITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKS-LGAEPLEvdikesgegqg 282
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 283 gyakemskefIEAEMKLFAKQCLDVDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELS--- 359
Cdd:smart01002 70 ----------LYSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTTHDdpt 139
|
170
....*....|
gi 47550793 360 -VHKGVIHVG 368
Cdd:smart01002 140 yVVDGVVHYC 149
|
|
| PNTB_4TM |
pfam12769 |
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of ... |
498-583 |
6.30e-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: 136.43 E-value: 6.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 498 VTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLSLMGGGYlpSSTAETLAVLAAFISSVNIAGGFLVTQRM 577
Cdd:pfam12769 1 LTVFVLALFVGYEVIWKVPPALHTPLMSVTNAISGIIIVGALLAAGGGD--TTLATVLGFIAVVLATINVVGGFLVTDRM 78
|
....*.
gi 47550793 578 LDMFKR 583
Cdd:pfam12769 79 LDMFKK 84
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
55-388 |
5.59e-37 |
|
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: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 55 VGVPKEIFQNERRVAISPAGVEALIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDV-KDVFSSDVLLKVRAPMLNPTl 133
Cdd:cd12154 1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTLaKALWSLDVVLKVKEPLTNAE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 134 gvHEASLMSEGATLVSFIYPAQNPELMDTLSQRKATVLAMDQVPRVTiaqgydaLSSMANIAGYKAVVLAANNFGRFFTG 213
Cdd:cd12154 80 --YALIQKLGDRLLFTYTIGADHRDLTEALARAGLTAIAVEGVELPL-------LTSNSIGAGELSVQFIARFLEVQQPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 214 QITAAGKVPPAKVLIIGGGVAGLAAAGSARAMGAIVRGFDTRAAALEQFKSLGaeplevdikesgegqGGYAKEMSKEFI 293
Cdd:cd12154 151 RLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELG---------------GKNVEELEEALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 294 EAemklfakqcldvDIIITTALIPGRKAPVLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELSVHKGVIHVGYTDIP 373
Cdd:cd12154 216 EA------------DVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDVNMP 283
|
330 340
....*....|....*....|
gi 47550793 374 SRLPTQ-----ASTLYSNNI 388
Cdd:cd12154 284 GPGCAMgvpwdATLRLAANT 303
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
54-393 |
1.10e-19 |
|
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: 90.75 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 54 TVGVPKEIFQNERRVAISPAGVEAlIKQGFNVVVESGAGESAKFSDDMYTKAGATIRDVKDVFS-SDV--LLKVRAPMLN 130
Cdd:cd12181 2 TGGFGISNKENEKRVPLLPADLER-IPLREQLYFEEGYGERLGISDEEYAALGAGIVSREEILAkCDVicDPKPGDADYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 131 PtlgvheaslMSEGATLVSFIYPAQNPELMDTLSQRKATVLA---M---DQVPRVTIaqgYDAlssmANIAGYKAVVLAA 204
Cdd:cd12181 81 E---------ILEGQILWGWVHCVQDKEITQLAIDKKLTLIAwedMfewSKIGRHVF---YKN----NELAGYAAVLHAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 205 NNFGRFFTGQItaagkvppaKVLIIGGgvaglaaagsaramGAIVRGfdtraaALEQFKSLGAEpleVDIkesgegqggy 284
Cdd:cd12181 145 QLYGITPYRQT---------KVAVLGF--------------GNTARG------AIRALKLGGAD---VTV---------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 285 akemskeFIEAEMKLFAKQCLDVDIIITTALI-PGRKAPvLITKEMVETMKDGSVVVDLAAEAGGNIETTVPGELS---- 359
Cdd:cd12181 183 -------YTRRTEALFKEELSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFAKPTTFDdpiy 254
|
330 340 350
....*....|....*....|....*....|....
