|
Name |
Accession |
Description |
Interval |
E-value |
| mycofact_OYE_2 |
TIGR03997 |
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow ... |
9-644 |
2.79e-152 |
|
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp., in Pelotomaculum thermopropionicum SI (Firmicutes), and in Geobacter uraniireducens Rf4 (Deltaproteobacteria). The function of this oxidoreductase is unknown.
Pssm-ID: 274912 [Multi-domain] Cd Length: 644 Bit Score: 454.15 E-value: 2.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLAdEQGNVTDRLLDYYRARARGGVALITTQIAAVsRESAAPFNLAI--YDDGFLPG 86
Cdd:TIGR03997 2 LFSPLRIGPVTLPNRIVFGAHLTNYA-VNNLPSERHAAYYAERAKGGAGLIITEELSV-HPSDRPYEKLIdgYRPAVIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 87 LRKLVETIHEHGAKVSIQLVHYGLLASivpkSMRQGVPIMVPSAMPWMVGDEPYREVDESDIERYVEDFSEAARRASEAG 166
Cdd:TIGR03997 80 YRRITDAVHAHGVKIFAQLNHNGGQGD----SSYSRLPVWAPSAVPDPLFREVPKAMEESDIAEVVAGFARVAGHVVAGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 167 ADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAVLQA 246
Cdd:TIGR03997 156 FDGIEIQASHSSLVRQFLSPLTNRRTDEYGGSLENRARFLLEVLEAVRKAIGPDRALGVRLCGDELVPGGLTLADAVEIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 247 RILEAAGA-DAVSVSGGIECWS-PLNIPCYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVALGR 323
Cdd:TIGR03997 236 RLLEALGLvDYINTSIGVATYTlHLVEASMHVPPGYAAFLAAAIREAVDLPVFAVGRInDPAQAERALAEGQADLVGMVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 324 PLLADPELPNKLRQGRVDHVRRCIYCNNC---ERQLGSPASCTVNPFLYREARSALVAAPS-PKKVMVVGGGPAGMQAAA 399
Cdd:TIGR03997 316 GQIADPDFAAKALEGREEDIRTCLSCNQEcigRVGLNRWLGCVVNPRAGREFGTVTLPPPRrPKRVLVVGGGPAGLEAAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 400 LLAQRGHRVSLHERDTDLGGQWKIACAMPGKEGYAAFVDYLRRCLGEHGVRVFLGSEVTREVVLAENPDALVLATGAVPQ 479
Cdd:TIGR03997 396 TAARRGHRVTLFEREDRLGGQVRLAARLPGRGEFADLIRNLASELRRAGVEVRLGVEADAELVLAEKPDAVVVATGSRPV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 480 GLGVPVASGGRVVQANDVILGRVDVGKKVAVIG--GRFLGMELAAWLAEQGREVTLVSRGRLGGRK-GPEEHFTYMAlvR 556
Cdd:TIGR03997 476 RPPWAGADGPRVVTVREVLTGRAEPGGRVLVVDelGFHQATSVAEFLAARGKKVTIITPSLFVGQDlGPTLDLEGWY--R 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 557 RLIALRIPMYLDTSVREITGAGVVL--DFGGETFHL-LADTVVLAIGAVPDSGLADAVEGLAPEVYRIGDCVEPRHAAAA 633
Cdd:TIGR03997 554 RAFQKGIEQTTDSLVTAVDGGTVTVvhHPTGRVRVLtGVDWVVLAAPPRPDDELYLSLKGRVPEVYRIGDCLAPRRVHAA 633
|
650
....*....|.
gi 1490726401 634 TLEAARVALKI 644
Cdd:TIGR03997 634 IREGHRVGLAI 644
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
3-370 |
5.31e-145 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 425.35 E-value: 5.31e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 3 MTKFHSLFQPGRIGGLRLENRLVMSAMGNFLADEQGNVTDRLLDYYRARARGGVALITTQIAAVSRES-AAPFNLAIYDD 81
Cdd:COG1902 1 MMKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGrGYPGQPGIWDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 82 GFLPGLRKLVETIHEHGAKVSIQLVHYGLLASIvpkSMRQGVPIMVPSAMPWMVGDEPYREVDESDIERYVEDFSEAARR 161
Cdd:COG1902 81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHP---DLPGGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 162 ASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDE 241
Cdd:COG1902 158 AKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 242 AVLQARILEAAGADAVSVSGGiECWSPLNIPcYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVA 320
Cdd:COG1902 238 SVELAKALEEAGVDYLHVSSG-GYEPDAMIP-TIVPEGYQLPFAARIRKAVGIPVIAVGGItTPEQAEAALASGDADLVA 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1490726401 321 LGRPLLADPELPNKLRQGRVDHVRRCIYCNNCERQLGSPASCTVNPFLYR 370
Cdd:COG1902 316 LGRPLLADPDLPNKAAAGRGDEIRPCIGCNQCLPTFYGGASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
10-338 |
7.92e-138 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 405.42 E-value: 7.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 10 FQPGRIGGLRLENRLVMSAMGNFLADEQGNVTDRLLDYYRARARGGVALITTQIAAVSRE-SAAPFNLAIYDDGFLPGLR 88
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEgKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 89 KLVETIHEHGAKVSIQLVHYGLLAsivpKSMRQGVPIMVPSAMPWMVGDEPYREVDESDIERYVEDFSEAARRASEAGAD 168
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQA----QPNLTGGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 169 AVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAVLQARI 248
Cdd:cd02803 157 GVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 249 LEAAGADAVSVSGGIECWSPLNIPCYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVALGRPLLA 327
Cdd:cd02803 237 LEEAGVDALHVSGGSYESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIrDPEVAEEILAEGKADLVALGRALLA 316
|
330
....*....|.
gi 1490726401 328 DPELPNKLRQG 338
Cdd:cd02803 317 DPDLPNKAREG 327
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
9-350 |
9.65e-103 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.
Pssm-ID: 240085 [Multi-domain] Cd Length: 343 Bit Score: 316.09 E-value: 9.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLAdEQGNVTDRLLDYYRARARGGVALITTQIAAV-SRESAAPFNLAIYDDGFLPGL 87
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYA-EDGLPSERYIAYHEERARGGAGLIITEGSSVhPSDSPAFGNLNASDDEIIPGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 88 RKLVETIHEHGAKVSIQLVHYGllasivPKSMRQ--GVPIMVPSAMPWMVGDEPYREVDESDIERYVEDFSEAARRASEA 165
Cdd:cd04734 80 RRLAEAVHAHGAVIMIQLTHLG------RRGDGDgsWLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 166 GADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAVLQ 245
Cdd:cd04734 154 GLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 246 ARILEAAGA-DAVSVSGG---IECWSPLNIPCYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVA 320
Cdd:cd04734 234 AARLAAEGLiDYVNVSAGsyyTLLGLAHVVPSMGMPPGPFLPLAARIKQAVDLPVFHAGRIrDPAEAEQALAAGHADMVG 313
|
330 340 350
....*....|....*....|....*....|
gi 1490726401 321 LGRPLLADPELPNKLRQGRVDHVRRCIYCN 350
Cdd:cd04734 314 MTRAHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
9-332 |
1.78e-95 |
|
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.
Pssm-ID: 239242 [Multi-domain] Cd Length: 336 Bit Score: 297.10 E-value: 1.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLADEqGNVTDRLLDYYRARARGGVALITTQIAAVSRESA-APFNLAIYDDGFLPGL 87
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAED-GVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRiTPGDLGLWNDEQIEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 88 RKLVETIHEHGAKVSIQLVHYGLLASIVP--KSMRQGVP-------IMVPSAMPWMVGDEPYREVDESDIERYVEDFSEA 158
Cdd:cd02932 80 KRIVDFIHSQGAKIGIQLAHAGRKASTAPpwEGGGPLLPpggggwqVVAPSAIPFDEGWPTPRELTREEIAEVVDAFVAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 159 ARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLT 238
Cdd:cd02932 160 ARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGWD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 239 VDEAVLQARILEAAGADAVSVS-GGIecwSPLNIPcylfPKGP--MVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSG 314
Cdd:cd02932 240 LEDSVELAKALKELGVDLIDVSsGGN---SPAQKI----PVGPgyQVPFAERIRQEAGIPVIAVGLItDPEQAEAILESG 312
|
330
....*....|....*...
gi 1490726401 315 RADFVALGRPLLADPELP 332
Cdd:cd02932 313 RADLVALGRELLRNPYWP 330
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
9-366 |
2.80e-91 |
|
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.
Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 286.88 E-value: 2.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLaDEQGNVTDRLLDYYRARARGGVALITTQIAAVSRESA-APFNLAIYDDGFLPGL 87
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGL-EELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKlGPGGPVLNSPRQAAGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 88 RKLVETIHEHGAKVSIQLVHYGLLASIvpksmrqgvPIMV-PSAMPWMVGDEPYREVDESDIERYVEDFSEAARRASEAG 166
Cdd:cd02930 80 RLITDAVHAEGGKIALQILHAGRYAYH---------PLCVaPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 167 ADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAVLQA 246
Cdd:cd02930 151 YDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 247 RILEAAGADAVSVSGGiecWSPLNIP--CYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVALGR 323
Cdd:cd02930 231 KALEAAGADILNTGIG---WHEARVPtiATSVPRGAFAWATAKLKRAVDIPVIASNRInTPEVAERLLADGDADMVSMAR 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1490726401 324 PLLADPELPNKLRQGRVDHVRRCIYCNN-CERQL--GSPASCTVNP 366
Cdd:cd02930 308 PFLADPDFVAKAAAGRADEINTCIACNQaCLDHIftGQRASCLVNP 353
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
9-366 |
4.12e-79 |
|
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.
