|
Name |
Accession |
Description |
Interval |
E-value |
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1-483 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 792.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 1 MGDPRGFIKHGRRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQAL 80
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 81 TALHATNNFPEFTGRVCPAPCETSCVLGINEPPVTIKLHEVSIVDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQ 160
Cdd:PRK12810 81 ERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 161 QLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEE 240
Cdd:PRK12810 161 QLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 241 PRDLPVEGRELKGIHFAMEFLPQQNRACWGDhniaalhPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNFEL 320
Cdd:PRK12810 241 PRDLGIPGRDLDGVHFAMDFLIQNTRRVLGD-------ETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 321 LEHPPAERSPNNPWPQWSRIMRVSTSVEEmhvlGGDVYYEIMTTRFIGRDKNVTGLETVKVKWKDGRPEKIPGSEQIWKC 400
Cdd:PRK12810 314 MPMPPSRRNKNNPWPYWPMKLEVSNAHEE----GVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGSEFVLPA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 401 DLVLLAMGFLGPRSELIKQAGCKTDQRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYLTGtES 480
Cdd:PRK12810 390 DLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG-ST 468
|
...
gi 1224321637 481 QLP 483
Cdd:PRK12810 469 ALP 471
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
3-483 |
0e+00 |
|
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.
Pssm-ID: 162300 [Multi-domain] Cd Length: 485 Bit Score: 691.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 3 DPRGFIKHGRRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVPFCM--TGCPLGNLIPEWNDLVYRGQWKQAL 80
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHndSGCPLNNLIPEFNDLVFRGRWKEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 81 TALHATNNFPEFTGRVCPAPCETSCVLGINEPPVTIKLHEVSIVDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQ 160
Cdd:TIGR01317 81 DRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 161 QLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEE 240
Cdd:TIGR01317 161 QLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 241 PRDLPVEGRELKGIHFAMEFLPQQNRACWGDhNIAALHPrqrlINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNFEL 320
Cdd:TIGR01317 241 PRDLPIPGRELKGIHYAMEFLPSATKALLGK-DFKDIIF----IKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 321 LEHPPAERSPNNPWPQWSRIMRVSTSVEEMHVLGGDV--YYEIMTTRFIGRDK-NVTGLETVKVKWK---DGR--PEKIP 392
Cdd:TIGR01317 316 MPKPPEARAKDNPWPEWPRVYRVDYAHEEAAAHYGRDprEYSILTKEFIGDDEgKVTALRTVRVEWKksqDGKwqFVEIP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 393 GSEQIWKCDLVLLAMGFLGPRSELIKQAGCKTDQRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVD 472
Cdd:TIGR01317 396 GSEEVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVD 475
|
490
....*....|.
gi 1224321637 473 EYLTGtESQLP 483
Cdd:TIGR01317 476 RYLMG-SSVLP 485
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
23-474 |
0e+00 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 623.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 23 RLQNFDEHYNYPSEEKVKTQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCPAPCE 102
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPAPCE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 103 TSCVLGINEPPVTIKLHEVSIVDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLL 182
Cdd:COG0493 81 GACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 183 MYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLP 262
Cdd:COG0493 161 RYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 263 QQNRACWGDhniaalhprqrLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNFELLehpPAERSPNNPWpqwsrimR 342
Cdd:COG0493 241 AVNLGEAPD-----------TILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRR---TREEMPASKE-------E 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 343 VSTSVEEmhvlGGDVYYEIMTTRFIGRDK-NVTGLETVKVKW----KDGR--PEKIPGSEQIWKCDLVLLAMGFLGPRSE 415
Cdd:COG0493 300 VEEALEE----GVEFLFLVAPVEIIGDENgRVTGLECVRMELgepdESGRrrPVPIEGSEFTLPADLVILAIGQTPDPSG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1224321637 416 LIKQAGCKTDQRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEY 474
Cdd:COG0493 376 LEEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
5-480 |
4.13e-155 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 448.86 E-value: 4.13e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 5 RGFIKHGRRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALH 84
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 85 ATNNFPEFTGRVCPAP--CETSCVLGINEPPVTIKLHEVSIVDKGFEEGWIRPQPPEqRTGKSVAIIGGGPAGLACAQQL 162
Cdd:PRK11749 81 ETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAP-KTGKKVAVIGAGPAGLTAAHRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 163 NRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPR 242
Cdd:PRK11749 160 ARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 243 DLPVEGRELKGIHFAMEFLPQQNRACWGDHNIaalhprqrlinaKGKKVIVIGGGDTGSDCIGTSMRQGATSV--FNFEL 320
Cdd:PRK11749 240 FLGIPGENLGGVYSAVDFLTRVNQAVADYDLP------------VGKRVVVIGGGNTAMDAARTAKRLGAESVtiVYRRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 321 LEHPPAerspnnpwpqwsrimrvstSVEEMH---VLGGDVYYEIMTTRFIGRDKNVTGLETVKVKWKDG-----RPEKIP 392
Cdd:PRK11749 308 REEMPA-------------------SEEEVEhakEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELGEPdasgrRRVPIE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 393 GSEQIWKCDLVLLAMGFLGPRSELIKQAGCKTDQRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVD 472
Cdd:PRK11749 369 GSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIH 448
|
....*...
gi 1224321637 473 EYLTGTES 480
Cdd:PRK11749 449 EYLEGAAS 456
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
52-479 |
2.98e-88 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 280.99 E-value: 2.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 52 PFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCPAPCETSCVLGINEPPVTIKLHEVSIVDKGFEEG 131
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAIANG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 132 WiRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFR 211
Cdd:PRK12771 127 W-KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 212 YSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLpqqnracwgdHNIAALHPrqrliNAKGKKV 291
Cdd:PRK12771 206 LGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL----------RAVGEGEP-----PFLGKRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 292 IVIGGGDTGSDCIGTSMRQGATSVFnfeLLEHPPAERSPNNPwpqwsrimrvsTSVEEMHVLGGDVYYEIMTTRFIGRDK 371
Cdd:PRK12771 271 VVIGGGNTAMDAARTARRLGAEEVT---IVYRRTREDMPAHD-----------EEIEEALREGVEINWLRTPVEIEGDEN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 372 NVTGLETVKV----KWKDGRPEKIPGSEQIWKCDLVLLAMGfLGPRSELIKQAGCKTDQRSNVVTDPKTRMSTVDGVFAA 447
Cdd:PRK12771 337 GATGLRVITVekmeLDEDGRPSPVTGEEETLEADLVVLAIG-QDIDSAGLESVPGVEVGRGVVQVDPNFMMTGRPGVFAG 415
|
410 420 430
....*....|....*....|....*....|..
