|
Name |
Accession |
Description |
Interval |
E-value |
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
7-345 |
6.13e-154 |
|
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: 448.99 E-value: 6.13e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRRLRLANRIVSTSHEPAYSEDGLPKGRYRRYHVEKARGGVGLTMIGGSAVVSRDSPpAFGNLQLHRDEIVPWL 86
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSP-AFGNLNASDDEIIPGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 87 RELTDAVHEHGTAVMCQVTHLGRRSsNFTGDWLPLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQRCVAAGLDGI 166
Cdd:cd04734 80 RRLAEAVHAHGAVIMIQLTHLGRRG-DGDGSWLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 167 ELQ-SYGHLLDSFLSPRTN----PDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEGLAAARCYL 241
Cdd:cd04734 159 ELQaAHGHLIDQFLSPLTNrrtdEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 242 ADG-IDFLSTIKGTIDSDAALARVIPPMGAPSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGMLDLVGMTRAH 320
Cdd:cd04734 239 AEGlIDYVNVSAGSYYTLLGLAHVVPSMGMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAH 318
|
330 340
....*....|....*....|....*
gi 521989364 321 LADPHLVAKIRAGQEDRIRPCVGAS 345
Cdd:cd04734 319 IADPHLVAKAREGREDDIRPCIGCN 343
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-367 |
6.25e-118 |
|
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: 357.17 E-value: 6.25e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 1 MREDDPLLRPYHLRRLRLANRIVSTSHEPAYS-EDGLPKGRYRRYHVEKARGGVGLTMIGGSAVvSRDSPPAFGNLQLHR 79
Cdd:COG1902 1 MMKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAdEDGVPTDLHAAYYAQRARGGAGLIITEATAV-SPEGRGYPGQPGIWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 80 DEIVPWLRELTDAVHEHGTAVMCQVTHLGRRSSNFTGDWLPLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQRCV 159
Cdd:COG1902 80 DEQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 160 AAGLDGIELQ-SYGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEGL 234
Cdd:COG1902 160 EAGFDGVEIHgAHGYLLDQFLSPLTNqrTDeyGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 235 AAARCYLADGIDFLSTIKGTIDSDAAlarviPPMGAPSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGMLDLV 314
Cdd:COG1902 240 ELAKALEEAGVDYLHVSSGGYEPDAM-----IPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 521989364 315 GMTRAHLADPHLVAKIRAGQEDRIRPCVGASYCLDAIYsdGAAKCVHNPATGR 367
Cdd:COG1902 315 ALGRPLLADPDLPNKAAAGRGDEIRPCIGCNQCLPTFY--GGASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
10-333 |
8.55e-82 |
|
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: 262.12 E-value: 8.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 10 PYHLRRLRLANRIVSTSHEPAYS-EDGLPKGRYRRYHVEKARGGVGLTMIGGSAVvSRDSPPAFGNLQLHRDEIVPWLRE 88
Cdd:cd02803 3 PIKIGGLTLKNRIVMAPMTENMAtEDGTPTDELIEYYEERAKGGVGLIITEAAYV-DPEGKGYPGQLGIYDDEQIPGLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 89 LTDAVHEHGTAVMCQVTHLGRRS-SNFTGDwlPLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQRCVAAGLDGIE 167
Cdd:cd02803 82 LTEAVHAHGAKIFAQLAHAGRQAqPNLTGG--PPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 168 LQ-SYGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEGLAAARCYLA 242
Cdd:cd02803 160 IHgAHGYLLSQFLSPYTNkrTDeyGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 243 DGIDFLSTIKGTIDSdaaLARVIPPMGAPSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGMLDLVGMTRAHLA 322
Cdd:cd02803 240 AGVDALHVSGGSYES---PPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLA 316
|
330
....*....|.
gi 521989364 323 DPHLVAKIRAG 333
Cdd:cd02803 317 DPDLPNKAREG 327
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
7-363 |
7.01e-61 |
|
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: 207.52 E-value: 7.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRRLRLANRIVSTSHEPAYSEDGLPKGRYRRYHVEKARGGVGLTMIGGSAVVSRDSPPAFGNLqLHRDEIVPWL 86
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPV-LNSPRQAAGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 87 RELTDAVHEHGTAVMCQVTHLGRRSsnFTGDwlpLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQRCVAAGLDGI 166
Cdd:cd02930 80 RLITDAVHAEGGKIALQILHAGRYA--YHPL---CVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 167 ELQ-SYGHLLDSFLSPRTNPD----GGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEGLAAARCYL 241
Cdd:cd02930 155 EIMgSEGYLINQFLAPRTNKRtdewGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 242 ADGIDFLSTIKGTIDSDaalarvIPPMGA--PSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGMLDLVGMTRA 319
Cdd:cd02930 235 AAGADILNTGIGWHEAR------VPTIATsvPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 521989364 320 HLADPHLVAKIRAGQEDRIRPCVGASY-CLDAIYSDGAAKCVHNP 363
Cdd:cd02930 309 FLADPDFVAKAAAGRADEINTCIACNQaCLDHIFTGQRASCLVNP 353
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
7-327 |
9.00e-47 |
|
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: 168.83 E-value: 9.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRRLRLANRIVsTSHEPAYS-EDGLPkGRYRRYH-VEKARGGVGLTMIGGSAVV--SRDSPpafGNLQLHRDEI 82
Cdd:cd02932 1 LFTPLTLRGVTLKNRIV-VSPMCQYSaEDGVA-TDWHLVHyGSRALGGAGLVIVEATAVSpeGRITP---GDLGLWNDEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 83 VPWLRELTDAVHEHGTAVMCQVTHLGRRSSN-------------FTGDWlPLVHPSPQREPAHRSVPKIAEPWDLERILA 149
Cdd:cd02932 76 IEALKRIVDFIHSQGAKIGIQLAHAGRKASTappwegggpllppGGGGW-QVVAPSAIPFDEGWPTPRELTREEIAEVVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 150 DYVSAAQRCVAAGLDGIELQS-YGHLLDSFLSP----RTNPDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESC 224
Cdd:cd02932 155 AFVAAARRAVEAGFDVIEIHAaHGYLLHQFLSPlsnkRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 225 AGGLPLAEGLAAARCYLADGIDFLSTIKGTIDSDAAlarvIPPmgAPSAPfLEFTAAVKRELGIPVMHAARIADVATARH 304
Cdd:cd02932 235 EGGWDLEDSVELAKALKELGVDLIDVSSGGNSPAQK----IPV--GPGYQ-VPFAERIRQEAGIPVIAVGLITDPEQAEA 307
|
330 340
....*....|....*....|...