Pssm-ID: 239241 [Multi-domain] Cd Length: 382 Bit Score: 255.90 E-value: 4.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNF-LADEQGNVTDRLLDYYRARARGGVALITTQIAAVSRE----SAAPFNLAIYDD-G 82
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLgLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEieqfPMPSLPCPTYNPtA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 83 FLPGLRKLVETIHEHGAKVSIQLVHyGLLASIVPKSMRQGVPImVPSAMPWMVGDE-PYREVDESDIERYVEDFSEAARR 161
Cdd:cd02931 81 FIRTAKEMTERVHAYGTKIFLQLTA-GFGRVCIPGFLGEDKPV-APSPIPNRWLPEiTCRELTTEEVETFVGKFGESAVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 162 ASEAGADAVELHACH-GCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVR-------------- 226
Cdd:cd02931 159 AKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRysvksyikdlrqga 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 227 MNGTDDVEGGLTVDEAVLQARILEAAGADAVSV-SGGIECWSPLNIPCYlFPKGPMVSLAEAVKKAVRIPVIVAGKID-A 304
Cdd:cd02931 239 LPGEEFQEKGRDLEEGLKAAKILEEAGYDALDVdAGSYDAWYWNHPPMY-QKKGMYLPYCKALKEVVDVPVIMAGRMEdP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726401 305 ELAEQIIGSGRADFVALGRPLLADPELPNKLRQGRVDHVRRCIYCNN-C--ERQLGSPASCTVNP 366
Cdd:cd02931 318 ELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDgClgRMALGGNLSCAVNP 382
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
7-332 |
9.54e-74 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 240.37 E-value: 9.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 7 HSLFQPGRIGGLRLENRLVMSAMGNFLADEQ-GNVTDRLLDYYRARARGGVALITTQIAAVSRES-AAPFNLAIYDDGFL 84
Cdd:PRK13523 1 SKLFSPYTIKDVTLKNRIVMSPMCMYSSENKdGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGrISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 85 PGLRKLVETIHEHGAKVSIQLVHYGllasivPKSMRQGvPIMVPSAMPWmvgDEPYR---EVDESDIERYVEDFSEAARR 161
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAG------RKAELEG-DIVAPSAIPF---DEKSKtpvEMTKEQIKETVLAFKQAAVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 162 ASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDkVGSGfPVSVRMNGTDDVEGGLTVDE 241
Cdd:PRK13523 151 AKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKE-VWDG-PLFVRISASDYHPGGLTVQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 242 AVLQARILEAAGADAVSVSGGieCWSPLNIPcyLFPkGPMVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVA 320
Cdd:PRK13523 229 YVQYAKWMKEQGVDLIDVSSG--AVVPARID--VYP-GYQVPFAEHIREHANIATGAVGLItSGAQAEEILQNNRADLIF 303
|
330
....*....|..
gi 1490726401 321 LGRPLLADPELP 332
Cdd:PRK13523 304 IGRELLRNPYFP 315
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
8-341 |
2.71e-71 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 234.27 E-value: 2.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 8 SLFQPGRIGGLRLENRLVMSAMGNFLADEQGNV-TDRLLDYYRARARGGVALITTQIAAVSRESAA-PFNLAIYDDGFLP 85
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVMAPMTRLRSLDDGTKaTGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGfDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 86 GLRKLVETIHEHGAKVSIQLVHYGLLASIVPKSMRQGVPIMVPSAMP--WMVGDEPYREVDESDIERYVEDFSEAARRAS 163
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREAPMEYRPDLEVDGPSDPFALGaqEFEIASPRYEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 164 EAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAV 243
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAETA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 244 LQARILEAAGADAVSVSGG--IECWSPlnIPCYLFPKGP-MVSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFV 319
Cdd:pfam00724 241 QFIYLLAELGVRLPDGWHLayIHAIEP--RPRGAGPVRTrQQHNTLFVKGVWKGPLITVGRIdDPSVAAEIVSKGRADLV 318
|
330 340
....*....|....*....|..
gi 1490726401 320 ALGRPLLADPELPNKLRQGRVD 341
Cdd:pfam00724 319 AMGRPFLADPDLPFKAKKGRPL 340
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
9-329 |
9.21e-70 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 241.38 E-value: 9.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLADEqGNVTDRLLDYYRARARGGVALITTQIAAVSRES-AAPFNLAIYDDGFLPGL 87
Cdd:PRK08255 399 MFTPFRLRGLTLKNRVVVSPMAMYSAVD-GVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGrITPGCPGLYNDEQEAAW 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 88 RKLVETIHEHG-AKVSIQLVHYGLLASIvpKSMRQGV---------PIMVPSAMPWMVGDEPYREVDESDIERYVEDFSE 157
Cdd:PRK08255 478 KRIVDFVHANSdAKIGIQLGHSGRKGST--RLGWEGIdepleegnwPLISASPLPYLPGSQVPREMTRADMDRVRDDFVA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 158 AARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGL 237
Cdd:PRK08255 556 AARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGGN 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 238 TVDEAVLQARILEAAGADAVSVSGGIEcwSPLNIPCYlfpkGPM--VSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSG 314
Cdd:PRK08255 636 TPDDAVEIARAFKAAGADLIDVSSGQV--SKDEKPVY----GRMyqTPFADRIRNEAGIATIAVGAIsEADHVNSIIAAG 709
|
330
....*....|....*
gi 1490726401 315 RADFVALGRPLLADP 329
Cdd:PRK08255 710 RADLCALARPHLADP 724
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
9-344 |
2.42e-68 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 226.71 E-value: 2.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIG-GLRLENRLVMSAMGNFLADEQGNVTDRLLDYYRARArGGVALITTQIAAVSRE-SAAPFNLAIYDDGFLPG 86
Cdd:cd04735 1 LFEPFTLKnGVTLKNRFVMAPMTTYSSNPDGTITDDELAYYQRRA-GGVGMVITGATYVSPSgIGFEGGFSADDDSDIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 87 LRKLVETIHEHGAKVSIQLVHYGLLAsiVPKSMRQGVPImVPSAM-PWMVGDEPYREVDESDIERYVEDFSEAARRASEA 165
Cdd:cd04735 80 LRKLAQAIKSKGAKAILQIFHAGRMA--NPALVPGGDVV-SPSAIaAFRPGAHTPRELTHEEIEDIIDAFGEATRRAIEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 166 GADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFA---VRIVQRMRDK-VGSGFPVSVRMNGTDDVEGGLTVDE 241
Cdd:cd04735 157 GFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPlavVKAVQEVIDKhADKDFILGYRFSPEEPEEPGIRMED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 242 A-VLQARILEaAGADAVSVSGgiecWSPLNIPcylfPKGPMV--SLAEAVKKAV--RIPVIVAGKID-AELAEQIIGSGr 315
Cdd:cd04735 237 TlALVDKLAD-KGLDYLHISL----WDFDRKS----RRGRDDnqTIMELVKERIagRLPLIAVGSINtPDDALEALETG- 306
|
330 340
....*....|....*....|....*....
gi 1490726401 316 ADFVALGRPLLADPELPNKLRQGRVDHVR 344
Cdd:cd04735 307 ADLVAIGRGLLVDPDWVEKIKEGREDEIN 335
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
17-338 |
1.67e-67 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240084 [Multi-domain] Cd Length: 338 Bit Score: 224.00 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 17 GLRLENRLVMSAMGNFLADEQGNVTDRLLDYYRARARGGVALITT---QIAAVSRESAAPF-NLAIYDDGFLPGLRKLVE 92
Cdd:cd04733 10 GATLPNRLAKAAMSERLADGRGLPTPELIRLYRRWAEGGIGLIITgnvMVDPRHLEEPGIIgNVVLESGEDLEAFREWAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 93 TIHEHGAKVSIQLVHYGLLAsivPKSMRQGvPIM----VPSAMPWMVGDEPyREVDESDIERYVEDFSEAARRASEAGAD 168
Cdd:cd04733 90 AAKANGALIWAQLNHPGRQS---PAGLNQN-PVApsvaLDPGGLGKLFGKP-RAMTEEEIEDVIDRFAHAARLAQEAGFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 169 AVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVEGGLTVDEAVLQARI 248
Cdd:cd04733 165 GVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEEDALEVVEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 249 LEAAGADAVSVSGGiecwsplnipCYLFPKGPM-------------VSLAEAVKKAVRIPVIVAGKI-DAELAEQIIGSG 314
Cdd:cd04733 245 LEEAGVDLVELSGG----------TYESPAMAGakkestiareayfLEFAEKIRKVTKTPLMVTGGFrTRAAMEQALASG 314
|
330 340
....*....|....*....|....
gi 1490726401 315 RADFVALGRPLLADPELPNKLRQG 338
Cdd:cd04733 315 AVDGIGLARPLALEPDLPNKLLAG 338
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
9-338 |
1.27e-64 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include 12-oxophytodienoate reductase, pentaerythritol tetranitrate reductase, morphinone reductase, and related enzymes.
Pssm-ID: 239243 [Multi-domain] Cd Length: 338 Bit Score: 216.18 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLADEQGNVTDRLLDYYRARARGGvaLITTQIAAVSRESAA-PFNLAIYDDGFLPGL 87
Cdd:cd02933 2 LFSPLKLGNLTLKNRIVMAPLTRSRADPDGVPTDLMAEYYAQRASAG--LIITEATQISPQGQGyPNTPGIYTDEQVEGW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 88 RKLVETIHEHGAKVSIQLVHYGLLASivPKSMRQGVPIMVPSAMPW---------MVGDEPYREVDESDIERYVEDFSEA 158
Cdd:cd02933 80 KKVTDAVHAKGGKIFLQLWHVGRVSH--PSLLPGGAPPVAPSAIAAegkvftpagKVPYPTPRALTTEEIPGIVADFRQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 159 ARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFpVSVRM------NGTDD 232
Cdd:cd02933 158 ARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADR-VGIRLspfgtfNDMGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 233 VEGGLTVDEAV--LQAR------ILEAAGADAvsvsggiecwsplnipcylfPKGPMVSLAEAVKKAVRIPVIVAGKIDA 304
Cdd:cd02933 237 SDPEATFSYLAkeLNKRglaylhLVEPRVAGN--------------------PEDQPPDFLDFLRKAFKGPLIAAGGYDA 296
|
330 340 350
....*....|....*....|....*....|....
gi 1490726401 305 ELAEQIIGSGRADFVALGRPLLADPELPNKLRQG 338
Cdd:cd02933 297 ESAEAALADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| mycofact_OYE_1 |
TIGR03996 |
mycofactocin system FadH/OYE family oxidoreductase 1; The yeast protein called old yellow ... |
9-628 |
4.92e-62 |
|
mycofactocin system FadH/OYE family oxidoreductase 1; The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp. The function of this oxidoreductase is unknown.