gi 1224321637 448 GDCRRGQSLVVWAISEGREIARCVDEYLTGTE 479
Cdd:PRK12771 416 GDMVPGPRTVTTAIGHGKKAARNIDAFLGGEP 447
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
18-477 |
2.01e-81 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 260.34 E-value: 2.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 18 QPVNSRLQNFDE-HYNYPSEEKVKtQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRV 96
Cdd:PRK12831 14 QDPEVRATNFEEvCLGYNEEEAVK-EASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 97 CP--APCETSCVLGINEPPVTIKLHEVSIVDKGFEEGwIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEK 174
Cdd:PRK12831 93 CPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 175 SDRAGGLLMYGIPHYKLWKQR-VQRRIDLLVAEGIEFRYSCEVGKDATFDEI--KSSFDAVVLATGAEEPRDLPVEGREL 251
Cdd:PRK12831 172 LHEPGGVLVYGIPEFRLPKETvVKKEIENIKKLGVKIETNVVVGKTVTIDELleEEGFDAVFIGSGAGLPKFMGIPGENL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 252 KGIHFAMEFLPQQNRacwgdhnIAALHPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNFELLEHP-PAersp 330
Cdd:PRK12831 252 NGVFSANEFLTRVNL-------MKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEElPA---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 331 nnpwpqwsRIMRVSTSVEEmhvlggDVYYEIMT--TRFIGRDK-NVTGLETVKVKWKD----GR--PEKIPGSEQIWKCD 401
Cdd:PRK12831 321 --------RVEEVHHAKEE------GVIFDLLTnpVEILGDENgWVKGMKCIKMELGEpdasGRrrPVEIEGSEFVLEVD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224321637 402 LVLLAMGfLGPrSELIKQA--GCKTDQRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYLTG 477
Cdd:PRK12831 387 TVIMSLG-TSP-NPLISSTtkGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSK 462
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
12-475 |
5.86e-78 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 256.60 E-value: 5.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 12 RRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGV-PFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFP 90
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 91 EFTGRVCPAP--CETSCVLGINEPPVTIKLHEVSIVDKGFEEGWiRPQPPE-QRTGKSVAIIGGGPAGLACAQQLNRAGH 167
Cdd:PRK12769 273 EITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGW-RPDLSQvTKSDKRVAIIGAGPAGLACADVLARNGV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 168 KVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVE 247
Cdd:PRK12769 352 AVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLP 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 248 GRELKGIHFAMEFLPQQNRACWGdhnIAALhPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVfnfellehPPAE 327
Cdd:PRK12769 432 NEDAPGVYDALPFLIANTKQVMG---LEEL-PEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNV--------TCAY 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 328 RSPNNPWPQWSRimRVSTSVEEmhvlGGDVYYEIMTTRF-IGRDKNVTGLETVKVKW--KDG----RPEKIPGSEQIWKC 400
Cdd:PRK12769 500 RRDEANMPGSKK--EVKNAREE----GANFEFNVQPVALeLNEQGHVCGIRFLRTRLgePDAqgrrRPVPIPGSEFVMPA 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224321637 401 DLVLLAMGFLGPRSELIKQAGCKTDQRSNVVTDPKTRM---STVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYL 475
Cdd:PRK12769 574 DAVIMAFGFNPHGMPWLESHGVTVDKWGRIIADVESQYryqTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
19-475 |
3.92e-76 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 245.94 E-value: 3.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 19 PVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVPF--CMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRV 96
Cdd:TIGR01316 1 PPEERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 97 CPAP--CETSCVLGINEP----PVTIKLHEVSIVDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVT 170
Cdd:TIGR01316 81 CPQErqCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 171 VIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVEGRE 250
Cdd:TIGR01316 161 VFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 251 LKGIHFAMEFLPQQNRAcwgdhnIAALHPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNFELLEHPPAERSp 330
Cdd:TIGR01316 241 LCGVYSANDFLTRANLM------KAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAEVHCLYRRTREDMTARV- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 331 nnpwPQWSRIMrvstsvEEmhvlGGDVYYEIMTTRFIGRDK-NVTGLETVKVKWKD----GRPEKIP--GSEQIWKCDLV 403
Cdd:TIGR01316 314 ----EEIAHAE------EE----GVKFHFLCQPVEIIGDEEgNVRAVKFRKMDCQEqidsGERRFLPcgDAECKLEADAV 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224321637 404 LLAMGfLGPRSELIKQAGCKTDQRSNVVTDpKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYL 475
Cdd:TIGR01316 380 IVAIG-NGSNPIMAETTRLKTSERGTIVVD-EDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
46-485 |
6.99e-73 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 243.10 E-value: 6.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 46 CMDCGVPfCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCPAPCETSCVL-GINEPpvtiklheVSI- 123
Cdd:PRK12814 97 CGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRhGVDEP--------VSIc 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 124 ------VDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQ 197
Cdd:PRK12814 168 alkryaADRDMESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVID 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 198 RRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLpqqnracwgdHNIA-- 275
Cdd:PRK12814 248 ADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL----------RNVAlg 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 276 -ALHPrqrlinakGKKVIVIGGGDTGSDCIGTSMRQGATSVfnfELLEHPPAERSPNNPwpqwSRIMRVSTSVEEMHVLG 354
Cdd:PRK12814 318 tALHP--------GKKVVVIGGGNTAIDAARTALRLGAESV---TILYRRTREEMPANR----AEIEEALAEGVSLRELA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 355 GDVYyeimttrfIGRDKNvtGLETVKVKWKDG--------RPEKIPGSEQIWKCDLVLLAMG-FLGPrsELIKQAGCKTD 425
Cdd:PRK12814 383 APVS--------IERSEG--GLELTAIKMQQGepdesgrrRPVPVEGSEFTLQADTVISAIGqQVDP--PIAEAAGIGTS 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 426 QRSNVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYLTGTESQLPKV 485
Cdd:PRK12814 451 RNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAPVQ 510
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
15-477 |
1.22e-70 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 238.87 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 15 KTLQPVNSRLQNFDE-HYNYPSEEKVkTQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFT 93
Cdd:PRK12778 300 PELDPEYRAHNRFEEvNLGLTKEQAM-TEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 94 GRVCP--APCETSCVLGI-NEPPVTIKLHEVSIVDKGFEEGWIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVT 170
Cdd:PRK12778 379 GRVCPqeKQCESKCIHGKmGEEAVAIGYLERFVADYERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 171 VIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKS-SFDAVVLATGAEEPRDLPVEGR 249
Cdd:PRK12778 459 VFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEeGFKGIFIASGAGLPNFMNIPGE 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 250 ELKGIHFAMEFLPQQNRacwgdhnIAALHPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFnfeLLEHPPAERS 329
Cdd:PRK12778 539 NSNGVMSSNEYLTRVNL-------MDAASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVT---IVYRRSEEEM 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 330 PnnpwpqwSRIMRVSTSVEEMhvlggdvyYEIMT----TRFIGRDKN-VTGLETVKVKWKD----GR--PEKIPGSEQIW 398
Cdd:PRK12778 609 P-------ARLEEVKHAKEEG--------IEFLTlhnpIEYLADEKGwVKQVVLQKMELGEpdasGRrrPVAIPGSTFTV 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 399 KCDLVLLAMGF----LGPRSelIKqaGCKTDQRSNVVTDPKTrMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEY 474
Cdd:PRK12778 674 DVDLVIVSVGVspnpLVPSS--IP--GLELNRKGTIVVDEEM-QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEY 748
|
...
gi 1224321637 475 LTG 477
Cdd:PRK12778 749 LSS 751
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
11-469 |
7.35e-68 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 229.14 E-value: 7.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 11 GRRDKTLQPVNSRL-----------QNFDEHYNYPSEEKVKTQAARCMDCG-VPFCMTGCPLGNLIPEWNDLVYRGQWKQ 78
Cdd:PRK12809 164 PSRSAALLPVNSRKgadkisaserkTHFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 79 ALTALHATNNFPEFTGRVCPAP--CETSCVLGINEPPVTIKLHEVSIVDKGFEEGWiRPQ-----PPEQRtgksVAIIGG 151
Cdd:PRK12809 244 AAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGW-RPDvskvvPRSEK----VAVIGA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 152 GPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDA 231
Cdd:PRK12809 319 GPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDA 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 232 VVLATGAEEPRDLPVEGRELKGIHFAMEFLPQQNRACWGDHNiAALHPrqrLINAKGKKVIVIGGGDTGSDCIGTSMRQG 311
Cdd:PRK12809 399 VFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGLPE-SEEYP---LTDVEGKRVVVLGGGDTTMDCLRTSIRLN 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 312 ATSV---FNFELLEHPPAERspnnpwpqwsrimRVSTSVEEmhvlggDVYYEI-MTTRFIGRDKN--VTGLETVKVKW-- 383
Cdd:PRK12809 475 AASVtcaYRRDEVSMPGSRK-------------EVVNAREE------GVEFQFnVQPQYIACDEDgrLTAVGLIRTAMge 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 384 --KDG--RPEKIPGSEQIWKCDLVLLAMGFLGPRSELIKQAGCKTDQRSNVVTDPKTRMST---VDGVFAAGDCRRGQSL 456
Cdd:PRK12809 536 pgPDGrrRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLPTqthLKKVFAGGDAVHGADL 615
|
490
....*....|...