gi 521989364 305 AVAEGMLDLVGMTRAHLADPHLV 327
Cdd:cd02932 308 ILESGRADLVALGRELLRNPYWP 330
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
7-333 |
8.53e-45 |
|
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: 163.52 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLR-RLRLANRIV-STSHEPAYSEDGLPKGR----YRRYhvekARGGVGLTMIGGSAVVSR--DSPPAFGNLQLH 78
Cdd:cd04733 1 LGQPLTLPnGATLPNRLAkAAMSERLADGRGLPTPElirlYRRW----AEGGIGLIITGNVMVDPRhlEEPGIIGNVVLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 79 RDEIVPWLRELTDAVHEHGTAVMCQVTHLGRRSSNF--TGDWLPLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQ 156
Cdd:cd04733 77 SGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPAGlnQNPVAPSVALDPGGLGKLFGKPRAMTEEEIEDVIDRFAHAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 157 RCVAAGLDGIELQS-YGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLA 231
Cdd:cd04733 157 LAQEAGFDGVQIHAaHGYLLSQFLSPLTNkrTDeyGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 232 EGLAAARCYLADGIDFLSTIKGTIDSDAALARVIPPMGAPSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGML 311
Cdd:cd04733 237 DALEVVEALEEAGVDLVELSGGTYESPAMAGAKKESTIAREAYFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASGAV 316
|
330 340
....*....|....*....|..
gi 521989364 312 DLVGMTRAHLADPHLVAKIRAG 333
Cdd:cd04733 317 DGIGLARPLALEPDLPNKLLAG 338
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
6-336 |
1.45e-44 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 163.00 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 6 PLLRPYHLRRLRLANRIV--STSHEPAYSEDGLPKGRYRRYHVEKARGGVGLtMIGGSAVVSRDSPPAFGNLQLHRDEIV 83
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVmaPMTRLRSLDDGTKATGLLAEYYSQRSRGPGTL-IITEGAFVNPQSGGFDNGPRIWDDEQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 84 PWLRELTDAVHEHGTAVMCQVTHLGRRSSNFTGDWLPLVHPSP---QREPAHRSVPKIAE--PWDLERILADYVSAAQRC 158
Cdd:pfam00724 80 EGWRKLTEAVHKNGSKAGVQLWHLGREAPMEYRPDLEVDGPSDpfaLGAQEFEIASPRYEmsKEEIKQHIQDFVDAAKRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 159 VAAGLDGIEL-QSYGHLLDSFLSPRTN----PDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEG 233
Cdd:pfam00724 160 REAGFDGVEIhGANGYLINQFLSPGTNqrtdEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 234 LAAARCYLADGIDFLSTIKGtidsdaALARVIPPMGAPSAPFL----EFTAAVKRELGIPVMHAARIADVATARHAVAEG 309
Cdd:pfam00724 240 AQFIYLLAELGVRLPDGWHL------AYIHAIEPRPRGAGPVRtrqqHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKG 313
|
330 340
....*....|....*....|....*..