Pssm-ID: 188511 [Multi-domain] Cd Length: 633 Bit Score: 217.49 E-value: 4.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLADEQGnVTDRLLDYYRARARGGVALITTQIAAVSrESAAPFNLAIYDDGFLPGLR 88
Cdd:TIGR03996 2 LSQAITLAGRRAPSRVLFGPHETNLGRGRA-LSERHVAYYERRAAGGAGIVVTEVASVT-SDDWPYERAPLASECGSGWA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 89 KLVETIHEHGAKVSIQLVHYGLLASivpkSMRQGVPIMVPSAMPWMVGDEPYREVDESDIERYVEDFSEAARRASEAGAD 168
Cdd:TIGR03996 80 AVAAACRPHGTLVLAGLGHTGGQGS----SAYSQSVLWGPSPVADVVSREVPMEMDQAEIDSLVAGFRAGAARAVAAGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 169 AVELHACHGCLVSTFLSPVTNRRNDAYGgtvEKRARFAVRIVQRMRDKVGSGFPVSVRMNGTDDVE-GGLTVDEAVLQAR 247
Cdd:TIGR03996 156 GVELDAGPRSLLRQFLSGLTNRRGDDYG---RDRLRLTREVLTAVREEVGDTPILSLRLSCDEEAPwAGITPDLAAGHAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 248 ILEAAGADAVSVSGGIecWSPLNI-PCYLFPKGPMVSLAEAVKKAV--RIPVIVAGKI-DAELAEQIIGSGRADFVALGR 323
Cdd:TIGR03996 233 ALADLLDLLVVVRGGP--FSTGAYrPDFHTPPAFNTDLCRRIRRAAagRVPVVLQGSVvDTADAQQALDSAVADVVEMTR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 324 PLLADPELpnKLRQGRVDHVRRCIYCNN-CE-RQLGSP-ASCTVNPFLYREA--RSALVAAPSPKKVMVVGGGPAGMQAA 398
Cdd:TIGR03996 311 AQIADPDL--VVKAGRGHRPRPCVLCNQtCQvRDPRNPvVTCVGNPAAGHETvdPDEGGRAATPGDVLVVGGGPAGLEAA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 399 ALLAQRGHRVSLHERDTDLGGQWKIACAMPGKEGYAAFVDYLRRCLGEHGVRVFLGSEVTREVVLAENPDA--LVLATGA 476
Cdd:TIGR03996 389 RVLAARGHRVTLAERSAHLGGMLRIAARGPGLHRLAALADWLEAECRRLGVRIRLGAAIGVEELDRARAAGgvVLLATGS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 477 VPQGLGVPVASGGRVVQANDVILGRVDVGK-KVAVIG--GRFLGMELAAWLAEQGREVTLVSRGRLGGRKGPEEHFTYMA 553
Cdd:TIGR03996 469 VPRPLPAPVDATVRVLDAVHVLAAGPALPQgPVVVHDplGGPVGVATAEWLAALGRPVSIVTPDSVVGSRLGASGDLAPA 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726401 554 LVrRLIALRIPMYLDTSVREITGAGVVLD--FGGETFHLLADTVVLAIGAVPDsglaDAVEGLAPEVYRIGDCVEPR 628
Cdd:TIGR03996 549 NT-RLQRAGVTRQLRSRVRAIGPDGLVLEdaWTGERSILACAVVIDCSPRLPR----DTLHSLRPDLPRAGDAVAPR 620
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
9-344 |
2.11e-58 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240095 [Multi-domain] Cd Length: 361 Bit Score: 200.62 E-value: 2.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLAdEQGNVTDRLLDYYRARARGGVALITTQIAAVSRESAA--PFNLAIYDDGFLPG 86
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFS-PGGVPGQDVAAYYRRRAAGGVGLIITEGTAVDHPAASgdPNVPRFHGEDALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 87 LRKLVETIHEHGAKVSIQLVHYGLLASiVPKSMRQGVPIMVPSAMpWMVGDEPYREVDESDIERYVEDFSEAARRASEAG 166
Cdd:cd04747 80 WKKVVDEVHAAGGKIAPQLWHVGAMRK-LGTPPFPDVPPLSPSGL-VGPGKPVGREMTEADIDDVIAAFARAAADARRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 167 ADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMN--GTDDVEGGLTVDEAVL 244
Cdd:cd04747 158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSqwKQQDYTARLADTPDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 245 QARI--LEAAGADAVSVSGGiECWSPlnipcyLFPKGPMvSLAEAVKKAVRIPVIVAGKI-------------------D 303
Cdd:cd04747 238 EALLapLVDAGVDIFHCSTR-RFWEP------EFEGSEL-NLAGWTKKLTGLPTITVGSVgldgdfigafagdegaspaS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1490726401 304 AELAEQIIGSGRADFVALGRPLLADPELPNKLRQGRVDHVR 344
Cdd:cd04747 310 LDRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDELI 350
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
2-366 |
9.04e-58 |
|
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.
Pssm-ID: 239239 [Multi-domain] Cd Length: 370 Bit Score: 199.12 E-value: 9.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 2 RMTKFHSLFQPGRIGGLRLENRLVMSAMGNFLadeqGNVTDRLLDYYRA-RARGGVALITTQIAAVSRESA-APFNLA-I 78
Cdd:cd02929 1 RDPRHDILFEPIKIGPVTARNRFYQVPHCNGM----GYRKPSAQAAMRGiKAEGGWGVVNTEQCSIHPSSDdTPRISArL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 79 YDDGFLPGLRKLVETIHEHGAKVSIQLVHYGLLASivpkSMRQGVPIMVPSAMPWMVGDEPY---REVDESDIERYVEDF 155
Cdd:cd02929 77 WDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAP----NRESRETPLGPSQLPSEFPTGGPvqaREMDKDDIKRVRRWY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 156 SEAARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGFPVSVRMnGTDDV-- 233
Cdd:cd02929 153 VDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRF-SVDELig 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 234 EGGLTVDEAVLqaRILEAAG--ADAVSVS-GGIECWSPlniPCYLFPKGPMVSLAEAVKKAVRIPVIVAGK-IDAELAEQ 309
Cdd:cd02929 232 PGGIESEGEGV--EFVEMLDelPDLWDVNvGDWANDGE---DSRFYPEGHQEPYIKFVKQVTSKPVVGVGRfTSPDKMVE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726401 310 IIGSGRADFVALGRPLLADPELPNKLRQGRVDHVRRCIYCNNC--ERQLGSPASCTVNP 366
Cdd:cd02929 307 VVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCNICisGDEGGVPMRCTQNP 365
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
9-338 |
1.99e-38 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 145.64 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 9 LFQPGRIGGLRLENRLVMSAMGNFLADEQGNVTDRLL-DYYRARARGGVaLIT--TQIAAVSRESA-APfnlAIYDDGFL 84
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMAPLTRLRSIEPGDIPTPLMaEYYRQRASAGL-IISeaTQISAQAKGYAgAP---GLHSPEQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 85 PGLRKLVETIHEHGAKVSIQLVHYGLL--------------ASIVPKSMR------QGVPIMVPSAMPwmvgdepyREVD 144
Cdd:PRK10605 79 AAWKKITAGVHAEGGHIAVQLWHTGRIshaslqpggqapvaPSAINAGTRtslrdeNGQAIRVETSTP--------RALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 145 ESDIERYVEDFSEAARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGfPVS 224
Cdd:PRK10605 151 LEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGAD-RIG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 225 VRM----------NGTDDVEGGLTVDEAVLQARI--LEAAGADAvsvSGGiecwsplnipcylfpkgpmVSLAEAVKKAV 292
Cdd:PRK10605 230 IRIsplgtfnnvdNGPNEEADALYLIEQLGKRGIayLHMSEPDW---AGG-------------------EPYSDAFREKV 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1490726401 293 RI----PVIVAGKIDAELAEQIIGSGRADFVALGRPLLADPELPNKLRQG 338
Cdd:PRK10605 288 RArfhgVIIGAGAYTAEKAETLIGKGLIDAVAFGRDYIANPDLVARLQRK 337
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
383-624 |
1.63e-27 |
|
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: 113.18 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTD-LGGQ---WKIACAMPGKEGYAAFVDYLRRCLGEH------GVRVF 452
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcPYGGcvlSKALLGAAEAPEIASLWADLYKRKEEVvkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 453 LGSEVT------REVVLAENP---------DALVLATGAVPQGLGVP-----VASGGRVVQANDVILgRVDVGKKVAVIG 512
Cdd:pfam07992 81 LGTEVVsidpgaKKVVLEELVdgdgetityDRLVIATGARPRLPPIPgvelnVGFLVRTLDSAEALR-LKLLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 513 GRFLGMELAAWLAEQGREVTLVSRGRLGGRKGPEEHftYMALVRRLIALRIPMYLDTSVREITGAGVVLD-FGGETFHLL 591
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEI--SAALEKALEKNGVEVRLGTSVKEIIGDGDGVEvILKDGTEID 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1490726401 592 ADTVVLAIGAVPDSGLADAVeGLA-----------------PEVYRIGDC 624
Cdd:pfam07992 238 ADLVVVAIGRRPNTELLEAA-GLElderggivvdeylrtsvPGIYAAGDC 286
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
382-629 |
2.58e-26 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 111.77 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 382 PKKVMVVGGGPAGMQAAALLAQRGHRVSLH----ERD---------TDLGGQWKIACAMPGKEGYAAfvdylrrclgEHG 448
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITvigaEPHppynrpplsKVLAGETDEEDLLLRPADFYE----------ENG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 449 VRVFLGSEVT------REVVLAENP----DALVLATGAVPQGLGVPVASGGRVVQANDV-----ILGRVDVGKKVAVIGG 513
Cdd:COG1251 71 IDLRLGTRVTaidraaRTVTLADGEtlpyDKLVLATGSRPRVPPIPGADLPGVFTLRTLddadaLRAALAPGKRVVVIGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 514 RFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEEhftyMA--LVRRLIALRIPMYLDTSVREITGA----GVVLDfGGE 586
Cdd:COG1251 151 GLIGLEAAAALRKRGLEVTVVERApRLLPRQLDEE----AGalLQRLLEALGVEVRLGTGVTEIEGDdrvtGVRLA-DGE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490726401 587 TfhLLADTVVLAIGAVPDSGLADAVeGLA---------------PEVYRIGDCVEPRH 629
Cdd:COG1251 226 E--LPADLVVVAIGVRPNTELARAA-GLAvdrgivvddylrtsdPDIYAAGDCAEHPG 280
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
7-336 |
6.37e-26 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 110.33 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 7 HSLFQPGRIGGLRLENRLVMSAMGNFLAdEQGNVTDRLLDYYRARARGGVALITtQIAAVSRESAA-PFNLAIYDDGFLP 85
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRCRA-LNGIPNAALAEYYAQRSTPGGFLIS-EGTLISPTAPGfPHVPGIYSDEQVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 86 GLRKLVETIHEHGAKVSIQLVHYGLlASIVPKSMRQGVPIMV---PSAMPW--MVGDEPY------REVDESDIERYVED 154
Cdd:PLN02411 88 AWKKVVDAVHAKGSIIFCQLWHVGR-ASHQVYQPGGAAPISStnkPISERWriLMPDGSYgkypkpRALETSEIPEVVEH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 155 FSEAARRASEAGADAVELHACHGCLVSTFLSPVTNRRNDAYGGTVEKRARFAVRIVQRMRDKVGSGfPVSVRMNGTDDVE 234
Cdd:PLN02411 167 YRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGAD-RVGVRVSPAIDHL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 235 GGLTVDEAVLQARILEAAGAdAVSVSGGIECWSPLNIPCYLF----------PKGPMVSLAEAVKKAVRIPVIVAGKIDA 304
Cdd:PLN02411 246 DATDSDPLNLGLAVVERLNK-LQLQNGSKLAYLHVTQPRYTAygqtesgrhgSEEEEAQLMRTLRRAYQGTFMCSGGFTR 324
|
330 340 350
....*....|....*....|....*....|..