gi 1224321637 457 VVWAISEGREIAR 469
Cdd:PRK12809 616 VVTAMAAGRQAAR 628
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
132-478 |
4.47e-51 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 177.49 E-value: 4.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 132 WIRPQPPEqRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFR 211
Cdd:PRK12770 8 FMCKEKPP-PTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 212 YSCEV---------------GKDATFDEIKSSFDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLpqqnracwgdHNIAA 276
Cdd:PRK12770 87 TRTKVccgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYL----------FRIRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 277 LH----PRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATSVFNF--ELLEHPPAERspnnpwpqwsrimrvsTSVEEM 350
Cdd:PRK12770 157 AKlgylPWEKVPPVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAyrRTINEAPAGK----------------YEIERL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 351 HVLGGDVYYEIMTTRFIGRDKnVTGLETVKVKWKDG------RPEKIPGSEQIWKCDLVLLAMGFLgPRSELIKQA-GCK 423
Cdd:PRK12770 221 IARGVEFLELVTPVRIIGEGR-VEGVELAKMRLGEPdesgrpRPVPIPGSEFVLEADTVVFAIGEI-PTPPFAKEClGIE 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1224321637 424 TDQRSNVVTDPKtRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYLTGT 478
Cdd:PRK12770 299 LNRKGEIVVDEK-HMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
23-476 |
1.44e-50 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 185.53 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 23 RLQNFDE-HYNYPSEEKVKtQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCP--A 99
Cdd:PRK12775 310 RARNFKEvNLGYSLEDALQ-EAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPqeT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 100 PCETSCVLGINEPPVTIKLHEVSIVDKGFEEGwIRPQPPEQRTGKsVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:PRK12775 389 QCEAQCIIAKKHESVGIGRLERFVGDNARAKP-VKPPRFSKKLGK-VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 180 GLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEI--KSSFDAVVLATGAEEPRDLPVEGRELKGIHFA 257
Cdd:PRK12775 467 GVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLmnDKGFDAVFLGVGAGAPTFLGIPGEFAGQVYSA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 258 MEFLPQQNrACWGDHniaalHPRQRLINAKGKKVIVIGGGDTGSDCIGTSMRQGATS---VFNFELLEHPpaerspnnpw 334
Cdd:PRK12775 547 NEFLTRVN-LMGGDK-----FPFLDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTvrcVYRRSEAEAP---------- 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 335 pqwSRIMRVSTSVEEmhvlGGDVYY-----EIMTTrfigRDKNVTGLETVKVKWKD----GRPEKIPGSEQI-WKCDLVL 404
Cdd:PRK12775 611 ---ARIEEIRHAKEE----GIDFFFlhspvEIYVD----AEGSVRGMKVEEMELGEpdekGRRKPMPTGEFKdLECDTVI 679
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224321637 405 LAMGflGPRSELIKQA--GCKTDQRSNVVTD----PKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIARCVDEYLT 476
Cdd:PRK12775 680 YALG--TKANPIITQStpGLALNKWGNIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
12-477 |
8.72e-48 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 174.18 E-value: 8.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 12 RRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVpfCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPE 91
Cdd:PRK13984 153 RVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI--CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 92 FTGRVCPAPCETSCVLGINEPPVTIKLHEVSIVDKGFEEGW--IRPQPPEQRtGKSVAIIGGGPAGLACAQQLNRAGHKV 169
Cdd:PRK13984 231 VCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYseILDDEPEKK-NKKVAIVGSGPAGLSAAYFLATMGYEV 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 170 TVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDATFDEIKSSFDAVVLATGAEEPRDLPVEGR 249
Cdd:PRK13984 310 TVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 250 ELKGIHFAMEFLPQQNRACWGDhniaalHPRQRLinakGKKVIVIGGGDTGSDcIGTSMRQ------GATSVFNFEL--- 320
Cdd:PRK13984 390 DHPDVIQALPLLREIRDYLRGE------GPKPKI----PRSLVVIGGGNVAMD-IARSMARlqkmeyGEVNVKVTSLert 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 321 LEHPPAERSpnnpwpqwsrimRVSTSVEEmhvlGGDVYYEIMTTRFIGRDKNVTGLETVK---VKWKDGR--PEKIPGSE 395
Cdd:PRK13984 459 FEEMPADME------------EIEEGLEE----GVVIYPGWGPMEVVIENDKVKGVKFKKcveVFDEEGRfnPKFDESDQ 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 396 QIWKCDLVLLAMGFLGPRSELIKQAGCKTD-QRSNVVTDpKTRMSTVDGVFAAGDCRRGQSlVVWAISEGREIARCVDEY 474
Cdd:PRK13984 523 IIVEADMVVEAIGQAPDYSYLPEELKSKLEfVRGRILTN-EYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMY 600
|
...
gi 1224321637 475 LTG 477
Cdd:PRK13984 601 LRK 603
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
57-469 |
2.20e-40 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 155.38 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 57 GCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCPAPCETSCVLGINEPPVTI-----------KLHEVSIVD 125
Cdd:PRK12779 213 GCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKRPIEIgqlewylpqheKLVNPNANE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 126 KgFEEgwiRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDLLVA 205
Cdd:PRK12779 293 R-FAG---RISPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 206 EGIEFRYSCEVGKDATFDEIKSS-FDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLPQQNRacwgdhnIAALHPRQR-- 282
Cdd:PRK12779 369 LGGRFVKNFVVGKTATLEDLKAAgFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNL-------MRGLDDDYEtp 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 283 LINAKGKKVIVIGGGDTGSDCIGTSMRQGA--TSVFNFELLEHPpaerspnnpwpqwsrimrvsTSVEEMH--VLGGDVY 358
Cdd:PRK12779 442 LPEVKGKEVFVIGGGNTAMDAARTAKRLGGnvTIVYRRTKSEMP--------------------ARVEELHhaLEEGINL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 359 YEIMTTR-FIGRDKN------VTGLETVKVKWKDGRPEKIP-GSEQIWKCDLVLLAMGflGPRSELIKQA--GCKTDQRS 428
Cdd:PRK12779 502 AVLRAPReFIGDDHThfvthaLLDVNELGEPDKSGRRSPKPtGEIERVPVDLVIMALG--NTANPIMKDAepGLKTNKWG 579
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1224321637 429 NVVTDPKTRMSTVDGVFAAGDCRRGQSLVVWAISEGREIAR 469
Cdd:PRK12779 580 TIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAK 620
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
144-464 |
5.05e-34 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 130.13 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEksdRAGGLLMYGIPHYK-------------LWKQRVQRR--IDLLVAEGI 208
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKallgaaeapeiasLWADLYKRKeeVVKKLNNGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 209 EFRYSCEV------------GKDATFDEIKSSFDAVVLATGAeEPRDLPVEGRELKGIHFameflpqqnracwgdhnIAA 276
Cdd:pfam07992 78 EVLLGTEVvsidpgakkvvlEELVDGDGETITYDRLVIATGA-RPRLPPIPGVELNVGFL-----------------VRT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 277 LHPRQRLINA-KGKKVIVIGGGDTGSDCIGTSMRQGAtsvfNFELLEHppAERSPNNPWPQWSRIMRvstsvEEMHVLGG 355
Cdd:pfam07992 140 LDSAEALRLKlLPKRVVVVGGGYIGVELAAALAKLGK----EVTLIEA--LDRLLRAFDEEISAALE-----KALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 356 DVYYEIMTTRFIGRDknvtglETVKVKWKDGRpekipgseqIWKCDLVLLAMGFlGPRSELIKQAGCKTDQRSNVVTDPK 435
Cdd:pfam07992 209 EVRLGTSVKEIIGDG------DGVEVILKDGT---------EIDADLVVVAIGR-RPNTELLEAAGLELDERGGIVVDEY 272
|
330 340 350
....*....|....*....|....*....|
gi 1224321637 436 TRmSTVDGVFAAGDCRRGQ-SLVVWAISEG 464
Cdd:pfam07992 273 LR-TSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
146-475 |
6.66e-31 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 121.38 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKsDRAGGLLM--------YGIPH----YKLwkqrVQRRIDLLVAEGIEFRYs 213
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEgisgPEL----AERLREQAERFGAEILL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 214 CEV----GKDATF-------DEIKSsfDAVVLATGAEePRDLPVEGREL---KGIHfameflpqqnrACwgdhniAALHP 279
Cdd:COG0492 77 EEVtsvdKDDGPFrvttddgTEYEA--KAVIIATGAG-PRKLGLPGEEEfegRGVS-----------YC------ATCDG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 280 RQrlinAKGKKVIVIGGGDTGSDcIGTSMRQGATSVFnfelLEHPPAErspnnpwPQWSRIMrvstsVEEMHVLGG-DVY 358
Cdd:COG0492 137 FF----FRGKDVVVVGGGDSALE-EALYLTKFASKVT----LIHRRDE-------LRASKIL-----VERLRANPKiEVL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 359 YEIMTTRFIGRDKnVTGLETVKVKwkdgrpekiPGSEQIWKCDLVLLAMGFLgPRSELIKQAGCKTDQRSNVVTDPKTRM 438
Cdd:COG0492 196 WNTEVTEIEGDGR-VEGVTLKNVK---------TGEEKELEVDGVFVAIGLK-PNTELLKGLGLELDEDGYIVVDEDMET 264
|
330 340 350
....*....|....*....|....*....|....*...