gi 521989364 310 MLDLVGMTRAHLADPHLVAKIRAGQED 336
Cdd:pfam00724 314 RADLVAMGRPFLADPDLPFKAKKGRPL 340
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
7-363 |
1.40e-40 |
|
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: 152.66 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRRLRLANRIVSTSHEPA--YSEDGLPKGRYRRYHVEKARGGVGLTMIGGSAV---VSRDSPPAFGNLQLHRDE 81
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPLglADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVdneIEQFPMPSLPCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 82 IVPWLRELTDAVHEHGTAVMCQVTH-LGRRS-SNFTGDWLPlVHPSPQrepAHRSVPKIA----EPWDLERILADYVSAA 155
Cdd:cd02931 81 FIRTAKEMTERVHAYGTKIFLQLTAgFGRVCiPGFLGEDKP-VAPSPI---PNRWLPEITcrelTTEEVETFVGKFGESA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 156 QRCVAAGLDGIELQSY--GHLLD----SFLSPRTNPDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCA---- 225
Cdd:cd02931 157 VIAKEAGFDGVEIHAVheGYLLDqftiSLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSVKSYIKdlrq 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 226 GGLP----------LAEGLAAARCYLADGIDFLSTIKGTIDsdaALARVIPPMGAPSAPFLEFTAAVKRELGIPVMHAAR 295
Cdd:cd02931 237 GALPgeefqekgrdLEEGLKAAKILEEAGYDALDVDAGSYD---AWYWNHPPMYQKKGMYLPYCKALKEVVDVPVIMAGR 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521989364 296 IADVATARHAVAEGMLDLVGMTRAHLADPHLVAKIRAGQEDRIRPCVGASY-CLDAIYSDGAAKCVHNP 363
Cdd:cd02931 314 MEDPELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDgCLGRMALGGNLSCAVNP 382
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
7-340 |
2.47e-36 |
|
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: 140.15 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRRLRLANRIVSTSHEPAYSEDGLPKGRYRRYHVEKARGGVGLTMIGGSAvVSRDSPPAFGNL-QLHRDEIVPW 85
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTA-VDHPAASGDPNVpRFHGEDALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 86 LRELTDAVHEHGTAVMCQVTHLG--RRSSNFTGDWLPLVHPSPQREPAHRSVPKIAEPwDLERILADYVSAAQRCVAAGL 163
Cdd:cd04747 80 WKKVVDEVHAAGGKIAPQLWHVGamRKLGTPPFPDVPPLSPSGLVGPGKPVGREMTEA-DIDDVIAAFARAAADARRLGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 164 DGIELQ-SYGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLA---EGLA 235
Cdd:cd04747 159 DGIELHgAHGYLIDQFFWAGTNrrADgyGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTARLAdtpDELE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 236 AARCYLAD-GIDFLstikgtidsDAALARVIPPMGAPSApfLEFTAAVKRELGIPVM------------HAARIADVA-T 301
Cdd:cd04747 239 ALLAPLVDaGVDIF---------HCSTRRFWEPEFEGSE--LNLAGWTKKLTGLPTItvgsvgldgdfiGAFAGDEGAsP 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 521989364 302 ARHAVAEGML-----DLVGMTRAHLADPHLVAKIRAGQEDRIRP 340
Cdd:cd04747 308 ASLDRLLERLergefDLVAVGRALLSDPAWVAKVREGRLDELIP 351
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
6-325 |
3.29e-36 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 145.47 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 6 PLLRPYHLRRLRLANRIVsTSHEPAYS-EDGLPkGRYRRYHV-EKARGGVGLTMIGGSAVvSRDSPPAFGNLQLHRDEIV 83
Cdd:PRK08255 398 PMFTPFRLRGLTLKNRVV-VSPMAMYSaVDGVP-GDFHLVHLgARALGGAGLVMTEMTCV-SPEGRITPGCPGLYNDEQE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 84 PWLRELTDAVHEHGTAVMC-QVTHLGRRSSNF-----------TGDWlPLVHPSPQREPAHRSVPKIAEPWDLERILADY 151
Cdd:PRK08255 475 AAWKRIVDFVHANSDAKIGiQLGHSGRKGSTRlgwegidepleEGNW-PLISASPLPYLPGSQVPREMTRADMDRVRDDF 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 152 VSAAQRCVAAGLDGIELQ-SYGHLLDSFLSP----RTNPDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAG 226
Cdd:PRK08255 554 VAAARRAAEAGFDWLELHcAHGYLLSSFISPltnqRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEG 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 227 GLPLAEGLAAARCYLADGIDFLSTIKGTIDSDAAlarviPPMG----APsapfleFTAAVKRELGIPVMHAARIADVATA 302
Cdd:PRK08255 634 GNTPDDAVEIARAFKAAGADLIDVSSGQVSKDEK-----PVYGrmyqTP------FADRIRNEAGIATIAVGAISEADHV 702
|
330 340
....*....|....*....|...