gi 1490726401 305 ELAEQIIGSGRADFVALGRPLLADPELPNKLR 336
Cdd:PLN02411 325 ELGMQAVQQGDADLVSYGRLFISNPDLVLRFK 356
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
378-615 |
2.81e-22 |
|
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: 99.82 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGqwkiacaM-----PG----KEGYAAFVDYLRrclgEHG 448
Cdd:COG0493 117 APRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG-------LlrygiPEfrlpKDVLDREIELIE----ALG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 449 VRVFLGSEVTREVVLAE---NPDALVLATGA-VPQGLGVPVASGGRVVQAND----VILGR-----VDVGKKVAVIGGRF 515
Cdd:COG0493 186 VEFRTNVEVGKDITLDElleEFDAVFLATGAgKPRDLGIPGEDLKGVHSAMDfltaVNLGEapdtiLAVGKRVVVIGGGN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 516 LGMELAAWLAEQG-REVTLVSRgrlggrkGPEEHFTYMAL---------VRRlialripMYLdTSVREITGAG------- 578
Cdd:COG0493 266 TAMDCARTALRLGaESVTIVYR-------RTREEMPASKEeveealeegVEF-------LFL-VAPVEIIGDEngrvtgl 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1490726401 579 --VVLDFG--------------GETFHLLADTVVLAIGAVPDSGLADAVEGLA 615
Cdd:COG0493 331 ecVRMELGepdesgrrrpvpieGSEFTLPADLVILAIGQTPDPSGLEEELGLE 383
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
446-629 |
3.60e-21 |
|
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: 94.88 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 446 EHGVRVFLGSEVT------REVVLAENP----DALVLATGAVP-----QGLGVPVASGGRVVQANDVILGRVDV--GKKV 508
Cdd:COG0446 48 RKGIDVRTGTEVTaidpeaKTVTLRDGEtlsyDKLVLATGARPrpppiPGLDLPGVFTLRTLDDADALREALKEfkGKRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 509 AVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEehftyMA--LVRRLIALRIPMYLDTSVREITGAG---VVLD 582
Cdd:COG0446 128 VVIGGGPIGLELAEALRKRGLKVTLVERApRLLGVLDPE-----MAalLEEELREHGVELRLGETVVAIDGDDkvaVTLT 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726401 583 fGGETFHllADTVVLAIGAVPDSGLADAvEGLA-----------------PEVYRIGDCVEPRH 629
Cdd:COG0446 203 -DGEEIP--ADLVVVAPGVRPNTELAKD-AGLAlgergwikvdetlqtsdPDVYAAGDCAEVPH 262
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
378-625 |
1.16e-18 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 89.08 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG--QWKIacamPG----KEGYAAFVDYLRrclgEHGVRV 451
Cdd:PRK11749 136 APKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllRYGI----PEfrlpKDIVDREVERLL----KLGVEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 452 FLGSEVTREVVLAE---NPDALVLATGA-VPQGLGVPVASGGRVVQANDVI--------LGRVDVGKKVAVIGGRFLGME 519
Cdd:PRK11749 208 RTNTEVGRDITLDElraGYDAVFIGTGAgLPRFLGIPGENLGGVYSAVDFLtrvnqavaDYDLPVGKRVVVIGGGNTAMD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 520 LAAWLAEQG-REVTLVSR-GR--LGGRK-----------------------GPEEHFTYMALVRrlialripMYLDtsVR 572
Cdd:PRK11749 288 AARTAKRLGaESVTIVYRrGReeMPASEeevehakeegvefewlaapveilGDEGRVTGVEFVR--------MELG--EP 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490726401 573 EITGAGVVLDfGGETFHLLADTVVLAIGAVPDSGLADAVEGLA------------------PEVYRIGDCV 625
Cdd:PRK11749 358 DASGRRRVPI-EGSEFTLPADLVIKAIGQTPNPLILSTTPGLElnrwgtiiaddetgrtslPGVFAGGDIV 427
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
384-609 |
1.69e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 86.71 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTdLGGQ-WKIAC-----AMPGKEGYAAFVDYLRRCLGEHGVRVFLGsEV 457
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQlATTKEienypGFPEGISGPELAERLREQAERFGAEILLE-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 458 TrEVVLAENP-------------DALVLATGAVPQGLGVP---------VASGGrVVQANDVilgrvdVGKKVAVIGGRF 515
Cdd:COG0492 80 T-SVDKDDGPfrvttddgteyeaKAVIIATGAGPRKLGLPgeeefegrgVSYCA-TCDGFFF------RGKDVVVVGGGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 516 LGMELAAWLAEQGREVTLVSRGrlggrkgpeEHFT-YMALVRRLIAL-RIPMYLDTSVREITG----AGVVLDFG--GET 587
Cdd:COG0492 152 SALEEALYLTKFASKVTLIHRR---------DELRaSKILVERLRANpKIEVLWNTEVTEIEGdgrvEGVTLKNVktGEE 222
|
250 260
....*....|....*....|..
gi 1490726401 588 FHLLADTVVLAIGAVPDSGLAD 609
Cdd:COG0492 223 KELEVDGVFVAIGLKPNTELLK 244
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
385-625 |
3.44e-16 |
|
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: 81.29 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTdLGGqwkiACA----MPGK---------------EGY------------ 433
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGG----TCLnvgcIPSKallhaaevahearhaAEFgisagapsvdwa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 434 ----------AAFVDYLRRCLGEHGVRVFLGS---------EVT-REVVLAENpdaLVLATGAVPQGLGVPVASGGRVVQ 493
Cdd:COG1249 81 almarkdkvvDRLRGGVEELLKKNGVDVIRGRarfvdphtvEVTgGETLTADH---IVIATGSRPRVPPIPGLDEVRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 494 ANDvILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRkgpEEHFTYMALVRRLIALRIPMYLDTSVR 572
Cdd:COG1249 158 SDE-ALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPG---EDPEISEALEKALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726401 573 EI--TGAGVVLDF--GGETFHLLADTVVLAIGAVPDS---GLADAveGL-----------------APEVYRIGDCV 625
Cdd:COG1249 234 SVekTGDGVTVTLedGGGEEAVEADKVLVATGRRPNTdglGLEAA--GVelderggikvdeylrtsVPGIYAIGDVT 308
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
385-617 |
4.27e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 81.38 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTdLGGqwkiACA----MPGK------------------------------ 430
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGP-LGG----TCLnvgcIPSKaliaaaeafheakhaeefgihadgpkidfk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 431 ----------EGYAAFV-DYLRRCLGE---HGVRVFLGS---EVTREVVLAENpdaLVLATGA-VPQGLGVPVASGGRVV 492
Cdd:PRK06292 81 kvmarvrrerDRFVGGVvEGLEKKPKIdkiKGTARFVDPntvEVNGERIEAKN---IVIATGSrVPPIPGVWLILGDRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 493 qANDVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEehftYMALVRRLIALRIPMYLDTSV 571
Cdd:PRK06292 158 -TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPE----VSKQAQKILSKEFKIKLGAKV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1490726401 572 REITGAG----VVLDFGGETFHLLADTVVLAIGAVPDsgladaVEGLAPE 617
Cdd:PRK06292 233 TSVEKSGdekvEELEKGGKTETIEADYVLVATGRRPN------TDGLGLE 276
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
378-615 |
5.19e-16 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 81.46 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQwkiacAMPGKEGY---AAFVDY-LRRCLgEHGVRVFL 453
Cdd:PRK12771 133 APDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGM-----MRYGIPAYrlpREVLDAeIQRIL-DLGVEVRL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 454 GSEVTREVVLAE---NPDALVLATGA-VPQGLGVPVASGGRVVQA----NDVILGRVD-VGKKVAVIGGRFLGMElAAWL 524
Cdd:PRK12771 207 GVRVGEDITLEQlegEFDAVFVAIGAqLGKRLPIPGEDAAGVLDAvdflRAVGEGEPPfLGKRVVVIGGGNTAMD-AART 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 525 AEQ--GREVTLVSRGRLggRKGPEEHFTYMALVR---RLIALRIPMYLDTSVREITGAGVV------LD-------FGGE 586
Cdd:PRK12771 286 ARRlgAEEVTIVYRRTR--EDMPAHDEEIEEALRegvEINWLRTPVEIEGDENGATGLRVItvekmeLDedgrpspVTGE 363
|
250 260
....*....|....*....|....*....