gi 47550793 360 VHKGVIHVGYTDIPSRLPTQASTLYSNNITKLIR 393
Cdd:cd12181 255 KVDGIDYYAVDHTPSLFYRSASRSISKALAPYLD 288
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
64-386 |
2.96e-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: 50.69 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 64 NERRVAISPAGVEALIKQGFNVVVEsgagESAK--FSDDMYTKAGATIRDVKDVfssdvllkVRAPMLNPTLGVHEasLM 141
Cdd:cd12188 12 LERRTALTPTTAKKLLDAGFKVTVE----RSPQriFPDEEYEAVGCELVPAGSW--------VNAPKDAIILGLKE--LP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 142 SEGATLV-SFIYPA----QNPELMDTLSQRKA---TVLAM-----DQVPRVTiAQGYdalssmanIAGYKAVVLAANNFG 208
Cdd:cd12188 78 EDTFPLPhRHIYFAhaykGQAGWKDVLSRFARgggTLLDLeylvdDDGRRVA-AFGY--------WAGFAGAALGLLAWA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 209 RFFTGQITAAGKVP--------------------PAKVLIIgggvaglaaagsaramGAIVRgfdTRAAALEQFKSLGAE 268
Cdd:cd12188 149 HQQLGPVTLPPVSPypneealvadvkkalatggrKPRALVI----------------GALGR---CGSGAVDLLEAAGIE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 269 PLEVDIKESGEGqGGYakemskefieaemklfaKQCLDVDIIITTALIPGrKAPVLITKEMVET-MKDGSVVVDLAAEAG 347
Cdd:cd12188 210 VTKWDMAETKAG-GPF-----------------PEILDHDIFVNCIYLSK-PIPPFLTPEMLQApGRRLRVIGDVSCDPT 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 47550793 348 G-------NIETTVPGE--LSVHKG--VIHVGYTD-IPSRLPTQASTLYSN 386
Cdd:cd12188 271 NpynpipiYDVATTFDKptLRVPTGgpPLDVIAIDhLPSLLPRESSEDFSN 321
|
|
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
65-127 |
9.62e-05 |
|
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: 46.01 E-value: 9.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47550793 65 ERRVAISPAGVEALIKQ-GFNVVVESgageSAK--FSDDMYTKAGATIRDvkDVFSSDVLLKVRAP 127
Cdd:cd12189 13 ERRAPLTPSHVRELVKKpGVKVLVQP----SNRraFPDQEYEAAGAIIQE--DLSDADLILGVKEP 72
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|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
54-354 |
2.61e-04 |
|
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: 44.53 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 54 TVGVPKE--IFQnERRVAISPAGVEALIKQGFNV--VVESGAGESakFSDDMYTKAGATIrdVKDVFSSDVLLKVRApml 129
Cdd:cd05199 1 KIGIIREgkTPP-DRRVPLTPEQCKELQAKYPGVeiFVQPSPVRC--FKDEEYRAAGIEV--VEDLSDCDILLGVKE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 130 nptlgVHEASLMSEGATL-VSFIYPAQ--NPELMDTLSQRKAT-----VLAMDQVPRVtIAQGYdalssMANIAG-YKAV 200
Cdd:cd05199 73 -----VPIEQLIPNKTYFfFSHTIKKQpyNRKLLQTILEKNITlidyeVLVDEQGKRV-IAFGR-----YAGIVGaYNGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 201 VLAANNFGRF----------FTGQITAAGKV--PPAKVLIIGGgvaglaaagsaramGAIVRGfdtraaALEQFKSLGAE 268
Cdd:cd05199 142 RAYGKKTGLFdlkrahecsdLEELIAELKKVglPPPKIVITGS--------------GRVGSG------AAEVLKALGIK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550793 269 PLEVDIKEsgegqgGYAkemskefieaemklfakqcldvDIIITTALIpGRKAPVLITKEMVeTMKDG--SVVVDLAAEA 346
Cdd:cd05199 202 EVSPEDFL------TVA----------------------DILINGHYW-DKRAPRLFTKEDL-KKPDFkiRVIADVTCDI 251
|
....*...
gi 47550793 347 GGNIETTV 354
Cdd:cd05199 252 HGSIPSTL 259
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