gi 521989364 303 RHAVAEGMLDLVGMTRAHLADPH 325
Cdd:PRK08255 703 NSIIAAGRADLCALARPHLADPA 725
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
7-339 |
2.05e-32 |
|
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: 128.87 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 7 LLRPYHLRR-LRLANRIV-------STSHEPAYSEDGLpkgryrRYHVEKArGGVGLTmIGGSAVVSRDSPPAFGNLQLH 78
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVmapmttySSNPDGTITDDEL------AYYQRRA-GGVGMV-ITGATYVSPSGIGFEGGFSAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 79 RDEIVPWLRELTDAVHEHGTAVMCQVTHLGRRS-SNFTGDwLPLVHPSPQREPAHRSVP----KIAEpwdLERILADYVS 153
Cdd:cd04735 73 DDSDIPGLRKLAQAIKSKGAKAILQIFHAGRMAnPALVPG-GDVVSPSAIAAFRPGAHTprelTHEE---IEDIIDAFGE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 154 AAQRCVAAGLDGIELQS-YGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVG----PEFIVGIRMALDESC 224
Cdd:cd04735 149 ATRRAIEAGFDGVEIHGaNGYLIQQFFSPHSNrrTDewGGSLENRMRFPLAVVKAVQEVIDkhadKDFILGYRFSPEEPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 225 AGGLPLAEGLaaarcYLAD-----GIDFLSTIKGTIDSdaaLARVIPPMGAPSAPfleftaAVKRELG--IPVMHAARIA 297
Cdd:cd04735 229 EPGIRMEDTL-----ALVDkladkGLDYLHISLWDFDR---KSRRGRDDNQTIME------LVKERIAgrLPLIAVGSIN 294
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 521989364 298 DVATARHAVAEGmLDLVGMTRAHLADPHLVAKIRAGQEDRIR 339
Cdd:cd04735 295 TPDDALEALETG-ADLVAIGRGLLVDPDWVEKIKEGREDEIN 335
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
6-333 |
6.86e-31 |
|
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: 123.74 E-value: 6.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 6 PLLRPYHLRRLRLANRIVstsHEP-----AySEDGLPKGRYRRYHVEkaRGGVGLtMIGGSAVVSRDSPPAFGNLQLHRD 80
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIV---MAPltrsrA-DPDGVPTDLMAEYYAQ--RASAGL-IITEATQISPQGQGYPNTPGIYTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 81 EIVPWLRELTDAVHEHGTAVMCQVTHLGRRS-SNFTGDWLPLVHPSPQREPAHR---------SVPKIAEPWDLERILAD 150
Cdd:cd02933 74 EQVEGWKKVTDAVHAKGGKIFLQLWHVGRVShPSLLPGGAPPVAPSAIAAEGKVftpagkvpyPTPRALTTEEIPGIVAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 151 YVSAAQRCVAAGLDGIEL-QSYGHLLDSFLSPRTN--PD--GGSLEERMAFPRRVITAVRAAVGPEFiVGIRMA-----L 220
Cdd:cd02933 154 FRQAARNAIEAGFDGVEIhGANGYLIDQFLRDGSNkrTDeyGGSIENRARFLLEVVDAVAEAIGADR-VGIRLSpfgtfN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 221 DESCAGGLPLAEGLAAArcyLAD-GIDFLSTIKGtidsdaalarviPPMGAPSAPFLEFTAAVKRELGIPVMHAARIaDV 299
Cdd:cd02933 233 DMGDSDPEATFSYLAKE---LNKrGLAYLHLVEP------------RVAGNPEDQPPDFLDFLRKAFKGPLIAAGGY-DA 296
|
330 340 350
....*....|....*....|....*....|....
gi 521989364 300 ATARHAVAEGMLDLVGMTRAHLADPHLVAKIRAG 333
Cdd:cd02933 297 ESAEAALADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
59-368 |
7.80e-30 |
|
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: 121.69 E-value: 7.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 59 GGSAVV----------SRDSPpaFGNLQLHRDEIVPWLRELTDAVHEHGTAVMCQVTHLGRRSSNFTGDWLPLVhPS--P 126
Cdd:cd02929 50 GGWGVVnteqcsihpsSDDTP--RISARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESRETPLG-PSqlP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 127 QREPAHRSV-PKIAEPWDLERILADYVSAAQRCVAAGLDGIEL-QSYGHLLDSFLSP----RTNPDGGSLEERMAFPRRV 200
Cdd:cd02929 127 SEFPTGGPVqAREMDKDDIKRVRRWYVDAALRARDAGFDIVYVyAAHGYLPLQFLLPrynkRTDEYGGSLENRARFWRET 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 201 ITAVRAAVGPEFIVGIRMALDESCA-GGLPL-AEGLAAARcYLADGIDFLSTIKGTIDSDAALARVIPPmgAPSAPFLEF 278
Cdd:cd02929 207 LEDTKDAVGDDCAVATRFSVDELIGpGGIESeGEGVEFVE-MLDELPDLWDVNVGDWANDGEDSRFYPE--GHQEPYIKF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 279 taaVKRELGIPVMHAARIADVATARHAVAEGMLDLVGMTRAHLADPHLVAKIRAGQEDRIRPCVGASYCldaIYSDGAA- 357
Cdd:cd02929 284 ---VKQVTSKPVVGVGRFTSPDKMVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCNIC---ISGDEGGv 357
|
330
....*....|...