gi 1490726401 587 TFHLLADTVVLAIGAVPDSGLADAVEGLA 615
Cdd:PRK12771 364 EETLEADLVVLAIGQDIDSAGLESVPGVE 392
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
383-614 |
3.77e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 71.97 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG--QWKIA-CAMPGKEGYAAFVDYLRRClgehGVR----VFLGS 455
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlVYGIPeFRLPKETVVKKEIENIKKL----GVKietnVVVGK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 456 EVTREVVLAENP-DALVLATGA-VPQGLGVPVASGGRVVQANDViLGRVD--------------VGKKVAVIGGRFLGME 519
Cdd:PRK12831 217 TVTIDELLEEEGfDAVFIGSGAgLPKFMGIPGENLNGVFSANEF-LTRVNlmkaykpeydtpikVGKKVAVVGGGNVAMD 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 520 LAAWLAEQGREVTLV---SRGRLGGRK-----GPEEHFTYMALVR----------RLIALR-IPMYL---DTSVR----E 573
Cdd:PRK12831 296 AARTALRLGAEVHIVyrrSEEELPARVeevhhAKEEGVIFDLLTNpveilgdengWVKGMKcIKMELgepDASGRrrpvE 375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1490726401 574 ITGAGVVLDfggetfhllADTVVLAIGAVPDSGLADAVEGL 614
Cdd:PRK12831 376 IEGSEFVLE---------VDTVIMSLGTSPNPLISSTTKGL 407
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
382-625 |
7.24e-13 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 70.55 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 382 PKKVMVVGGGPAGMQAAALLAQR---GHRV-------------SLHE-----RDTDlggqwkiACAMPgkegyaafvdyL 440
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKlggDAEVtlidpnpyhlfqpLLPEvaagtLSPD-------DIAIP-----------L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 441 RRCLGEHGVRVFLGsEVT------REVVLAENP----DALVLATGAVPQGLGVP--------VASGGRVVQANDVILGRV 502
Cdd:COG1252 63 RELLRRAGVRFIQG-EVTgidpeaRTVTLADGRtlsyDYLVIATGSVTNFFGIPglaehalpLKTLEDALALRERLLAAF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 503 DVGK-----KVAVIGGRFLGMELAAWLAEQGR-------------EVTLVSRG-RLGGRKGPEehfTYMALVRRLIALRI 563
Cdd:COG1252 142 ERAErrrllTIVVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGpRILPGLGEK---LSEAAEKELEKRGV 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726401 564 PMYLDTSVREITGAGVVLDfGGETFHllADTVVLAIGAVP-----DSGLA---------DA---VEGLaPEVYRIGDCV 625
Cdd:COG1252 219 EVHTGTRVTEVDADGVTLE-DGEEIP--ADTVIWAAGVKAppllaDLGLPtdrrgrvlvDPtlqVPGH-PNVFAIGDCA 293
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
372-478 |
1.01e-12 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 71.04 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 372 ARSALVAAPSP------KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQW-KIACAMPGKEGYAAFVDYL-RRC 443
Cdd:COG1148 124 AKAKLLEPLEPikvpvnKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAaQLHKTFPGLDCPQCILEPLiAEV 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1490726401 444 LGEHGVRVFLGSEVTR--------EVVLAENP--------DALVLATGAVP 478
Cdd:COG1148 204 EANPNITVYTGAEVEEvsgyvgnfTVTIKKGPreeieievGAIVLATGFKP 254
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
378-513 |
2.05e-12 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 69.81 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG-------QWKiacaMPGKegyaaFVDYLRRCLGEHGVR 450
Cdd:PRK12810 139 VKRTGKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipDFK----LEKE-----VIDRRIELMEAEGIE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 451 VFLGSEVTREVV---LAENPDALVLATGA-VPQGLGVPvasgGR-----------VVQANDVILGRVD------VGKKVA 509
Cdd:PRK12810 210 FRTNVEVGKDITaeeLLAEYDAVFLGTGAyKPRDLGIP----GRdldgvhfamdfLIQNTRRVLGDETepfisaKGKHVV 285
|
....
gi 1490726401 510 VIGG 513
Cdd:PRK12810 286 VIGG 289
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
385-627 |
2.83e-12 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 69.21 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTdLGG--------------------------------------------Q 420
Cdd:TIGR01350 4 VIVIGGGPGGYVAAIRAAQLGLKVALVEKEY-LGGtclnvgciptkallhsaevydeikhakdlgievenvsvdwekmqK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 421 WKIACAMPGKEGyaafVDYLRRClgeHGVRVFLG-------------SEVTREVVLAENpdaLVLATGAVPQGLGVPVAS 487
Cdd:TIGR01350 83 RKNKVVKKLVGG----VSGLLKK---NKVTVIKGeakfldpgtvsvtGENGEETLEAKN---IIIATGSRPRSLPGPFDF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 488 GGRVVQANDVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLggrKGPEEHFTYMALVRRLIALRIPMY 566
Cdd:TIGR01350 153 DGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLdRI---LPGEDAEVSKVLQKALKKKGVKIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 567 LDTSVREIT--GAGVVLDF-GGETFHLLADTVVLAIGAVPDSGLADaVEGL-------------------APEVYRIGDC 624
Cdd:TIGR01350 230 TNTKVTAVEknDDQVTYENkGGETETLTGEKVLVAVGRKPNTEGLG-LEKLgveldergrivvdeymrtnVPGIYAIGDV 308
|
...
gi 1490726401 625 VEP 627
Cdd:TIGR01350 309 IGG 311
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
378-600 |
3.20e-10 |
|
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: 62.57 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWK------IAC------------AMPG-KEGYAA--- 435
Cdd:COG2072 2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTWRdnrypgLRLdtpshlyslpffPNWSdDPDFPTgde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 436 FVDYLRRCLGEHGVR--VFLGSEVTR-----------------EVVLAenpDALVLATGAvpqgLGVPV--------ASG 488
Cdd:COG2072 82 ILAYLEAYADKFGLRrpIRFGTEVTSarwdeadgrwtvttddgETLTA---RFVVVATGP----LSRPKipdipgleDFA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 489 GRVVQA----NDVILgrvdVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSR---------------GRLGGRKGPEEHF 549
Cdd:COG2072 155 GEQLHSadwrNPVDL----AGKRVLVVGTGASAVQIAPELARVAAHVTVFQRtppwvlprpnydperGRPANYLGLEAPP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 550 -----TYMALVRRLIALRIPMY---------------------------------LDTSVREITGAGVVLDFGGEtfhLL 591
Cdd:COG2072 231 alnrrDARAWLRRLLRAQVKDPelglltpdyppgckrpllstdyyealrrgnvelVTGGIERITEDGVVFADGTE---HE 307
|
....*....
gi 1490726401 592 ADTVVLAIG 600
Cdd:COG2072 308 VDVIVWATG 316
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
468-626 |
5.25e-10 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 61.86 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 468 DALVLATGA---VPqglgvPVASGGRVVQAN-----DVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSR-GR 538
Cdd:PRK04965 101 DKLVLATGAsafVP-----PIPGRELMLTLNsqqeyRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNaAS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 539 LGGRKGPEehFTYMALVRRLIALRIPMYLDTSVREI--TGAGVVLDF-GGETFHllADTVVLAIGAVPDSGLADAVeGL- 614
Cdd:PRK04965 176 LLASLMPP--EVSSRLQHRLTEMGVHLLLKSQLQGLekTDSGIRATLdSGRSIE--VDAVIAAAGLRPNTALARRA-GLa 250
|
170 180
....*....|....*....|....*.
gi 1490726401 615 --------------APEVYRIGDCVE 626
Cdd:PRK04965 251 vnrgivvdsylqtsAPDIYALGDCAE 276
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
378-603 |
8.74e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 60.77 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQwkIACAMPG--------KEGYaafvdylrRCLGEHGV 449
Cdd:PRK12770 14 PPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGL--MLFGIPEfripiervREGV--------KELEEAGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 450 RVF--------------LGSEVTREVV----LAENPDALVLATGA-VPQGLGVPVASGGRVVQANDVI-------LGRVD 503
Cdd:PRK12770 84 VFHtrtkvccgeplheeEGDEFVERIVsleeLVKKYDAVLIATGTwKSRKLGIPGEDLPGVYSALEYLfriraakLGYLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 504 -------VGKKVAVIGGRFLGMELAAWLAEQG-REVTLVSRGRLggRKGPEEHFTYMALVRR---LIALRIPM--YLDTS 570
Cdd:PRK12770 164 wekvppvEGKKVVVVGAGLTAVDAALEAVLLGaEKVYLAYRRTI--NEAPAGKYEIERLIARgveFLELVTPVriIGEGR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1490726401 571 VREI------------TGAGVVLDFGGETFHLLADTVVLAIGAVP 603
Cdd:PRK12770 242 VEGVelakmrlgepdeSGRPRPVPIPGSEFVLEADTVVFAIGEIP 286
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
152-339 |
2.58e-09 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 57.89 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 152 VEDFSEAARRASEAGADAVELHAchGCLVSTflspVTNRRndaYGGTVEKRARFAVRIVQRMRDKVgsGFPVSV--RMNG 229
Cdd:cd02801 66 PETLAEAAKIVEELGADGIDLNM--GCPSPK----VTKGG---AGAALLKDPELVAEIVRAVREAV--PIPVTVkiRLGW 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 230 TDDveggltvDEAVLQARILEAAGADAVSVSG--GIECWSPlniPCYLfpkgpmvSLAEAVKKAVRIPVIVAGKI-DAEL 306
Cdd:cd02801 135 DDE-------EETLELAKALEDAGASALTVHGrtREQRYSG---PADW-------DYIAEIKEAVSIPVIANGDIfSLED 197
|
170 180 190
....*....|....*....|....*....|...
gi 1490726401 307 AEQIIGSGRADFVALGRPLLADPELPNKLRQGR 339
Cdd:cd02801 198 ALRCLEQTGVDGVMIGRGALGNPWLFREIKELL 230
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
383-614 |
2.74e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 60.14 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWKIACA---MPgKEGYAAFVDYLRRcLGEHGVR-VFLGSEVT 458
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPefrLP-KKIVDVEIENLKK-LGVKFETdVIVGKTIT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 459 REVVLAENPDALVLATGA-VPQGLGVPVASGGRVVQANDvILGRVD--------------VGKKVAVIGGRFLGMELAAW 523
Cdd:PRK12778 510 IEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVMSSNE-YLTRVNlmdaaspdsdtpikFGKKVAVVGGGNTAMDSART 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 524 LAEQGRE-VTLV---SRGRLGGRK-----GPEEHFTYMALVR----------RLIALR-IPMYL---DTSVR----EITG 576
Cdd:PRK12778 589 AKRLGAErVTIVyrrSEEEMPARLeevkhAKEEGIEFLTLHNpieyladekgWVKQVVlQKMELgepDASGRrrpvAIPG 668
|
250 260 270
....*....|....*....|....*....|....*...