gi 1224321637 439 StVDGVFAAGDCRRGQS-LVVWAISEGREIARCVDEYL 475
Cdd:COG0492 265 S-VPGVFAAGDVRDYKYrQAATAAGEGAIAALSAARYL 301
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
23-132 |
7.33e-30 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 112.63 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 23 RLQNFDEHYNYPSEEKVKTQAARCMDCGVPFCMTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTGRVCPA--P 100
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQ 80
|
90 100 110
....*....|....*....|....*....|....
gi 1224321637 101 CETSCVLGINEP-PVTI-KLhEVSIVDKGFEEGW 132
Cdd:pfam14691 81 CEGACVLGKKGFePVAIgRL-ERFAADWARENGI 113
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
168-450 |
1.75e-24 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 103.74 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 168 KVTVIEKSDRAGGLLmYGIPHYklWKQRVQRRIDLLV-------AEGIEFRYSCEVgkdATFD------EIKS----SFD 230
Cdd:COG0446 7 EITVIEKGPHHSYQP-CGLPYY--VGGGIKDPEDLLVrtpesfeRKGIDVRTGTEV---TAIDpeaktvTLRDgetlSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 231 AVVLATGAEePRDLPVEGRELKGIHFAmeflpqqnracwgdHNIA-ALHPRQRLINAKGKKVIVIGGGdtgsdCIGTSM- 308
Cdd:COG0446 81 KLVLATGAR-PRPPPIPGLDLPGVFTL--------------RTLDdADALREALKEFKGKRAVVIGGG-----PIGLELa 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 309 ----RQGAtsvfNFELLEHPPAerspnnPWPQWSRIMrvSTSVEEMHVLGG-DVYYEIMTTRFIGRDKnvtgletVKVKW 383
Cdd:COG0446 141 ealrKRGL----KVTLVERAPR------LLGVLDPEM--AALLEEELREHGvELRLGETVVAIDGDDK-------VAVTL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224321637 384 KDGrpEKIPgseqiwkCDLVLLAMGFlGPRSELIKQAGCKTDQRSNVVTDPKTRMStVDGVFAAGDC 450
Cdd:COG0446 202 TDG--EEIP-------ADLVVVAPGV-RPNTELAKDAGLALGERGWIKVDETLQTS-DPDVYAAGDC 257
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
144-491 |
8.31e-21 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 94.05 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGH--KVTVIekSDRAGG-----LLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEV 216
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPdgEITVI--GAEPHPpynrpPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 217 ------GKDATFDEIKS-SFDAVVLATGAEePRDLPVEGRELKGIHfameflpqqnrACWgdhNIA-ALHPRQRLinAKG 288
Cdd:COG1251 80 taidraARTVTLADGETlPYDKLVLATGSR-PRVPPIPGADLPGVF-----------TLR---TLDdADALRAAL--APG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 289 KKVIVIGGGDTGSDcIGTSMRQGATSVfnfELLEhpPAERspnnPWPQW-----SRIMRvsTSVEEMHVlggDVYYEIMT 363
Cdd:COG1251 143 KRVVVIGGGLIGLE-AAAALRKRGLEV---TVVE--RAPR----LLPRQldeeaGALLQ--RLLEALGV---EVRLGTGV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 364 TRFIGRDKnVTGLETvkvkwKDGrpEKIPgseqiwkCDLVLLAMGfLGPRSELIKQAGCKTDQRsnVVTDPktRMST-VD 442
Cdd:COG1251 208 TEIEGDDR-VTGVRL-----ADG--EELP-------ADLVVVAIG-VRPNTELARAAGLAVDRG--IVVDD--YLRTsDP 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 443 GVFAAGDC------RRGQSLVV-WAIseGREIARCVDEYLTGTESQ----LPKVRLEFFD 491
Cdd:COG1251 268 DIYAAGDCaehpgpVYGRRVLElVAP--AYEQARVAAANLAGGPAAyegsVPSTKLKVFG 325
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
146-465 |
3.09e-17 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 83.98 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKsDRAGG------------LL-------------MYGIPHYKL--------- 191
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskaLLhaaevahearhaaEFGISAGAPsvdwaalma 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 192 WKQRVQRRI-----DLLVAEGIEF---------RYSCEVGKDATFdeiksSFDAVVLATGAEePRDLPVEGRELKGIH-- 255
Cdd:COG1249 85 RKDKVVDRLrggveELLKKNGVDVirgrarfvdPHTVEVTGGETL-----TADHIVIATGSR-PRVPPIPGLDEVRVLts 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 256 ---FAMEFLPqqnracwgdhniaalhprqrlinakgKKVIVIGGGDTGsdC-IGTSMRQ-GA-TSVFnfellehppaERS 329
Cdd:COG1249 159 deaLELEELP--------------------------KSLVVIGGGYIG--LeFAQIFARlGSeVTLV----------ERG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 330 PnnpwpqwsRIMR-----VSTSVEE-MHVLGGDVYYEIMTTRFIGRDKNVTgletvkVKWKDGrpekipGSEQIWKCDLV 403
Cdd:COG1249 201 D--------RLLPgedpeISEALEKaLEKEGIDILTGAKVTSVEKTGDGVT------VTLEDG------GGEEAVEADKV 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224321637 404 LLAMGFlGPRSELI--KQAGCKTDQRSNVVTDPKTRmSTVDGVFAAGDCRRGQSLVVWAISEGR 465
Cdd:COG1249 261 LVATGR-RPNTDGLglEAAGVELDERGGIKVDEYLR-TSVPGIYAIGDVTGGPQLAHVASAEGR 322
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
146-475 |
9.36e-17 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 80.75 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLM------Y-----GIPHYKLwkqrVQRRIDLLVAEGIEFRYSc 214
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTttevenYpgfpeGISGPEL----MEKMKEQAVKFGAEIIYE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 215 EVGKDATFDEIKSSF---------DAVVLATGAEePRDLPVEGRElkgihfamEFLpqqnracwgdhniaalhprQRLIN 285
Cdd:TIGR01292 77 EVIKVDKSDRPFKVYtgdgkeytaKAVIIATGAS-ARKLGIPGED--------EFW-------------------GRGVS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 286 A---------KGKKVIVIGGGDT-----------GSDCIGTSMRQG--ATSVfnfeLLEHppAERSPNNPWpQWSRImrv 343
Cdd:TIGR01292 129 YcatcdgpffKNKEVAVVGGGDSaieealyltriAKKVTLVHRRDKfrAEKI----LLDR--LKKNPKIEF-LWNST--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 344 stsVEEMHvlgGDvyyeimttrfigrdknvTGLETVKVKwkdgrpEKIPGSEQIWKCDLVLLAMGFLgPRSELIKQAgCK 423
Cdd:TIGR01292 199 ---VEEIV---GD-----------------NKVEGVKIK------NTVTGEEEELEVDGVFIAIGHE-PNTELLKGL-LE 247
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1224321637 424 TDQRSNVVTDPKTRMStVDGVFAAGDCR-RGQSLVVWAISEGREIARCVDEYL 475
Cdd:TIGR01292 248 LDENGYIVTDEGMRTS-VPGVFAAGDVRdKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
145-303 |
2.86e-14 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 74.73 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 145 SVAIIGGGPAGLACAQQLNRA--GHKVTVIEKSDRAGGLLMYGI-PHYKLWKQRVQRRIDLLVAEGIEFRYSCEVGKDAT 221
Cdd:PLN02852 28 HVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 222 FDEIKSSFDAVVLATGAEEPRDLPVEGRELKGIHFAMEFLPQQNRacwgdhniaalHPRQRLINA---KGKKVIVIGGGD 298
Cdd:PLN02852 108 LSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNG-----------HPDCVHLPPdlkSSDTAVVLGQGN 176
|
....*
gi 1224321637 299 TGSDC 303
Cdd:PLN02852 177 VALDC 181
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
146-304 |
8.01e-13 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 69.89 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG---------------LLMYGIPHYKLWK---------------QR 195
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNWSddpdfptgdeilaylEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 196 VQRRIDLlvAEGIEFRysCEVgKDATFDEIKS------------SFDAVVLATGA-EEPRDLPVEGRElkgihfameflp 262
Cdd:COG2072 89 YADKFGL--RRPIRFG--TEV-TSARWDEADGrwtvttddgetlTARFVVVATGPlSRPKIPDIPGLE------------ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1224321637 263 qqnracwgDHNIAALHPrQRLINA---KGKKVIVIGGGDTGSDCI 304
Cdd:COG2072 152 --------DFAGEQLHS-ADWRNPvdlAGKRVLVVGTGASAVQIA 187
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
144-182 |
8.74e-13 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 70.25 E-value: 8.74e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLL 182
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
144-180 |
2.08e-12 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 67.98 E-value: 2.08e-12
10 20 30
....*....|....*....|....*....|....*..