gi 521989364 358 --KCVHNPATGRE 368
Cdd:cd02929 358 pmRCTQNPTAGEE 370
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
6-331 |
4.10e-24 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 104.94 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 6 PLLRPYHLRRLRLANRIVSTSHEPAYSEDGLPKGRYRRYHVEKARGGvGLTMIGGSAVvsrdSP--PAFGNLQ-LHRDEI 82
Cdd:PLN02411 11 TLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLI----SPtaPGFPHVPgIYSDEQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 83 VPWLRELTDAVHEHGTAVMCQVTHLGRRSSN----------------FTGDWLPLVhpsPQREPAHRSVPKIAEPWDLER 146
Cdd:PLN02411 86 VEAWKKVVDAVHAKGSIIFCQLWHVGRASHQvyqpggaapisstnkpISERWRILM---PDGSYGKYPKPRALETSEIPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 147 ILADYVSAAQRCVAAGLDGIELQ-SYGHLLDSFL----SPRTNPDGGSLEERMAFPRRVITAVRAAVGPEFiVGIRM--A 219
Cdd:PLN02411 163 VVEHYRQAALNAIRAGFDGIEIHgAHGYLIDQFLkdgiNDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVRVspA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 220 LDESCA-GGLPLAEGLAAarcyladgIDFLSTIKGTIDSDAALARVIPPmgapsapflEFTAAVKRELGIP--------V 290
Cdd:PLN02411 242 IDHLDAtDSDPLNLGLAV--------VERLNKLQLQNGSKLAYLHVTQP---------RYTAYGQTESGRHgseeeeaqL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521989364 291 MHAARIADVAT-----------ARHAVAEGMLDLVGMTRAHLADPHLVAKIR 331
Cdd:PLN02411 305 MRTLRRAYQGTfmcsggftrelGMQAVQQGDADLVSYGRLFISNPDLVLRFK 356
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-616 |
4.35e-14 |
|
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: 73.51 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQE-PGGQLLLA---ARSPRRRDLLGIV-DWRVREAKQ-----AGVRLRF 453
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcPYGGCVLSkalLGAAEAPEIASLWaDLYKRKEEVvkklnNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 454 G-------------MLAEPEDIRAERP--DTVILATGGSPAR-------AFLGEGGELIEDTWDVLSGGTQaaGDVLVYd 511
Cdd:pfam07992 82 GtevvsidpgakkvVLEELVDGDGETItyDRLVIATGARPRLppipgveLNVGFLVRTLDSAEALRLKLLP--KRVVVV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 512 ehGA-NQALDAAEVLANAGARVRYATPERALAPDVGAMIAPGYLKVFAEHGVTTTLAERLVAVRRAEGRLRARLrseyaE 590
Cdd:pfam07992 159 --GGgYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVIL-----K 231
|
250 260
....*....|....*....|....*.
gi 521989364 591 HEHEITVDRVVTERGTLPNDELYFAL 616
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAA 257
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
368-580 |
1.37e-11 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 67.83 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 368 EGTLPhELSPIHGapRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAArsPRRRDLLGIVDWRVREAKQA 447
Cdd:PRK12814 182 ERYIP-ERAPKSG--KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGI--PRFRLPESVIDADIAPLRAM 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 448 GVRLR----FGMLAEPEDIRAERpDTVILATGGSPArAFLGEGGeliEDTWDVLSG---------GTQAA--GDVLVYDe 512
Cdd:PRK12814 257 GAEFRfntvFGRDITLEELQKEF-DAVLLAVGAQKA-SKMGIPG---EELPGVISGidflrnvalGTALHpgKKVVVIG- 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521989364 513 hGANQALDAAEVLANAGA--------RVRYATPerALAPDVGAMIApgylkvfaeHGVTTTLAERLVAVRRAEGRL 580
Cdd:PRK12814 331 -GGNTAIDAARTALRLGAesvtilyrRTREEMP--ANRAEIEEALA---------EGVSLRELAAPVSIERSEGGL 394
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
383-475 |
2.15e-11 |
|
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: 66.31 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlLL-----AARSPRRrdllgIVDWRVREAKQAGVRLRFGML- 456
Cdd:COG0493 122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG--LLrygipEFRLPKD-----VLDREIELIEALGVEFRTNVEv 194
|
90 100
....*....|....*....|..
gi 521989364 457 ---AEPEDIRAERpDTVILATG 475
Cdd:COG0493 195 gkdITLDELLEEF-DAVFLATG 215
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
383-488 |
2.39e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 66.36 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlLL-----AARSPRRrdllgIVDWRVREAKQAGVRLRFGML- 456
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLrygipEFRLPKD-----IVDREVERLLKLGVEIRTNTEv 213
|
90 100 110
....*....|....*....|....*....|....*
gi 521989364 457 ---AEPEDIRAERpDTVILATGGSPARaFLGEGGE 488
Cdd:PRK11749 214 grdITLDELRAGY-DAVFIGTGAGLPR-FLGIPGE 246
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
385-612 |
6.66e-11 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 63.99 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 385 IVVVGAGPAGLEAARVLGGRGHEVVLFEAGqEPGGQLllaARSPRRRDLLGIVDW--------RVRE-AKQAGVRLRFGM 455
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQL---ATTKEIENYPGFPEGisgpelaeRLREqAERFGAEILLEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 456 --------------LAEPEDIRAerpDTVILATGGSP-------ARAFLGEGgeliedtwdvLSggTQAAGDVLVY-DEH 513
Cdd:COG0492 79 vtsvdkddgpfrvtTDDGTEYEA---KAVIIATGAGPrklglpgEEEFEGRG----------VS--YCATCDGFFFrGKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 514 -----GANQALDAAEVLANAGARVRYATPERALAPDvGAMIApgylKVFAEHGVTTTLAERLVAVrRAEGRLRA-RLRSE 587
Cdd:COG0492 144 vvvvgGGDSALEEALYLTKFASKVTLIHRRDELRAS-KILVE----RLRANPKIEVLWNTEVTEI-EGDGRVEGvTLKNV 217
|
250 260
....*....|....*....|....*
gi 521989364 588 YAEHEHEITVDRVVTERGTLPNDEL 612
Cdd:COG0492 218 KTGEEKELEVDGVFVAIGLKPNTEL 242
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
382-453 |
8.47e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.16 E-value: 8.47e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLA---ARSPRRRDLLGivdwrVREAKQAGVRLRF 453
Cdd:PRK12770 18 GKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGipeFRIPIERVREG-----VKELEEAGVVFHT 87
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
383-489 |
9.63e-10 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 61.33 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlllaarsprrrdLL--GI---------VDWRVREAKQAGVRL 451
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG-------------LLryGIpdfklekevIDRRIELMEAEGIEF 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 521989364 452 RFGmlAE------PEDIRAERpDTVILATGGSPARAFLGEGGEL 489
Cdd:PRK12810 211 RTN--VEvgkditAEELLAEY-DAVFLGTGAYKPRDLGIPGRDL 251
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
380-489 |
2.82e-09 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 59.88 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 380 GAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlLLAARSPRRRDLLGIVDWRVREAKQAGVRLRFGML--- 456
Cdd:TIGR01316 131 STHKKVAVIGAGPAGLACASELAKAGHSVTVFEALHKPGG--VVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLvgk 208
|
90 100 110
....*....|....*....|....*....|....