gi 1490726401 577 AGVVLDfggetfhllADTVVLAIGAVPDSGLADAVEGL 614
Cdd:PRK12778 669 STFTVD---------VDLVIVSVGVSPNPLVPSSIPGL 697
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
126-333 |
5.08e-09 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 58.11 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 126 MVPSamPWMVGDEPYREVDESDIER-----------YVEDFSEAARRASEAGADAVELHAchGClvstflsPVTNRRNDA 194
Cdd:pfam01207 30 MVTA--KAQLRPEKVRIRMLSELEEptplavqlggsDPALLAEAAKLVEDRGADGIDINM--GC-------PSKKVTRGG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 195 YGGTVEKRARFAVRIVQRMRDKVgsGFPVSVRMN-GTDDVEggltvDEAVLQARILEAAGADAVSVSGGI-ECWS--PLN 270
Cdd:pfam01207 99 GGAALLRNPDLVAQIVKAVVKAV--GIPVTVKIRiGWDDSH-----ENAVEIAKIVEDAGAQALTVHGRTrAQNYegTAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726401 271 IPcylfpkgpmvSLAEaVKKAVRIPVIVAGKI-DAELAEQIIGSGRADFVALGRPLLADPELPN 333
Cdd:pfam01207 172 WD----------AIKQ-VKQAVSIPVIANGDItDPEDAQRCLAYTGADGVMIGRGALGNPWLFA 224
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
375-492 |
3.07e-08 |
|
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: 55.79 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 375 ALVAAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWKIACAmpgkegyaafvDYLRRCLGEHGVRVFLG 454
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEIS-----------AALEKALEKNGVEVRLG 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1490726401 455 SEVTR--------EVVLAE----NPDALVLATGAVP-----QGLGVPVASGGRVV 492
Cdd:pfam07992 214 TSVKEiigdgdgvEVILKDgteiDADLVVVAIGRRPntellEAAGLELDERGGIV 268
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
153-337 |
3.10e-08 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 55.49 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 153 EDFSEAARRASEAGADAVELHAchGCLVSTflspVTNRRndayGG-----TVEKrarfAVRIVQRMRDKVgsGFPVSV-- 225
Cdd:COG0042 74 EELAEAARIAEELGADEIDINM--GCPVKK----VTKGG----AGaallrDPEL----VAEIVKAVVEAV--DVPVTVki 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 226 RMnGTDDVEggLTVDEAvlqARILEAAGADAVSV---------SGgiecwsPLNipcYlfpkgpmvSLAEAVKKAVRIPV 296
Cdd:COG0042 138 RL-GWDDDD--ENALEF---ARIAEDAGAAALTVhgrtreqryKG------PAD---W--------DAIARVKEAVSIPV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490726401 297 IVAGKI-DAELAEQIIGSGRADFVALGRPLLADPELPNKLRQ 337
Cdd:COG0042 195 IGNGDIfSPEDAKRMLEETGCDGVMIGRGALGNPWLFREIDA 236
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
375-478 |
1.01e-07 |
|
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: 54.05 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 375 ALVAAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLggqwkiaCAMPGKEgyaaFVDYLRRCLGEHGVRVFLG 454
Cdd:COG0446 117 EALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL-------LGVLDPE----MAALLEEELREHGVELRLG 185
|
90 100 110
....*....|....*....|....*....|....*
gi 1490726401 455 SEVTR-------EVVLAENP----DALVLATGAVP 478
Cdd:COG0446 186 ETVVAidgddkvAVTLTDGEeipaDLVVVAPGVRP 220
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
385-627 |
1.81e-07 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 54.00 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDtDLGG---QW-----K--IACA--------------MPGKEGY--AAFVD 438
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-KLGGtclNRgcipsKalLHAAeradearhsedfgiKAENVGIdfKKVQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 439 Y-------LRRCLG----EHGVRVFLG----SEVTREVVLAENPD------ALVLATGAVPQGL-GVPVasGGRVVQAND 496
Cdd:PRK06416 86 WkngvvnrLTGGVEgllkKNKVDIIRGeaklVDPNTVRVMTEDGEqtytakNIILATGSRPRELpGIEI--DGRVIWTSD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 497 VILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRGR--LGGrkgpEEHFTYMALVRRLIALRIPMYLDTSVREI 574
Cdd:PRK06416 164 EALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPriLPG----EDKEISKLAERALKKRGIKIKTGAKAKKV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726401 575 T----GAGVVLDFGGETFHLLADTVVLAIGAVPDS---GLADA-VE---GL----------APEVYRIGDCVEP 627
Cdd:PRK06416 240 EqtddGVTVTLEDGGKEETLEADYVLVAVGRRPNTenlGLEELgVKtdrGFievdeqlrtnVPNIYAIGDIVGG 313
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
384-519 |
7.12e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 52.64 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG--QWKIacamPGKEGYAAFVDYLRRCLGEHGVRV----FLGSEV 457
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGvlQYGI----PSFRLPRDIIDREVQRLVDIGVKIetnkVIGKTF 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726401 458 TREVVLAENP-DALVLATGA-VPQGLGVPVASGGRVVQANDvILGRVD---------------VGKKVAVIGGRFLGME 519
Cdd:PRK12775 508 TVPQLMNDKGfDAVFLGVGAgAPTFLGIPGEFAGQVYSANE-FLTRVNlmggdkfpfldtpisLGKSVVVIGAGNTAMD 585
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
490-603 |
7.30e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 52.17 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 490 RVVQANDVILGRVDVGKKVAVIGGRFLGMElAAW-LAEQGREVTLVSR-GRLGGR--------KGPEEHFTYMALVRRLI 559
Cdd:COG1148 125 KAKLLEPLEPIKVPVNKRALVIGGGIAGMT-AALeLAEQGYEVYLVEKePELGGRaaqlhktfPGLDCPQCILEPLIAEV 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1490726401 560 AL--RIPMYLDTSVREITGAG-----VVLDFGGETFHLLADTVVLAIGAVP 603
Cdd:COG1148 204 EAnpNITVYTGAEVEEVSGYVgnftvTIKKGPREEIEIEVGAIVLATGFKP 254
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
387-421 |
8.60e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 46.37 E-value: 8.60e-07
10 20 30
....*....|....*....|....*....|....*
gi 1490726401 387 VVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQW 421
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
383-624 |
1.82e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 50.81 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLA--QRGHRVSLHE-RDTDLGGqwkiACAMPGKEGyaAFVDYLRRCLG-------EHGVRVF 452
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKrlNKELEITVYEkTDIVSFG----ACGLPYFVG--GFFDDPNTMIArtpeefiKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 453 LGSEVTR---------------EVVLAENPDALVLATGAVPQglgVPVASGgrvVQANDV-ILGRVDVG----------- 505
Cdd:PRK09564 75 TEHEVVKvdaknktitvknlktGSIFNDTYDKLMIATGARPI---IPPIKN---INLENVyTLKSMEDGlalkellkdee 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 506 -KKVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEEhFTYMaLVRRLIALRIPMYLDTSVREITG----AGV 579
Cdd:PRK09564 149 iKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdRILPDSFDKE-ITDV-MEEELRENGVELHLNEFVKSLIGedkvEGV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490726401 580 VLDFGgetfHLLADTVVLAIGAVP------DSGLADAVEGL----------APEVYRIGDC 624
Cdd:PRK09564 227 VTDKG----EYEADVVIVATGVKPntefleDTGLKTLKNGAiivdeygetsIENIYAAGDC 283
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
383-608 |
1.89e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.69 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHerdtdlggqwkiacaMPGKEGYAAF------VDYL-------RRCLGEH-- 447
Cdd:PRK09754 4 KTIIIVGGGQAAAMAAASLRQQGFTGELH---------------LFSDERHLPYerpplsKSMLledspqlQQVLPANww 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 448 ---------GVRVFLGSEVTREVVLAENP----DALVLATGAVPQGLGVPVASGGRVV---QANDVILGR--VDVGKKVA 509
Cdd:PRK09754 69 qennvhlhsGVTIKTLGRDTRELVLTNGEswhwDQLFIATGAAARPLPLLDALGERCFtlrHAGDAARLRevLQPERSVV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 510 VIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEEHFTYmaLVRRLIALRIPMYLDTSVREIT-GAGVVLDFG-GE 586
Cdd:PRK09754 149 IVGAGTIGLELAASATQRRCKVTVIELAaTVMGRNAPPPVQRY--LLQRHQQAGVRILLNNAIEHVVdGEKVELTLQsGE 226
|
250 260
....*....|....*....|..
gi 1490726401 587 TfhLLADTVVLAIGAVPDSGLA 608
Cdd:PRK09754 227 T--LQADVVIYGIGISANDQLA 246
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
384-419 |
3.44e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 49.89 E-value: 3.44e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG 419
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
383-535 |
4.65e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 49.77 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG-------QWKIACAMPGKEgyAAFVDYLrrclgehGVRVFLGS 455
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGvmrygipSYRLPDEALDKD--IAFIEAL-------GVKIHLNT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 456 EVTREVV---LAENPDALVLATG-AVPQGLGVPVASGGRVVQA-------NDVILG---RVDVGKKVAVIGGRFLGMELA 521
Cdd:PRK13984 355 RVGKDIPleeLREKHDAVFLSTGfTLGRSTRIPGTDHPDVIQAlpllreiRDYLRGegpKPKIPRSLVVIGGGNVAMDIA 434
|
170 180
....*....|....*....|
gi 1490726401 522 AWLA-----EQGR-EVTLVS 535
Cdd:PRK13984 435 RSMArlqkmEYGEvNVKVTS 454
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
381-625 |
5.52e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 49.34 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 381 SPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWKIacAMPGKEGYAAFVDYLRRCLGEHGVRVFLGSEVTRE 460
Cdd:PRK12814 192 SGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRY--GIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGRD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 461 VVLAE---NPDALVLATGAVPQG-LGVP------VASGGRVVQanDVILGR-VDVGKKVAVIGGRFLGMELAAWLAEQGR 529
Cdd:PRK12814 270 ITLEElqkEFDAVLLAVGAQKASkMGIPgeelpgVISGIDFLR--NVALGTaLHPGKKVVVIGGGNTAIDAARTALRLGA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 530 E-VTLVSrgrlggRKGPEEHFTYMALVRRLIALRI---PMYLDTSVREITGAGVV------------------LDFGGET 587
Cdd:PRK12814 348 EsVTILY------RRTREEMPANRAEIEEALAEGVslrELAAPVSIERSEGGLELtaikmqqgepdesgrrrpVPVEGSE 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726401 588 FHLLADTVVLAIGAVPDSGLADAvEGLAPE------------------VYRIGDCV 625
Cdd:PRK12814 422 FTLQADTVISAIGQQVDPPIAEA-AGIGTSrngtvkvdpetlqtsvagVFAGGDCV 476
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
380-599 |
5.67e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 49.15 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 380 PSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHE-RD-----------------TDLGGQWkiacaMPGkeGYAAFVDYLR 441
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRDrvggrvwtlrfgddglyAELGAMR-----IPP--SHTNLLALAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 442 rclgEHGVRVFLGSEVTREVVLAEN-----PDALVLATGAVPQGLGvpvasggrvvQANDVILGRVDVGKKVAViggRFL 516
Cdd:COG1231 78 ----ELGLPLEPFPNENGNALLYLGgkrvrAGEIAADLRGVAELLA----------KLLRALAAALDPWAHPAA---ELD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 517 GMELAAWLAEQG------REVTLVSRGRLGG----------------RKGPEEHFT----YMALVRRLIA-LRIPMYLDT 569
Cdd:COG1231 141 RESLAEWLRRNGaspsarRLLGLLGAGEYGAdpdelslldllryaasAGGGAQQFRivggMDQLPRALAAeLGDRIRLGA 220
|
250 260 270
....*....|....*....|....*....|...