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
141-180 |
4.21e-12 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 68.02 E-value: 4.21e-12
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1224321637 141 RTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
146-450 |
1.06e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 66.31 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNR---AGHKVTVIEKSDRA--GGLLmYGIP--HYKLWKQRVQRRiDLLVAEGIEFRYScEV-- 216
Cdd:COG1252 4 IVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHlfQPLL-PEVAagTLSPDDIAIPLR-ELLRRAGVRFIQG-EVtg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 217 ----GKDATFDEIKS-SFDAVVLATGAEePRDLPVEG-RE----LKGIHFAMEFlpqqnracwgdhniaalhpRQRLINA 286
Cdd:COG1252 81 idpeARTVTLADGRTlSYDYLVIATGSV-TNFFGIPGlAEhalpLKTLEDALAL-------------------RERLLAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 287 -------KGKKVIVIGGGDTG------------SDCIGTSMRQGATSVFNFELLEHPPAERSPnnpwpqwsrimRVSTSV 347
Cdd:COG1252 141 feraerrRLLTIVVVGGGPTGvelagelaellrKLLRYPGIDPDKVRITLVEAGPRILPGLGE-----------KLSEAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 348 ----EEMHVlggdvyyEIMTtrfigrDKNVTGLETVKVKWKDGrpEKIPgseqiwkCDLVLLAMGFLGPrsELIKQAGCK 423
Cdd:COG1252 210 ekelEKRGV-------EVHT------GTRVTEVDADGVTLEDG--EEIP-------ADTVIWAAGVKAP--PLLADLGLP 265
|
330 340
....*....|....*....|....*..
gi 1224321637 424 TDQRSNVVTDPKTRMSTVDGVFAAGDC 450
Cdd:COG1252 266 TDRRGRVLVDPTLQVPGHPNVFAIGDC 292
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
146-182 |
1.98e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 65.68 E-value: 1.98e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLL 182
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLA 38
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
148-180 |
3.02e-10 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 56.00 E-value: 3.02e-10
10 20 30
....*....|....*....|....*....|...
gi 1224321637 148 IIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
144-180 |
4.78e-10 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 61.79 E-value: 4.78e-10
10 20 30
....*....|....*....|....*....|....*..
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
135-240 |
6.48e-10 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 61.41 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 135 PQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGlLMYGIphYKLWK-------------QRVQR--R 199
Cdd:COG1148 132 LEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGG-RAAQL--HKTFPgldcpqcilepliAEVEAnpN 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1224321637 200 IDLL----VAE--GIEFRYSCEVGKDATfDEIKSSFDAVVLATGAEE 240
Cdd:COG1148 209 ITVYtgaeVEEvsGYVGNFTVTIKKGPR-EEIEIEVGAIVLATGFKP 254
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
146-212 |
1.06e-09 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 59.72 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEK--------SDRAGGLLMYGI---PHYKLWK--QRVQRRIDLLVAE-GIEFR 211
Cdd:pfam01266 2 VVVIGGGIVGLSTAYELARRGLSVTLLERgddpgsgaSGRNAGLIHPGLrylEPSELARlaLEALDLWEELEEElGIDCG 81
|
.
gi 1224321637 212 Y 212
Cdd:pfam01266 82 F 82
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
139-237 |
2.53e-09 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 58.67 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 139 EQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRaggLLMYGIPHY-KLWKQRVQRRidllvaeGIEFRYSCEV- 216
Cdd:COG0446 120 KEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR---LLGVLDPEMaALLEEELREH-------GVELRLGETVv 189
|
90 100
....*....|....*....|....*...
gi 1224321637 217 ---GKD---ATFDEIKS-SFDAVVLATG 237
Cdd:COG0446 190 aidGDDkvaVTLTDGEEiPADLVVVAPG 217
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
142-180 |
3.02e-09 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 59.10 E-value: 3.02e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1224321637 142 TGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
147-179 |
3.10e-09 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 58.91 E-value: 3.10e-09
10 20 30
....*....|....*....|....*....|...
gi 1224321637 147 AIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
146-450 |
3.17e-09 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 59.04 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKsDRAGG-----------LLMY--------------GI--PHYKL-WK---Q 194
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGtclnvgcipskALIAaaeafheakhaeefGIhaDGPKIdFKkvmA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 195 RVQRRIDLLVAeGIEFRYSCEVGKD-----ATF--------DEIKSSFDAVVLATGAEEPrdlPVEGRELKGIH------ 255
Cdd:PRK06292 85 RVRRERDRFVG-GVVEGLEKKPKIDkikgtARFvdpntvevNGERIEAKNIVIATGSRVP---PIPGVWLILGDrlltsd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 256 --FAMEFLPqqnracwgdhniaalhprqrlinakgKKVIVIGGGdtgsdCIGtsmrqgatsvfnfelLEHPPAerspnnp 333
Cdd:PRK06292 161 daFELDKLP--------------------------KSLAVIGGG-----VIG---------------LELGQA------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 334 wpqWSRiMRVSTSVEEM--HVLGG------DVYYEIMTTRFigrdKNVTGLETVKVKWKDGRPEKIP---GSEQIWKCDL 402
Cdd:PRK06292 188 ---LSR-LGVKVTVFERgdRILPLedpevsKQAQKILSKEF----KIKLGAKVTSVEKSGDEKVEELekgGKTETIEADY 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1224321637 403 VLLAMG------FLGPrseliKQAGCKTDQRSNVVTDPKTrMSTVDGVFAAGDC 450
Cdd:PRK06292 260 VLVATGrrpntdGLGL-----ENTGIELDERGRPVVDEHT-QTSVPGIYAAGDV 307
|
|
| PRK06567 |
PRK06567 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated |
55-261 |
3.40e-09 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
Pssm-ID: 235832 [Multi-domain] Cd Length: 1028 Bit Score: 59.53 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 55 MTGCPLGNLIPEWNDLVYRGQWKQALTALHATNNFPEFTG-RVCpAPCETSCVLGiNEPPVTIKLHEVSIVDK------G 127
Cdd:PRK06567 281 KQGCPLKQKISEMNYVKAQGFNLSALAIIVIDNPMVAATGhRIC-NDCSKACIYQ-KQDPVNIPLIESNILEEtlklpyG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 128 FE-----EGW----IRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEK------------------------ 174
Cdd:PRK06567 359 LEiylllTRWnplnIYAPLPKEPTNYNILVTGLGPAGFSLSYYLLRSGHNVTAIDGlkitllpfdvhkpikfwheyknll 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 175 SDRA----GGLLMYGIPhyKLWKQRVQRRIDLLVAEGIEFRY------SCEVGKDATFDeikSSFDAVVLATGAEEPRDL 244
Cdd:PRK06567 439 SERMprgfGGVAEYGIT--VRWDKNNLDILRLILERNNNFKYydgvalDFNITKEQAFD---LGFDHIAFCIGAGQPKVL 513
|
250
....*....|....*..
gi 1224321637 245 PVEGRELKGIHFAMEFL 261
Cdd:PRK06567 514 DIENFEAKGVKTASDFL 530
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
144-181 |
4.45e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 58.36 E-value: 4.45e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGL 181
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
144-483 |
4.82e-09 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 58.51 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNR--AGHKVTVIEKSDR----AGGLLMYGIPHYKLWKQRVQRRIDLLVAEGIEFRYSCEVG 217
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIvsfgACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 218 K-DA-----------TFDEIKSSFDAVVLATGAEE--PrdlPVEGRELKGIHFAMEFLPQQNRacwgdhniaalhpRQRL 283
Cdd:PRK09564 81 KvDAknktitvknlkTGSIFNDTYDKLMIATGARPiiP---PIKNINLENVYTLKSMEDGLAL-------------KELL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 284 INAKGKKVIVIGGGDTGSDCIGTSMRQGAtsvfNFELLEHppAERSPNNPW-PQWSRIMRvstsvEEMHVLGGDVYYEIM 362
Cdd:PRK09564 145 KDEEIKNIVIIGAGFIGLEAVEAAKHLGK----NVRIIQL--EDRILPDSFdKEITDVME-----EELRENGVELHLNEF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 363 TTRFIGRDKnVTGLETVKVKWKdgrpekipgseqiwkCDLVLLAMGFlGPRSELIKQAGCKTDQRSNVVTDPKTRMStVD 442
Cdd:PRK09564 214 VKSLIGEDK-VEGVVTDKGEYE---------------ADVVIVATGV-KPNTEFLEDTGLKTLKNGAIIVDEYGETS-IE 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1224321637 443 GVFAAGDCRrgqslVVWAISEGR-----------EIARCVDEYLTGTESQLP 483
Cdd:PRK09564 276 NIYAAGDCA-----TIYNIVSNKnvyvplattanKLGRMVGENLAGRHVSFK 322
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
146-210 |
1.58e-08 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 56.45 E-value: 1.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEK-------SDRAGGLLMYGiphyklWKQRVQRRIDLLVAEGIEF 210
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERgrpgsgaSGRNAGQLRPG------LAALADRALVRLAREALDL 70
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
146-179 |
1.81e-08 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 56.10 E-value: 1.81e-08
10 20 30
....*....|....*....|....*....|....