gi 521989364 457 -AEPEDIRAERpDTVILATGGSPARAFLGEGGEL 489
Cdd:TIGR01316 209 tATLEELFSQY-DAVFIGTGAGLPKLMNIPGEEL 241
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
384-426 |
8.04e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 58.36 E-value: 8.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqllLAAR 426
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG---LAAS 40
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
383-530 |
1.48e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 57.96 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLL---LAARSPRRR---DLLGIVDwrvreakqAGVRLRFGMl 456
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRygiPAYRLPREVldaEIQRILD--------LGVEVRLGV- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 457 AEPEDIRAERP----DTVILATGGSPARAFL--GEGGELIEDTWDVL----SGGTQAAGD-VLVYDehGANQALDAAEVL 525
Cdd:PRK12771 209 RVGEDITLEQLegefDAVFVAIGAQLGKRLPipGEDAAGVLDAVDFLravgEGEPPFLGKrVVVIG--GGNTAMDAARTA 286
|
....*
gi 521989364 526 ANAGA 530
Cdd:PRK12771 287 RRLGA 291
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
382-612 |
2.97e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 56.30 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGH--EVVLFeaGQEPGG-----QL--LLAARSPRRRDLLGIVDWrvreAKQAGVRLR 452
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPdgEITVI--GAEPHPpynrpPLskVLAGETDEEDLLLRPADF----YEENGIDLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 453 FGMLAepEDIRAERP------------DTVILATGGSPARAFLgEGGEL--------IEDTW---DVLSGGTQAA---GD 506
Cdd:COG1251 75 LGTRV--TAIDRAARtvtladgetlpyDKLVLATGSRPRVPPI-PGADLpgvftlrtLDDADalrAALAPGKRVVvigGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 507 VLvydehganqALDAAEVLANAGARVRYATP-----ERALAPDVGAMIApgylKVFAEHGVTTTLAERLVAVRRAEGRLR 581
Cdd:COG1251 152 LI---------GLEAAAALRKRGLEVTVVERaprllPRQLDEEAGALLQ----RLLEALGVEVRLGTGVTEIEGDDRVTG 218
|
250 260 270
....*....|....*....|....*....|.
gi 521989364 582 ARLRSeyaehEHEITVDRVVTERGTLPNDEL 612
Cdd:COG1251 219 VRLAD-----GEELPADLVVVAIGVRPNTEL 244
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
384-488 |
6.55e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 55.90 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAA---RSPRRrdllgIVDWRVREAKQAGVRLRF----GML 456
Cdd:PRK12778 433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIpefRLPKK-----IVDVEIENLKKLGVKFETdvivGKT 507
|
90 100 110
....*....|....*....|....*....|...
gi 521989364 457 AEPEDIRAERPDTVILATG-GSParAFLGEGGE 488
Cdd:PRK12778 508 ITIEELEEEGFKGIFIASGaGLP--NFMNIPGE 538
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
385-601 |
1.40e-07 |
|
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: 54.32 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 385 IVVVGAGPAGLEAARVLGGRGHEVVLFEAGqEPGG----------QLLLAA----RSPRRRDLLGI------VDW----- 439
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGGtclnvgcipsKALLHAaevaHEARHAAEFGIsagapsVDWaalma 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 440 RVRE------------AKQAGVRLRFGM----------LAEPEDIRAERpdtVILATGGSPAR-AFLGEGGELIEDTWDV 496
Cdd:COG1249 85 RKDKvvdrlrggveelLKKNGVDVIRGRarfvdphtveVTGGETLTADH---IVIATGSRPRVpPIPGLDEVRVLTSDEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 497 LS-----------GGtqaagdvlvydehGAnQALDAAEVLANAGARV----RYATPERALAPDVGAMIApgylKVFAEHG 561
Cdd:COG1249 162 LEleelpkslvviGG-------------GY-IGLEFAQIFARLGSEVtlveRGDRLLPGEDPEISEALE----KALEKEG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 521989364 562 VTTTLAERLVAVRRAEGRLRARLRSEyaEHEHEITVDRVV 601
Cdd:COG1249 224 IDILTGAKVTSVEKTGDGVTVTLEDG--GGEEAVEADKVL 261
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
382-421 |
2.97e-07 |
|
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: 53.30 E-value: 2.97e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQL 421
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
380-419 |
8.39e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 51.85 E-value: 8.39e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 521989364 380 GAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGG 419
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
383-424 |
1.29e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 51.43 E-value: 1.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLA 424
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILIS 42
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
373-489 |
1.30e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 51.56 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 373 HELSPIHGAPR---RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAA---RSPRRrdllGIVDWRVREAKQ 446
Cdd:PRK12831 128 NGIDLSETEEKkgkKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIpefRLPKE----TVVKKEIENIKK 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 521989364 447 AGVRLR----FGMLAEPEDIRAERP-DTVILATG-GSParAFLGEGGEL 489
Cdd:PRK12831 204 LGVKIEtnvvVGKTVTIDELLEEEGfDAVFIGSGaGLP--KFMGIPGEN 250
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
84-605 |
1.81e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.41 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 84 PWLRELTDAVHehgtavmcQVTHLGRRSSNFTGDWLPLVHPSPQREPAHRSVPKIAEPWDLERILADYVSAAQRCVAAGL 163