gi 1490726401 570 SVREI--TGAGVVLDF-GGETFHllADTVVLAI 599
Cdd:COG1231 221 PVTRIrqDGDGVTVTTdDGGTVR--ADAVIVTV 251
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
381-419 |
5.79e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 5.79e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1490726401 381 SPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG 419
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
428-604 |
5.88e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 48.37 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 428 PGKEGYAafvDYLRRCLGEHGVRVFLGSEV--------------TREVVLAENpdaLVLATG--AVPQGLGVPVAsggrV 491
Cdd:pfam13738 72 PSGNEYA---EYLRRVADHFELPINLFEEVtsvkkeddgfvvttSKGTYQARY---VIIATGefDFPNKLGVPEL----P 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 492 VQANDVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRGRLGGRKGPEEHFTYMALVR-RLIAL----RIPMY 566
Cdd:pfam13738 142 KHYSYVKDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLSPDTLnRLEELvkngKIKAH 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490726401 567 LDTSVREIT--GAGVVLDFGGETFHLLADTVVLAIGAVPD 604
Cdd:pfam13738 222 FNAEVKEITevDVSYKVHTEDGRKVTSNDDPILATGYHPD 261
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
431-610 |
8.72e-06 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 48.80 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 431 EGYAAFVdylrrclGEHGVRVFLGSEVTrevvlaenPDALVLATGAVPQGLGVPVASGGRVvQANDVILGRVDVGKKVAV 510
Cdd:PRK07846 108 RGHARFI-------GPKTLRTGDGEEIT--------ADQVVIAAGSRPVIPPVIADSGVRY-HTSDTIMRLPELPESLVI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 511 IGGRFLGMELAAWLAEQGREVTLVSRGRLGGRKGPE---EHFTYMALVRRLIALRIPMyldTSVREiTGAGVVLDFGGET 587
Cdd:PRK07846 172 VGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDdisERFTELASKRWDVRLGRNV---VGVSQ-DGSGVTLRLDDGS 247
|
170 180
....*....|....*....|...
gi 1490726401 588 fHLLADTVVLAIGAVPDSGLADA 610
Cdd:PRK07846 248 -TVEADVLLVATGRVPNGDLLDA 269
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
152-338 |
1.18e-05 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 47.54 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 152 VEDFSEAARRASEAGADAVEL-----HACHGCLvstflspvtnrrndAYGGTVEKrarfAVRIVQRMRDKVgsGFPVSVR 226
Cdd:cd04740 101 VEEFVEVAEKLADAGADAIELniscpNVKGGGM--------------AFGTDPEA----VAEIVKAVKKAT--DVPVIVK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 227 M--NGTDDVEggltvdeavlQARILEAAGADAVS----VSGG---IECWSPL--NI------PCyLFPKGpmVSLAEAVK 289
Cdd:cd04740 161 LtpNVTDIVE----------IARAAEEAGADGLTlintLKGMaidIETRKPIlgNVtgglsgPA-IKPIA--LRMVYQVY 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490726401 290 KAVRIPVI-VAGKIDAELAEQIIGSGrADFVALGRPLLADPELPNKLRQG 338
Cdd:cd04740 228 KAVEIPIIgVGGIASGEDALEFLMAG-ASAVQVGTANFVDPEAFKEIIEG 276
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
387-624 |
1.19e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 48.27 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 387 VVGGGPAGMQAAALLAQRGHRVSLHERDtDLGGqwkiAC----AMPGK----EGYAAFV--------------------- 437
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERG-LLGG----TCvntgCVPTKtliaSARAAHLarraaeygvsvggpvsvdfka 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 438 --------------DYLRRCLGEHGVRVFLGS---------EVTREVVLAENpdaLVLATGAVPQglgVPVASGgrVVQA 494
Cdd:PRK06370 85 vmarkrrirarsrhGSEQWLRGLEGVDVFRGHarfespntvRVGGETLRAKR---IFINTGARAA---IPPIPG--LDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 495 ----NDVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEehftYMALVRR-LIALRIPMYLD 568
Cdd:PRK06370 157 gyltNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGpRLLPREDED----VAAAVREiLEREGIDVRLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 569 TSVREITGAG----VVLDFGGETFHLLADTVVLAIGAVP---DSGLADAveGLA-----------------PEVYRIGDC 624
Cdd:PRK06370 233 AECIRVERDGdgiaVGLDCNGGAPEITGSHILVAVGRVPntdDLGLEAA--GVEtdargyikvddqlrttnPGIYAAGDC 310
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
366-414 |
1.22e-05 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 48.33 E-value: 1.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1490726401 366 PFLYREARSALVAAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERD 414
Cdd:PRK08132 7 KFPYRPHADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDD 55
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
382-454 |
1.25e-05 |
|
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: 47.93 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490726401 382 PKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGqwkiACampgkegyAAFVDYLRRCLGEHGVRVFLG 454
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG----RA--------RSFPDPDTGLPIDNGQHVLLG 63
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
384-418 |
1.97e-05 |
|
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: 47.24 E-value: 1.97e-05
10 20 30
....*....|....*....|....*....|....*
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLG 418
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
382-618 |
2.23e-05 |
|
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: 47.13 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 382 PKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGqwKIACAM-------PGKEGYAAFVDYLRRCLGEHGvrvfLG 454
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG--LIRTVEvdgfridRGPHSFLTRDPEVLELLRELG----LG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 455 SevtrEVVLAENPDALVLATG---AVPQGLGVPVASG-----GRVVQANDVILGRVDVGKKVAVigGRF----LGMEL-- 520
Cdd:COG1232 75 D----ELVWPNTRKSYIYYGGklhPLPQGPLALLRSPllslaGKLRALLELLAPRRPPGEDESL--AEFvrrrFGREVye 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 521 -------------------AAW----LAEQGREVTLVSRGRLGGRKG--PEEHFTYM---------ALVRRLIALRIpmY 566
Cdd:COG1232 149 rlvepllegvyagdpdelsADWafprLKRLELEHGSLIKGALALRKGakAGEVFGYLrgglgtlveALAEALEAGEI--R 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1490726401 567 LDTSVREI--TGAGVVLDFG-GETFHllADTVVLAIGAVPdsgLADAVEGLAPEV 618
Cdd:COG1232 227 LGTRVTAIerEGGGWRVTTSdGETIE--ADAVVSATPAPA---LARLLAPLPPEV 276
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
507-580 |
2.24e-05 |
|
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: 42.96 E-value: 2.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726401 507 KVAVIGGRFLGMELAAWLAEQGREVTLVSRG-RLGGRKGPEehfTYMALVRRLIALRIPMYLDTSVREITGAGVV 580
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRdRLLPGFDPE---IAKILQEKLEKNGIEFLLNTTVEAIEGNGDG 72
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
460-625 |
2.99e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 46.84 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 460 EVVLAENpdaLVLATGAVPQGL-GVPVasGGRVVQANDVILGRVDVGKKVAVIGGRFLGMELAAWLAEQGREVTLVsrgr 538
Cdd:PRK06327 142 TVITAKH---VIIATGSEPRHLpGVPF--DNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTIL---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 539 lggrkgpEEHFTYMALVRRLIA-----------LRIPMYLDTSVREITGAGVVL---DFGGETFHLLADTVVLAIGAVPD 604
Cdd:PRK06327 213 -------EALPAFLAAADEQVAkeaakaftkqgLDIHLGVKIGEIKTGGKGVSVaytDADGEAQTLEVDKLIVSIGRVPN 285
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490726401 605 S-GL-ADAVeGLA-----------------PEVYRIGDCV 625
Cdd:PRK06327 286 TdGLgLEAV-GLKldergfipvddhcrtnvPNVYAIGDVV 324
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
387-413 |
5.34e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.81 E-value: 5.34e-05
10 20
....*....|....*....|....*..
gi 1490726401 387 VVGGGPAGMQAAALLAQRGHRVSLHER 413
Cdd:COG2081 2 VIGAGAAGLMAAITAAERGARVLLLEK 28
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
383-418 |
5.88e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.03 E-value: 5.88e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLG 418
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
380-513 |
6.13e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 46.17 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 380 PSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQwkIACAMPGKEGYAAFVDYLRRCLGEHGVRVFLGSEVTR 459
Cdd:PRK12809 308 PRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGM--LTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGR 385
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726401 460 EVV---LAENPDALVLATG---------------AVPQGLGVPVASGGRVV---QANDVILGRVDvGKKVAVIGG 513
Cdd:PRK12809 386 DITfsdLTSEYDAVFIGVGtygmmradlphedapGVIQALPFLTAHTRQLMglpESEEYPLTDVE-GKRVVVLGG 459
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
379-419 |
6.37e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 46.04 E-value: 6.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1490726401 379 APSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGG 419
Cdd:PRK07208 1 MTNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
378-492 |
3.19e-04 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 43.58 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWKIACAMP--GKEGYAAFVDYLRRCLGEHGVRVFLGS 455
Cdd:COG1252 145 ERRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEAGPriLPGLGEKLSEAAEKELEKRGVEVHTGT 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1490726401 456 EVTR----EVVLAENP----DALVLATGA----VPQGLGVPVASGGRVV 492
Cdd:COG1252 225 RVTEvdadGVTLEDGEeipaDTVIWAAGVkappLLADLGLPTDRRGRVL 273
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
381-419 |
3.31e-04 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 43.57 E-value: 3.31e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1490726401 381 SPKKVMVVGGGPAGMQAAALLAQRgHRVSLHERDTDLGG 419
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-459 |
3.44e-04 |
|
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: 39.49 E-value: 3.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSL-HERDTDLGGQwkiacampGKEGYAAFVDYLRrclgEHGVRVFLGSEVTR 459
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVvERRDRLLPGF--------DPEIAKILQEKLE----KNGIEFLLNTTVEA 65
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
384-576 |
4.53e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 42.74 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 384 KVMVVGGGPAGMqAAALLAQRGHRVSLHERDTDLGGQWKIACAM---PGKEGYAAFVDYLRRcLGEHGVRvfLGSEV--- 457
Cdd:PRK10262 8 KLLILGSGPAGY-TAAVYAARANLQPVLITGMEKGGQLTTTTEVenwPGDPNDLTGPLLMER-MHEHATK--FETEIifd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 458 -TREVVLAENP------------DALVLATGAVPQGLGVPV--ASGGRVVQANDVILGRVDVGKKVAVIGGRFLGMELAA 522
Cdd:PRK10262 84 hINKVDLQNRPfrltgdsgeytcDALIIATGASARYLGLPSeeAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEAL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490726401 523 WLAEQGREVTLVSRgRLGGRKgpeEHFTYMALVRRLIALRIPMYLDTSVREITG 576
Cdd:PRK10262 164 YLSNIASEVHLIHR-RDGFRA---EKILIKRLMDKVENGNIILHTNRTLEEVTG 213
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
385-421 |
6.01e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 42.60 E-value: 6.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQW 421
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
383-492 |
8.05e-04 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 42.03 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQwkiacampgkegyaafvDYLRRCLGEH-GVRVFLGSEVTR-- 459
Cdd:COG0492 142 KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS-----------------KILVERLRANpKIEVLWNTEVTEie 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1490726401 460 ------EVVLAENP---------DALVLATGAVP-----QGLGVPVASGGRVV 492
Cdd:COG0492 205 gdgrveGVTLKNVKtgeekelevDGVFVAIGLKPntellKGLGLELDEDGYIV 257
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
157-323 |
9.89e-04 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 41.78 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 157 EAARRASEAGADAVELHachgclvSTFLSPVTNRRNDAYGGTVEKRARFA-------------------VRIVQRMRDKV 217
Cdd:PRK07565 28 DNVKRLEDAGAGAVVLK-------SLFEEQIRHEAAELDRHLTHGTESFAealdyfpepakfyvgpeeyLELIRRAKEAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 218 GsgFPVSVRMNGTddvegglTVDEAVLQARILEAAGADAvsvsggIEcwspLNIpcYLFPKGP----------MVSLAEA 287
Cdd:PRK07565 101 D--IPVIASLNGS-------SAGGWVDYARQIEQAGADA------LE----LNI--YYLPTDPdisgaeveqrYLDILRA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490726401 288 VKKAVRIPVIVagKID------AELAEQIIGSGRADFVALGR 323
Cdd:PRK07565 160 VKSAVSIPVAV--KLSpyfsnlANMAKRLDAAGADGLVLFNR 199
|
|
| TrmFO |
COG1206 |
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ... |
383-412 |
1.00e-03 |
|
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440819 Cd Length: 436 Bit Score: 41.97 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|
gi 1490726401 383 KKVMVVGGGPAGMQAAALLAQRGHRVSLHE 412
Cdd:COG1206 2 KPVTVIGGGLAGSEAAWQLAERGVPVRLYE 31
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
379-421 |
1.14e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 41.77 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1490726401 379 APSP---KKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQW 421
Cdd:PLN02172 4 AQNPinsQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLW 49
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
385-410 |
1.27e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 41.43 E-value: 1.27e-03
10 20
....*....|....*....|....*.