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
146-185 |
4.05e-08 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 55.28 E-value: 4.05e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG-GLLMYG 185
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrKILISG 43
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
147-279 |
6.13e-08 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 54.91 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 147 AIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG-----------------------------GLLMY------------- 184
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGkkllisgggrcnltnscptpefvayyprnGKFLRsalsrfsnkdlid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 185 -----GIPHYKLWKQRV-------QRRIDLLVAE----GIEFRYSCEV--------GKDATFDEIKSSFDAVVLATGAee 240
Cdd:TIGR00275 81 ffeslGLELKVEEDGRVfpcsdsaADVLDALLNElkelGVEILTNSKVksiekedgGFGVETSGGEYEADKVIIATGG-- 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1224321637 241 pRDLPVEGRELKGIHFAMEFlpqqnracwGdHNIAALHP 279
Cdd:TIGR00275 159 -LSYPQLGSTGDGYEIAESL---------G-HTIVPPVP 186
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
142-239 |
1.07e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 53.48 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 142 TGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIphyklwKQRVQRRidlLVAEGIEFRYSCEV----- 216
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEI------SAALEKA---LEKNGVEVRLGTSVkeiig 221
|
90 100
....*....|....*....|....*..
gi 1224321637 217 --GKDATFDEIKSSFDA--VVLATGAE 239
Cdd:pfam07992 222 dgDGVEVILKDGTEIDAdlVVVAIGRR 248
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
133-180 |
1.43e-07 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 54.26 E-value: 1.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1224321637 133 IRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN03000 174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
145-216 |
1.45e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 48.74 E-value: 1.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224321637 145 SVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPhyklwkQRVQRRidlLVAEGIEFRYSCEV 216
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIA------KILQEK---LEKNGIEFLLNTTV 63
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
146-277 |
2.50e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 53.00 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYG----IPHYKLWKQRVQRRI--DLLVA----EGIEFRYSCE 215
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSGlvgpDMGFYLNKEQVVGGIarEFRQRlrarGGLPGPYGLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224321637 216 VGKDaTFD-EI-KSSFDAVVLATGAE-----EPRDLPVEGRELKGIHFAMEFLPQQNRA-----CWGDHNIAAL 277
Cdd:pfam12831 82 GGWV-PFDpEVaKAVLDEMLAEAGVTvllhtRVVGVVKEGGRITGVTVETKGGRITIRAkvfidATGDGDLAAL 154
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
154-180 |
2.54e-07 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 52.88 E-value: 2.54e-07
10 20
....*....|....*....|....*..
gi 1224321637 154 AGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGG 28
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
142-180 |
3.23e-07 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 52.43 E-value: 3.23e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1224321637 142 TGKSVAIIGGGPAGLACAQQLNRAgHKVTVIEKSDRAGG 180
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
141-243 |
7.91e-07 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 51.30 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 141 RTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDR---------AGGLLMygiphyklwkqrvqrriDLLVAEGIEFR 211
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRllprqldeeAGALLQ-----------------RLLEALGVEVR 202
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1224321637 212 YSCEV----GKD----ATFD---EIKSsfDAVVLATGAeEPRD 243
Cdd:COG1251 203 LGTGVteieGDDrvtgVRLAdgeELPA--DLVVVAIGV-RPNT 242
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
144-237 |
1.22e-06 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 50.86 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRaggLLmygiPHY-----KLWKQRvqrridlLVAEGIEFRYSCEV-- 216
Cdd:COG1249 169 KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDR---LL----PGEdpeisEALEKA-------LEKEGIDILTGAKVts 234
|
90 100 110
....*....|....*....|....*....|.
gi 1224321637 217 ------GKDATFD----EIKSSFDAVVLATG 237
Cdd:COG1249 235 vektgdGVTVTLEdgggEEAVEADKVLVATG 265
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
146-180 |
1.62e-06 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 50.36 E-value: 1.62e-06
10 20 30
....*....|....*....|....*....|....*
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
144-182 |
1.87e-06 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 50.23 E-value: 1.87e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAG--HKVTVIEKSDRAGGLL 182
Cdd:PRK11883 1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
146-178 |
2.06e-06 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 49.94 E-value: 2.06e-06
10 20 30
....*....|....*....|....*....|...
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRA 178
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPLA 38
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
138-184 |
2.10e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 50.25 E-value: 2.10e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1224321637 138 PEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMY 184
Cdd:PLN02172 5 QNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
151-240 |
5.12e-06 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 48.04 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 151 GGPAGLACAQQLNRAGHKVTVIEKSDR------AGGLLMYGIPHYKLWK-----QRVQRRIDLLVAEGIEFRYSCEVGKD 219
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFpgdkicGGGLLPRALEELEPLGldeplERPVRGARFYSPGGKSVELPPGRGGG 80
|
90 100
....*....|....*....|.
gi 1224321637 220 ATFDeiKSSFDAvVLATGAEE 240
Cdd:COG0644 81 YVVD--RARFDR-WLAEQAEE 98
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
144-237 |
5.37e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 48.66 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRaggLLmygiphyklwkQRVQRRI-----DLLVAEGIEFRYSCEV-- 216
Cdd:PRK06370 172 EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPR---LL-----------PREDEDVaaavrEILEREGIDVRLNAECir 237
|
90 100 110
....*....|....*....|....*....|.
gi 1224321637 217 ------GKDATFD----EIKSSFDAVVLATG 237
Cdd:PRK06370 238 verdgdGIAVGLDcnggAPEITGSHILVAVG 268
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
145-180 |
5.71e-06 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 48.53 E-value: 5.71e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1224321637 145 SVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN02268 2 SVIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
135-180 |
7.21e-06 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 48.73 E-value: 7.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1224321637 135 PQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN02529 152 SPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
144-237 |
1.09e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 47.86 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGIPhyKLWKQRVQRRIDLLV---AEGIEFRYSCEVGKDA 220
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVS--KQAQKILSKEFKIKLgakVTSVEKSGDEKVEELE 247
|
90
....*....|....*...
gi 1224321637 221 TFDEIKS-SFDAVVLATG 237
Cdd:PRK06292 248 KGGKTETiEADYVLVATG 265
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
132-240 |
1.52e-05 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 46.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 132 WIRPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRA-------GGLLMYGIPhyklwkqrvqRRIDLLV 204
Cdd:COG0569 84 RRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERverlaeeDVLVIVGDA----------TDEEVLE 153
|
90 100 110
....*....|....*....|....*....|....*.
gi 1224321637 205 AEGIEfryscevgkdatfdeiksSFDAVVLATGAEE 240
Cdd:COG0569 154 EAGIE------------------DADAVIAATGDDE 171
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
143-180 |
1.53e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 47.94 E-value: 1.53e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1224321637 143 GKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
144-188 |
1.62e-05 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 47.26 E-value: 1.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGH---KVTVIEKSDRAGgllmYGIPH 188
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELG----RGVAY 49
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
146-186 |
2.51e-05 |
|
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.