Cdd:COG3321 867 PFQREDAAAAL--------LAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 164 DGIELQSYGHLLDSFLSPRTNPDGGSLEERMAFPRRVITAVRAAVGPEFIVGIRMALDESCAGGLPLAEGLAAARCYLAD 243
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 244 GIDFLSTIKGTIDSDAALARVIPPMGAPSAPFLEFTAAVKRELGIPVMHAARIADVATARHAVAEGMLDLVGMTRAHLAD 323
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 324 PHLVAKIRAGQEDRIRPCVGASYCLDAIYSDGAAKCVHNPATGREGTLPHELSPIHGAPRRIVVVGAGPAGLEAARVLGG 403
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 404 RGHEVVLFEAGqEPGGQLLLAARSPRRRDLLGIVDWRVREAKQAGVRLRFGMLAEPEDIRAERPDTVILATGGSPARAFL 483
Cdd:COG3321 1179 LALAAALAAAL-AGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 484 GEGGELIEDTWDVLSGGTQAAGDVLVYDEHGANQALDAAEVLANAGARVRYATPERALAPDVGAMIAPGYLKVFAEHGVT 563
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 521989364 564 TTLAERLVAVRRAEGRLRARLRSEYAEHEHEITVDRVVTERG 605
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
381-433 |
2.75e-06 |
|
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: 50.24 E-value: 2.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 521989364 381 APRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlllAARSPRRRDL 433
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG----RARSFPDPDT 50
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
382-487 |
3.12e-06 |
|
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: 49.62 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAARsprrrdllgivDWRVREAKQAGVRLRFG------- 454
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEIS-----------AALEKALEKNGVEVRLGtsvkeii 220
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 521989364 455 --------MLAEPEDIRAerpDTVILATGGSPARAFLGEGG 487
Cdd:pfam07992 221 gdgdgvevILKDGTEIDA---DLVVVAIGRRPNTELLEAAG 258
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
381-432 |
3.35e-06 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 49.49 E-value: 3.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 521989364 381 APRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLllaarSPRRRD 432
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRM-----ATRRLD 48
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
386-424 |
5.62e-06 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 49.28 E-value: 5.62e-06
10 20 30
....*....|....*....|....*....|....*....
gi 521989364 386 VVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLA 424
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGRKILIS 39
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
381-419 |
9.30e-06 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 48.57 E-value: 9.30e-06
10 20 30
....*....|....*....|....*....|....*....
gi 521989364 381 APRRIVVVGAGPAGLEAARVLGGRgHEVVLFEAGQEPGG 419
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
387-420 |
1.22e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 43.29 E-value: 1.22e-05
10 20 30
....*....|....*....|....*....|....
gi 521989364 387 VVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQ 420
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
383-427 |
1.49e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 47.92 E-value: 1.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGqlllAARS 427
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG----RART 44
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
383-481 |
1.98e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.93 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLL-LAARSPRRRDLLGIVDWRVREAKQ-AGVRLRFGmlAEPE 460
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPGLDCPQCILEPLIAEVEAnPNITVYTG--AEVE 218
|
90 100 110
....*....|....*....|....*....|....*....
gi 521989364 461 DI---------------RAERP---DTVILATGGSPARA 481
Cdd:COG1148 219 EVsgyvgnftvtikkgpREEIEievGAIVLATGFKPYDP 257
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
390-454 |
3.32e-05 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 46.11 E-value: 3.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521989364 390 AGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAARSPRRRDLL---GIVDWRVREAKQAGVRLRFG 454
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELeplGLDEPLERPVRGARFYSPGG 68
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
380-477 |
3.69e-05 |
|
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: 46.34 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 380 GAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQepggQLLLAARSPrrrdllgIVDWRVREAKQAGVRLRFGmlAEP 459
Cdd:COG0446 122 FKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAP----RLLGVLDPE-------MAALLEEELREHGVELRLG--ETV 188
|
90
....*....|....*...
gi 521989364 460 EDIRAERPDTVILATGGS 477
Cdd:COG0446 189 VAIDGDDKVAVTLTDGEE 206
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
384-419 |
5.66e-05 |
|
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: 46.01 E-value: 5.66e-05
10 20 30
....*....|....*....|....*....|....*.
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGG 419
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
383-420 |
9.43e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 46.01 E-value: 9.43e-05
10 20 30
....*....|....*....|....*....|....*...