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSL 410
Cdd:PRK07494 10 IAVIGGGPAGLAAAIALARAGASVAL 35
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
381-412 |
1.37e-03 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 41.67 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|..
gi 1490726401 381 SPKKVMVVGGGPAGMQAAALLAQRGHRVSLHE 412
Cdd:PRK05335 1 MMKPVNVIGAGLAGSEAAWQLAKRGVPVELYE 32
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
505-542 |
1.41e-03 |
|
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: 41.38 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1490726401 505 GKKVAVIGGRFLGMELAAWLAEQGREVTLV-SRGRLGGR 542
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLeARPRLGGR 41
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
385-470 |
1.51e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 41.65 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQWKIACA---MPG-KEGYAAFVD--------YLRRCLGEHgvrvf 452
Cdd:PRK12843 19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGttwIPGtRHGLAVGPDdsleaartYLDALVGDR----- 93
|
90
....*....|....*...
gi 1490726401 453 lGSEVTREVVLAENPDAL 470
Cdd:PRK12843 94 -SPEELRDAFLASGPRAI 110
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
382-492 |
1.85e-03 |
|
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: 41.23 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 382 PKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLggqwkiacaMPGKEgyAAFVDYLRRCLGEHGVRVFLGSEVTR-- 459
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRL---------LPGED--PEISEALEKALEKEGIDILTGAKVTSve 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1490726401 460 -------------EVVLAENPDALVLATGAVP--QGL-----GVPVASGGRVV 492
Cdd:COG1249 237 ktgdgvtvtledgGGEEAVEADKVLVATGRRPntDGLgleaaGVELDERGGIK 289
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
385-417 |
2.06e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 41.05 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|...
gi 1490726401 385 VMVVGGGPAGMQAAALLAQRGHRVSLHERDTDL 417
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
382-454 |
3.01e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 40.55 E-value: 3.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726401 382 PK-KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLGGQwkiacampgkegYAAFVDylRRclGEH---GVRVFLG 454
Cdd:PLN02487 74 PKlKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGK------------VGSFVD--KN--GNHiemGLHVFFG 134
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
246-398 |
3.29e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 40.09 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 246 ARILEAAGADAVSVSGGiEC-----WSPLnipcylfpkGPMVsLAEAVKKAVRIPVIVAGKidaelaeqiIGSGR----- 315
Cdd:COG2070 117 ARKAEKAGADAVVAEGA-EAgghrgADEV---------STFA-LVPEVRDAVDIPVIAAGG---------IADGRgiaaa 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 316 ----ADFVALG-RPLL-----ADPELPNKLRQGRVDHVRRciycnnCERQLGSPASCTVNPFLYR-EARSALVAAPSPKK 384
Cdd:COG2070 177 lalgADGVQMGtRFLAteespAHEAYKQALVDAKEEDTVL------TRSFTGRPARALRNSFTREgLDLEAECLYPILEA 250
|
170
....*....|....
gi 1490726401 385 VMVVGGGPAGMQAA 398
Cdd:COG2070 251 LTAGKRLRAAAAEG 264
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
431-603 |
3.64e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 40.14 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 431 EGYAAFVDylrrclgEHGVrvflgsEVTREVVLAENpdaLVLATGAVPQGLGVPvasGGRVVQANDVILGRVDVGKKVAV 510
Cdd:PRK06116 112 EGFARFVD-------AHTV------EVNGERYTADH---ILIATGGRPSIPDIP---GAEYGITSDGFFALEELPKRVAV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 511 IGGRFLGMELAAWLAEQGREVTLVSRGRLggrkgPEEHFTYM---ALVRRLIALRIPMYLDTSVREI--TGAG---VVLD 582
Cdd:PRK06116 173 VGAGYIAVEFAGVLNGLGSETHLFVRGDA-----PLRGFDPDireTLVEEMEKKGIRLHTNAVPKAVekNADGsltLTLE 247
|
170 180
....*....|....*....|.
gi 1490726401 583 fGGETfhLLADTVVLAIGAVP 603
Cdd:PRK06116 248 -DGET--LTVDCLIWAIGREP 265
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
387-418 |
3.91e-03 |
|
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: 39.89 E-value: 3.91e-03
10 20 30
....*....|....*....|....*....|..
gi 1490726401 387 VVGGGPAGMQAAALLAQRGHRVSLHERDTDLG 418
Cdd:TIGR00275 2 IIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
380-416 |
3.94e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 39.86 E-value: 3.94e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1490726401 380 PSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTD 416
Cdd:PRK06847 2 AAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPE 38
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
384-417 |
4.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 39.67 E-value: 4.33e-03
10 20 30
....*....|....*....|....*....|....
gi 1490726401 384 KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDL 417
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
506-587 |
5.13e-03 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 39.20 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 506 KKVAVIGG-RFLGMELAAWLAEQGREVTLVSRGRLGGRKGPEehftymalVRRLIALRipmYLDTSVREITGAG---VVL 581
Cdd:cd05265 1 MKILIIGGtRFIGKALVEELLAAGHDVTVFNRGRTKPDLPEG--------VEHIVGDR---NDRDALEELLGGEdfdVVV 69
|
....*.
gi 1490726401 582 DFGGET 587
Cdd:cd05265 70 DTIAYT 75
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
148-323 |
5.43e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 38.72 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 148 IERYVEDFSEAARRASEAGADAVELHACHGclvstflspvtnrrndayggtveKRARFAVRIVQRMRDKVGsGFPVSVRM 227
Cdd:cd04722 66 INDAAAAVDIAAAAARAAGADGVEIHGAVG-----------------------YLAREDLELIRELREAVP-DVKVVVKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 228 NGTDDVEggltvdeavlqARILEAAGADAVSVSGGIecwsplNIPCYLFPKGPMVSLAEAVKKAVRIPVIVAGKI-DAEL 306
Cdd:cd04722 122 SPTGELA-----------AAAAEEAGVDEVGLGNGG------GGGGGRDAVPIADLLLILAKRGSKVPVIAGGGInDPED 184
|
170
....*....|....*..
gi 1490726401 307 AEQIIGSGrADFVALGR 323
Cdd:cd04722 185 AAEALALG-ADGVIVGS 200
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
370-416 |
5.90e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 39.74 E-value: 5.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1490726401 370 REARSALVAAPSPK------KVMVVGGGPAGMQAAALLAQRGHRVSLHERDTD 416
Cdd:PLN00093 21 RPGLRVLAAAASKKlsgrklRVAVIGGGPAGACAAETLAKGGIETFLIERKLD 73
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
207-298 |
8.48e-03 |
|
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.
Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 38.68 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 207 VRIVQRMRDKVGSGFPVSVrmnGTddveGGLTVDEAVLQARILEAAGADAVSVsggiecwsplnIPCYLFPKGP--MVSL 284
Cdd:cd00408 53 KEVIEAVVEAVAGRVPVIA---GV----GANSTREAIELARHAEEAGADGVLV-----------VPPYYNKPSQegIVAH 114
|
90
....*....|....
gi 1490726401 285 AEAVKKAVRIPVIV 298
Cdd:cd00408 115 FKAVADASDLPVIL 128
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
369-459 |
9.01e-03 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 38.74 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 369 YREARSALVAApspKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLggqwkIACAMPgkegyaAFVDY-LRRCLGEH 447
Cdd:PRK04965 131 YRAAETQLRDA---QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL-----LASLMP------PEVSSrLQHRLTEM 196
|
90
....*....|..
gi 1490726401 448 GVRVFLGSEVTR 459
Cdd:PRK04965 197 GVHLLLKSQLQG 208
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
378-418 |
9.19e-03 |
|
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: 39.06 E-value: 9.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1490726401 378 AAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLG 418
Cdd:PRK01747 256 GSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
366-475 |
9.59e-03 |
|
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: 38.51 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726401 366 PFLYREARSALVAAPSPKKVMVVGGGPAGMQAAALLAQRGHRVSLHERDTDLggqwkiacampgkegyaafVDYLRrclg 445
Cdd:COG0569 79 LEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPER-------------------VERLA---- 135
|
90 100 110
....*....|....*....|....*....|....
gi 1490726401 446 EHGVRVFLGSeVTREVVL----AENPDALVLATG 475
Cdd:COG0569 136 EEDVLVIVGD-ATDEEVLeeagIEDADAVIAATG 168
|
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| |