Pssm-ID: 130850 [Multi-domain] Cd Length: 388 Bit Score: 46.66 E-value: 2.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYGI 186
Cdd:TIGR01790 2 LAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGNHTYGV 42
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
148-450 |
2.58e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 46.73 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 148 IIGGGPAGLACAQQLNRAGHKVTVIEK--------------------SDRAGGLLM----YGIP---HYKLWKQRVQRRI 200
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERgllggtcvntgcvptktliaSARAAHLARraaeYGVSvggPVSVDFKAVMARK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 201 DLLVAE---GIEFRYSCEVGKD-----ATF--------DEIKSSFDAVVLATGAeEPRDLPVEGRELKGIH-----FAME 259
Cdd:PRK06370 90 RRIRARsrhGSEQWLRGLEGVDvfrghARFespntvrvGGETLRAKRIFINTGA-RAAIPPIPGLDEVGYLtnetiFSLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 260 FLPqqnracwgdhniaalhprQRLinakgkkvIVIGGGDTGSDcIGTSMRQGATSVFNFE----LLEHPPAErspnnpwp 335
Cdd:PRK06370 169 ELP------------------EHL--------VIIGGGYIGLE-FAQMFRRFGSEVTVIErgprLLPREDED-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 336 qwsrimrVSTSVEE-MHVLGGDVYYEIMTTRFIGRDKNVtgleTVKVKWKDGRPEkIPGSEqiwkcdlVLLAMG------ 408
Cdd:PRK06370 214 -------VAAAVREiLEREGIDVRLNAECIRVERDGDGI----AVGLDCNGGAPE-ITGSH-------ILVAVGrvpntd 274
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1224321637 409 FLGPrseliKQAGCKTDQRSNVVTDPKTRmSTVDGVFAAGDC 450
Cdd:PRK06370 275 DLGL-----EAAGVETDARGYIKVDDQLR-TTNPGIYAAGDC 310
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
146-180 |
4.50e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 45.59 E-value: 4.50e-05
10 20 30
....*....|....*....|....*....|....*
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
134-179 |
5.65e-05 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 45.61 E-value: 5.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1224321637 134 RPQPPEQRTgksVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:PRK01747 254 RPGSPKARD---AAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
146-181 |
7.41e-05 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 45.01 E-value: 7.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSD------RAGGL 181
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVERHAttsvlpRAHGL 45
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
138-240 |
7.81e-05 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 45.11 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 138 PEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKS-DRA--------GGLLMYGIPhyklwkqrvqRRIDLLVAEGI 208
Cdd:PRK09496 226 RLEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDpERAeelaeelpNTLVLHGDG----------TDQELLEEEGI 295
|
90 100 110
....*....|....*....|....*....|..
gi 1224321637 209 EfryscevgkdatfdeiksSFDAVVLATGAEE 240
Cdd:PRK09496 296 D------------------EADAFIALTNDDE 309
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
146-212 |
8.55e-05 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 44.79 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAggllmygiphYKLWKQRV----QRRIDLL--------------VAEG 207
Cdd:PRK08243 5 VAIIGAGPAGLLLGQLLHLAGIDSVVLERRSRE----------YVEGRIRAgvleQGTVDLLreagvgermdreglVHDG 74
|
....*
gi 1224321637 208 IEFRY 212
Cdd:PRK08243 75 IELRF 79
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
146-240 |
1.32e-04 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 44.49 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGH-KVTVIEKSDRAGGLLMYGIPHYKLWKQRVQRRIDL-LVAEGIEFRYSCEVGKDATFD 223
Cdd:PTZ00188 42 VGIIGAGPSALYCCKHLLKHERvKVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPvFLSPNYRFFGNVHVGVDLKME 121
|
90
....*....|....*..
gi 1224321637 224 EIKSSFDAVVLATGAEE 240
Cdd:PTZ00188 122 ELRNHYNCVIFCCGASE 138
|
|
| PRK13977 |
PRK13977 |
myosin-cross-reactive antigen; Provisional |
134-180 |
1.89e-04 |
|
myosin-cross-reactive antigen; Provisional
Pssm-ID: 237575 Cd Length: 576 Bit Score: 44.05 E-value: 1.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1224321637 134 RPQPPEQRTGKSVAIIGGGPAGLACAQQLNRAGH----KVTVIEKSDRAGG 180
Cdd:PRK13977 13 RPRKPEGVDNKKAYIIGSGLASLAAAVFLIRDGQmpgeNITILEELDVPGG 63
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
146-175 |
2.10e-04 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 43.55 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKS 175
Cdd:PLN02463 31 LVVVGGGPAGLAVAQQVSEAGLSVCCIDPS 60
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
135-180 |
2.63e-04 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 43.46 E-value: 2.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1224321637 135 PQPPEQRTGKSVAIIGGGPAGLACAQQLNRA-GHKVTVIEKSDRAGG 180
Cdd:PLN02576 4 AEGSAAASSKDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGG 50
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
146-172 |
3.13e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.92 E-value: 3.13e-04
10 20
....*....|....*....|....*..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVI 172
Cdd:PRK05329 5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
79-180 |
3.23e-04 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 43.25 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 79 ALTALHATNNFPEFTGRVCPAPCETSCVLGINEPPVTIKLHEVSIVDKGF--EEGWIRPQPPEQRTGK-SVAIIGGGPAG 155
Cdd:PLN02487 8 VLAAATPAKLVTSSSSLRSPVAGAVLRSPLKSARLSVSSSLDSNVSDMSVnaPKGLFPPEPEAYKGPKlKVAIIGAGLAG 87
|
90 100
....*....|....*....|....*
gi 1224321637 156 LACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN02487 88 MSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
135-177 |
4.18e-04 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 42.93 E-value: 4.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1224321637 135 PQPPEQRTGKS----VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDR 177
Cdd:PRK08132 11 RPHADQDADDParhpVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDT 57
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
146-177 |
4.27e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 42.59 E-value: 4.27e-04
10 20 30
....*....|....*....|....*....|..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDR 177
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPT 44
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
146-172 |
5.35e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 42.47 E-value: 5.35e-04
10 20
....*....|....*....|....*..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVI 172
Cdd:COG3075 5 VVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
138-175 |
5.37e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 42.15 E-value: 5.37e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1224321637 138 PEQRTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKS 175
Cdd:PRK06185 1 MAEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKH 38
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
146-179 |
6.16e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 42.06 E-value: 6.16e-04
10 20 30
....*....|....*....|....*....|....*
gi 1224321637 146 VAIIGGGPAGLACAQQLNRA-GHKVTVIEKSDRAG 179
Cdd:COG0579 7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
144-237 |
6.22e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 42.04 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAggllmygIPHYKLWKQRVQRriDLLVAEGIEFRYSC---EVGKDA 220
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI-------LPREEPSVAALAK--QYMEEDGITFLLNAhttEVKNDG 228
|
90 100
....*....|....*....|..
gi 1224321637 221 -----TFDEIKSSFDAVVLATG 237
Cdd:PRK07251 229 dqvlvVTEDETYRFDALLYATG 250
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
146-176 |
6.29e-04 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 42.19 E-value: 6.29e-04
10 20 30
....*....|....*....|....*....|.
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSD 176
Cdd:TIGR01988 2 IVIVGGGMVGLALALALARSGLKVALIEATP 32
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
148-180 |
6.79e-04 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 42.07 E-value: 6.79e-04
10 20 30
....*....|....*....|....*....|...
gi 1224321637 148 IIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PRK05249 10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
146-220 |
7.63e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 41.81 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVI----EKSD-RAGGLLMYGIPHYK---LWKQ--------RVQRRID----LLVA 205
Cdd:PRK07494 10 IAVIGGGPAGLAAAIALARAGASVALVapepPYADlRTTALLGPSIRFLErlgLWARlaphaaplQSMRIVDatgrLIRA 89
|
90
....*....|....*
gi 1224321637 206 EGIEFRySCEVGKDA 220
Cdd:PRK07494 90 PEVRFR-AAEIGEDA 103
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
146-449 |
8.00e-04 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 41.67 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGGLLMYG-IP---------HYKL-----------------------W 192
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGcIPskallhaaeRADEarhsedfgikaenvgidfkkvqeW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 193 KQRVQRRID-----LLVAEGIEFRY---------SCEVGKDATFDEIKssFDAVVLATGAeEPRDLPvegrelkGIHF-- 256
Cdd:PRK06416 87 KNGVVNRLTggvegLLKKNKVDIIRgeaklvdpnTVRVMTEDGEQTYT--AKNIILATGS-RPRELP-------GIEIdg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 257 ----------AMEFLPqqnracwgdhniaalhprqrlinakgKKVIVIGGGDTGSDcIGTSMRQGATSVFNFELLEH-PP 325
Cdd:PRK06416 157 rviwtsdealNLDEVP--------------------------KSLVVIGGGYIGVE-FASAYASLGAEVTIVEALPRiLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 326 AErspnNPWpqwsrimrVSTSVEEMHVLGGdvyYEIMT-TRFIGRDKNVTGletVKVKWKDGrpekipGSEQIWKCDLVL 404
Cdd:PRK06416 210 GE----DKE--------ISKLAERALKKRG---IKIKTgAKAKKVEQTDDG---VTVTLEDG------GKEETLEADYVL 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1224321637 405 LAMGfLGPRSELI--KQAGCKTDqRSNVVTDPKTRMStVDGVFAAGD 449
Cdd:PRK06416 266 VAVG-RRPNTENLglEELGVKTD-RGFIEVDEQLRTN-VPNIYAIGD 309
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
146-199 |
9.20e-04 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 41.70 E-value: 9.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRA----------GGLLMYGIPHyklwkqrvQRR 199
Cdd:COG3573 8 VIVVGAGLAGLVAAAELADAGRRVLLLDQEPEAnlggqafwsfGGLFLVDSPE--------QRR 63
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
144-174 |
1.03e-03 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 41.64 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|.