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQ 420
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
383-475 |
9.45e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 45.53 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAArsPRRRDLLGIVDWRVREAKQAGVRLRFGMLAEP--- 459
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGI--PSYRLPDEALDKDIAFIEALGVKIHLNTRVGKdip 361
|
90
....*....|....*..
gi 521989364 460 -EDIRaERPDTVILATG 475
Cdd:PRK13984 362 lEELR-EKHDAVFLSTG 377
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
379-419 |
1.58e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.88 E-value: 1.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 521989364 379 HGAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGG 419
Cdd:PRK07208 1 MTNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-476 |
2.42e-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: 40.27 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEagqepggqlllaaRSPRRRDLLG--IVDWRVREAKQAGVRLRFGmlAEPED 461
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVE-------------RRDRLLPGFDpeIAKILQEKLEKNGIEFLLN--TTVEA 65
|
90
....*....|....*
gi 521989364 462 IRAERPDTVILATGG 476
Cdd:pfam00070 66 IEGNGDGVVVVLTDG 80
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
382-421 |
2.42e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 44.60 E-value: 2.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQL 421
Cdd:PLN02328 238 PANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRV 277
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
385-436 |
3.52e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 43.08 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 521989364 385 IVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQLLLAARSPRRRDLLGI 436
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGALSPRALEELDL 54
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
385-419 |
6.31e-04 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 43.03 E-value: 6.31e-04
10 20 30
....*....|....*....|....*....|....*
gi 521989364 385 IVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGG 419
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
385-419 |
8.46e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 41.69 E-value: 8.46e-04
10 20 30
....*....|....*....|....*....|....*.
gi 521989364 385 IVVVGAGPAGLEAARVLG-GRGHEVVLFEAGQEPGG 419
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAkNRGLKVAIIERSVSPGG 55
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
384-488 |
9.45e-04 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 42.62 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQL---LLAARSPRRrdllgIVDWRVREAKQAGVRLR----FGML 456
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLqygIPSFRLPRD-----IIDREVQRLVDIGVKIEtnkvIGKT 506
|
90 100 110
....*....|....*....|....*....|....
gi 521989364 457 AEPEDIRAERP-DTVILATG-GSParAFLGEGGE 488
Cdd:PRK12775 507 FTVPQLMNDKGfDAVFLGVGaGAP--TFLGIPGE 538
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
384-537 |
9.56e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 42.00 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPG--------GQLLLAARSPRRRDLLGIV-----DWRVREAKQA--- 447
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSELARLAlealdLWEELEEELGidc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 448 GVRLRFGM-LAEPEDIRAERPDTVILATGGSPARAFLGEGGELIEDTWDVLSGGTQAAGDVLVYDeHGANQALdaAEVLA 526
Cdd:pfam01266 81 GFRRCGVLvLARDEEEEALEKLLAALRRLGVPAELLDAEELRELEPLLPGLRGGLFYPDGGHVDP-ARLLRAL--ARAAE 157
|
170
....*....|.
gi 521989364 527 NAGARVRYATP 537
Cdd:pfam01266 158 ALGVRIIEGTE 168
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
383-418 |
1.05e-03 |
|
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: 41.85 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*.
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPG 418
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
383-419 |
1.19e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 41.77 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|....*..
gi 521989364 383 RRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGG 419
Cdd:PLN02172 11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
356-412 |
1.26e-03 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 41.62 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 521989364 356 AAKCVHNPATGReGTLpheLSPIHGAPR-RIVVVGAGPAGLEAARVLGGRGHEVVLFE 412
Cdd:cd05305 145 GAEYLEKPNGGR-GVL---LGGVPGVPPaKVVILGAGVVGENAARVALGLGAEVTVLD 198
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
369-421 |
3.41e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 40.64 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 521989364 369 GTLPHELSPI--HGAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEPGGQL 421
Cdd:PLN02529 145 GVSPSFASPIpeEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRV 199
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
372-413 |
3.95e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 40.24 E-value: 3.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 521989364 372 PHELSPIHGAPRRIVVVGAGPAGLEAARVLGGRGHEVVLFEA 413
Cdd:PRK08132 13 HADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
384-443 |
5.01e-03 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 40.10 E-value: 5.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQepggqlllAARSpRRRDLLGIvdWRVRE 443
Cdd:COG2509 32 DVVIVGAGPAGLFAALELAEAGLKPLVLERGK--------DVEE-RTCPVAEF--WRKGK 80
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
382-475 |
7.36e-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: 38.89 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521989364 382 PRRIVVVGAGPAGLEAARVLGGRGHEVVLFEAGQEpggqlllaarsprrrdllgivdwRVREAKQAGVRLRFGMLAEPE- 460
Cdd:COG0569 95 KMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPE-----------------------RVERLAEEDVLVIVGDATDEEv 151
|
90
....*....|....*..
gi 521989364 461 --DIRAERPDTVILATG 475
Cdd:COG0569 152 leEAGIEDADAVIAATG 168
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
384-412 |
9.48e-03 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 38.97 E-value: 9.48e-03
10 20
....*....|....*....|....*....
gi 521989364 384 RIVVVGAGPAGLEAARVLGGRGHEVVLFE 412
Cdd:PRK05335 4 PVNVIGAGLAGSEAAWQLAKRGVPVELYE 32
|
|
| |