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEK 174
Cdd:COG2509 31 YDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
143-237 |
1.11e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.06 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 143 GKSVAIIGGGPAGLACAQQLNRAGHKVTVIeksDRaGGLLMYGIPHYKLW-KQRVQRRIDLLVAEG-IEFRYSCEVGK-- 218
Cdd:pfam13738 155 GQKVVVIGGYNSAVDAALELVRKGARVTVL---YR-GSEWEDRDSDPSYSlSPDTLNRLEELVKNGkIKAHFNAEVKEit 230
|
90 100
....*....|....*....|....*..
gi 1224321637 219 ------DATFDEIKS--SFDAVVLATG 237
Cdd:pfam13738 231 evdvsyKVHTEDGRKvtSNDDPILATG 257
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
144-182 |
1.23e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 41.26 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSD--RAGGLL 182
Cdd:PRK07588 1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPelRTGGYM 41
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
7-59 |
1.64e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.01 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224321637 7 FIKHGRRDKTLQPVNSRLQNFDEHYNYPSEEKVKTQAARCMDCGVPF----CMTGCP 59
Cdd:PRK12771 467 FTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCFecdnCYGACP 523
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
146-240 |
2.13e-03 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 37.89 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 146 VAIIGGGPAGLACAQQLnRAGHKVTVIEKSdraggllmygiphyklwkqrvQRRIDLLVAEGIEFRYscevGkDATFDEI 225
Cdd:pfam02254 1 IIIIGYGRVGRSLAEEL-SEGGDVVVIDKD---------------------EERVEELREEGVPVVV----G-DATDEEV 53
|
90 100
....*....|....*....|
gi 1224321637 226 --K---SSFDAVVLATGAEE 240
Cdd:pfam02254 54 leEagiEEADAVIAATGDDE 73
|
|
| sugar_DH |
cd08236 |
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ... |
141-177 |
2.17e-03 |
|
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.
Pssm-ID: 176198 [Multi-domain] Cd Length: 343 Bit Score: 40.29 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1224321637 141 RTGKSVAIIGGGPAGLACAQQLNRAG-HKVTVIEKSDR 177
Cdd:cd08236 158 TLGDTVVVIGAGTIGLLAIQWLKILGaKRVIAVDIDDE 195
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
145-180 |
2.68e-03 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 40.36 E-value: 2.68e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1224321637 145 SVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PLN02328 240 NVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGG 275
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
146-172 |
2.70e-03 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 40.00 E-value: 2.70e-03
10 20
....*....|....*....|....*..
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVI 172
Cdd:TIGR03378 3 VIIIGGGLAGLSCALRLAEAGKKCAII 29
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
141-177 |
2.81e-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: 2.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1224321637 141 RTGKSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDR 177
Cdd:cd05188 133 KPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDE 169
|
|
| Lycopene_cycl |
pfam05834 |
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ... |
146-176 |
2.89e-03 |
|
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.
Pssm-ID: 310433 [Multi-domain] Cd Length: 380 Bit Score: 40.09 E-value: 2.89e-03
10 20 30
....*....|....*....|....*....|...
gi 1224321637 146 VAIIGGGPAGLACAQQL--NRAGHKVTVIEKSD 176
Cdd:pfam05834 2 VVIIGAGPAGLSLAARLaaAKPGLSVVLIEPGP 34
|
|
| NAD_binding_9 |
pfam13454 |
FAD-NAD(P)-binding; |
147-180 |
3.25e-03 |
|
FAD-NAD(P)-binding;
Pssm-ID: 433222 [Multi-domain] Cd Length: 155 Bit Score: 38.41 E-value: 3.25e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1224321637 147 AIIGGGPAGLACA----QQLNRAGHKVTVIEKSDRAGG 180
Cdd:pfam13454 1 AIVGGGPSGLALLerllARAPKRPLEITLFDPSPPGAG 38
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
144-180 |
3.31e-03 |
|
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213540 [Multi-domain] Cd Length: 462 Bit Score: 39.82 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNR----AGHKVTVIEKSDRAGG 180
Cdd:TIGR00562 3 KHVVIIGGGISGLCAAYYLEKeipeLPVELTLVEASDRVGG 43
|
|
| PLN02661 |
PLN02661 |
Putative thiazole synthesis |
146-180 |
3.90e-03 |
|
Putative thiazole synthesis
Pssm-ID: 178267 Cd Length: 357 Bit Score: 39.43 E-value: 3.90e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGH-KVTVIEKSDRAGG 180
Cdd:PLN02661 95 VVIVGAGSAGLSCAYELSKNPNvKVAIIEQSVSPGG 130
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
146-174 |
4.34e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 39.29 E-value: 4.34e-03
10 20
....*....|....*....|....*....
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEK 174
Cdd:PRK06753 3 IAIIGAGIGGLTAAALLQEQGHEVKVFEK 31
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
134-180 |
4.52e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 39.70 E-value: 4.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1224321637 134 RPQPPEQRtgkSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAGG 180
Cdd:PRK06134 6 AYPPDLEC---DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
145-179 |
4.89e-03 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 39.25 E-value: 4.89e-03
10 20 30
....*....|....*....|....*....|....*
gi 1224321637 145 SVAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:PRK08163 6 PVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
144-176 |
6.44e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 38.70 E-value: 6.44e-03
10 20 30
....*....|....*....|....*....|...
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEKSD 176
Cdd:PRK06847 5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
146-180 |
6.65e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.22 E-value: 6.65e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1224321637 146 VAIIGGGPAGLACAQQLNRA-GHKVTVIEKSDRAGG 180
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVSPGG 55
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
141-240 |
7.01e-03 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 38.58 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224321637 141 RTGKSVAIIGGGPAGLACAQQLNRAG-HKVTVIEKSDRaggllmygiphyklwkqrvqrRIDLlvAEGIEFRYSCEVGKD 219
Cdd:COG1063 160 KPGDTVLVIGAGPIGLLAALAARLAGaARVIVVDRNPE---------------------RLEL--ARELGADAVVNPREE 216
|
90 100
....*....|....*....|....*.
gi 1224321637 220 ATFDEIKS-----SFDAVVLATGAEE 240
Cdd:COG1063 217 DLVEAVREltggrGADVVIEAVGAPA 242
|
|
| PRK08244 |
PRK08244 |
monooxygenase; |
146-174 |
7.12e-03 |
|
monooxygenase;
Pssm-ID: 236199 [Multi-domain] Cd Length: 493 Bit Score: 38.96 E-value: 7.12e-03
10 20
....*....|....*....|....*....
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEK 174
Cdd:PRK08244 5 VIIIGGGPVGLMLASELALAGVKTCVIER 33
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
146-179 |
7.55e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 38.63 E-value: 7.55e-03
10 20 30
....*....|....*....|....*....|....
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIEKSDRAG 179
Cdd:PRK00711 3 VVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPA 36
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
144-174 |
9.26e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 38.47 E-value: 9.26e-03
10 20 30
....*....|....*....|....*....|.
gi 1224321637 144 KSVAIIGGGPAGLACAQQLNRAGHKVTVIEK 174
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
146-173 |
9.97e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 38.34 E-value: 9.97e-03
10 20
....*....|....*....|....*...
gi 1224321637 146 VAIIGGGPAGLACAQQLNRAGHKVTVIE 173
Cdd:PRK07538 3 VLIAGGGIGGLTLALTLHQRGIEVVVFE 30
|
|
| |
