|
Name |
Accession |
Description |
Interval |
E-value |
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
7-359 |
0e+00 |
|
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: 642.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMHVGLEEAEGGFARMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQHR 86
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 87 VVTEAVHREGGRIAMQILHFGRYAYHRDLVAPSPLQAPISPFPPRELTDAEVERTIDDYARAARLAQRAGYDGVEIMGSE 166
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 167 GYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVITLARAVEAAGATI 246
Cdd:cd02930 161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 247 INTGIGWHEARIPTIATSVPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLLAEGYADMVSMARPMLADPDFVAKAA 326
Cdd:cd02930 241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 1751412095 327 DGRPEAINTCIGCNQACLDHTFSGQITSCLVNP 359
Cdd:cd02930 321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-363 |
5.97e-160 |
|
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: 464.64 E-value: 5.97e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 1 MSRYPHLLTPLDLGFTTLPNRVLMGSMHVGLEEAEG-GFARMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTE 79
Cdd:COG1902 1 MMKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEDGvPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 80 AEAEQHRVVTEAVHREGGRIAMQILHFGRYAYHRDL-----VAPSPLQAPISPFPPRELTDAEVERTIDDYARAARLAQR 154
Cdd:COG1902 81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPggwppVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 155 AGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVIT 234
Cdd:COG1902 161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 235 LARAVEAAGATIINTGIGWHEARiPTIATSVPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLLAEGYADMVSMARP 314
Cdd:COG1902 241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1751412095 315 MLADPDFVAKAADGRPEAINTCIGCNQaCLDHTFSGqiTSCLVNPRACH 363
Cdd:COG1902 320 LLADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
8-328 |
3.82e-118 |
|
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: 356.11 E-value: 3.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 8 LTPLDLGFTTLPNRVLMGSMHVGLEEAEGGFA-RMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQHR 86
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMATEDGTPTdELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 87 VVTEAVHREGGRIAMQILHFGRYAYH----RDLVAPSPLQAPISPFPPRELTDAEVERTIDDYARAARLAQRAGYDGVEI 162
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQAQPnltgGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 163 MGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVITLARAVEAA 242
Cdd:cd02803 161 HGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 243 GATIINTGIGWHEARIPTIATS-VPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLLAEGYADMVSMARPMLADPDF 321
Cdd:cd02803 241 GVDALHVSGGSYESPPPIIPPPyVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDL 320
|
....*..
gi 1751412095 322 VAKAADG 328
Cdd:cd02803 321 PNKAREG 327
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
7-330 |
4.13e-98 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 304.76 E-value: 4.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMHVGLEEAEGGFA--RMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQ 84
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPMTRLRSLDDGTKAtgLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 85 HRVVTEAVHREGGRIAMQILHFGRYAY-----HRDLVAPS-----PLQAPISPFPPRELTDAEVERTIDDYARAARLAQR 154
Cdd:pfam00724 82 WRKLTEAVHKNGSKAGVQLWHLGREAPmeyrpDLEVDGPSdpfalGAQEFEIASPRYEMSKEEIKQHIQDFVDAAKRARE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 155 AGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVit 234
Cdd:pfam00724 162 AGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 235 lARAVEAAGATIINTGIGWHEARIpTIATSVPRGAYTWVT------KRLMGEVSVPLVTTNRINTPELAEQLLAEGYADM 308
Cdd:pfam00724 240 -AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTrqqhntLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRADL 317
|
330 340
....*....|....*....|..
gi 1751412095 309 VSMARPMLADPDFVAKAADGRP 330
Cdd:pfam00724 318 VAMGRPFLADPDLPFKAKKGRP 339
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
7-340 |
2.94e-85 |
|
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: 271.41 E-value: 2.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMHVGLeeAEGGF--ARMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQ 84
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNY--AEDGLpsERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 85 HRVVTEAVHREGGRIAMQILHFGR---YAYHR-DLVAPSPLQAPISPFPPRELTDAEVERTIDDYARAARLAQRAGYDGV 160
Cdd:cd04734 79 FRRLAEAVHAHGAVIMIQLTHLGRrgdGDGSWlPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 161 EIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVITLARAVE 240
Cdd:cd04734 159 ELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 241 AAGAT-IINTGIG------WHEARIPTIAtsVPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLLAEGYADMVSMAR 313
Cdd:cd04734 239 AEGLIdYVNVSAGsyytllGLAHVVPSMG--MPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTR 316
|
330 340
....*....|....*....|....*..
gi 1751412095 314 PMLADPDFVAKAADGRPEAINTCIGCN 340
Cdd:cd04734 317 AHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
7-359 |
4.62e-70 |
|
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: 232.78 E-value: 4.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMHV-GLEEAEGGFA-RMAEFYAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQ 84
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFNqRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPMPSLPCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 85 H----RVVTEAVHREGGRIAMQI-LHFGRYAYHRDL-----VAPSPLQAPISPFPP-RELTDAEVERTIDDYARAARLAQ 153
Cdd:cd02931 81 FirtaKEMTERVHAYGTKIFLQLtAGFGRVCIPGFLgedkpVAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 154 RAGYDGVEIMG-SEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLS----MLDL----VP 224
Cdd:cd02931 161 EAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksyIKDLrqgaLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 225 G------GSTLDEVITLARAVEAAGATIINTGIG----WHEARIPTIATsvpRGAYTWVTKRLMGEVSVPLVTTNRINTP 294
Cdd:cd02931 241 GeefqekGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQK---KGMYLPYCKALKEVVDVPVIMAGRMEDP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751412095 295 ELAEQLLAEGYADMVSMARPMLADPDFVAKAADGRPEAINTCIGCNQACLDHTFSGQITSCLVNP 359
Cdd:cd02931 318 ELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
7-327 |
2.40e-66 |
|
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: 221.21 E-value: 2.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSM--HVgleeAEGGFArmAEF----YAARARGGVGLIVTGGIAPNDEGR--PHEGGarLTT 78
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMcqYS----AEDGVA--TDWhlvhYGSRALGGAGLVIVEATAVSPEGRitPGDLG--LWN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 79 EAEAEQHRVVTEAVHREGGRIAMQILHFGRYAYHR-----------------DLVAPSPLQAPISPFPPRELTDAEVERT 141
Cdd:cd02932 73 DEQIEALKRIVDFIHSQGAKIGIQLAHAGRKASTAppwegggpllppggggwQVVAPSAIPFDEGWPTPRELTREEIAEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 142 IDDYARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLD 221
Cdd:cd02932 153 VDAFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 222 LVPGGSTLDEVITLARAVEAAGATIINTGIG--WHEARIPtiatsVPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQ 299
Cdd:cd02932 233 WVEGGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIP-----VGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEA 307
|
330 340
....*....|....*....|....*...
gi 1751412095 300 LLAEGYADMVSMARPMLADPDFVAKAAD 327
Cdd:cd02932 308 ILESGRADLVALGRELLRNPYWPLHAAA 335
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
6-330 |
1.21e-61 |
|
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: 208.87 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 6 HLLTPLDLGFTTLPNRVLMGSM--------HVGLEeaeggfaRMAEFYAARArgGVGLIVTGG--IAPNDEGRPHEGGar 75
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrsradpdGVPTD-------LMAEYYAQRA--SAGLIITEAtqISPQGQGYPNTPG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 76 LTTEAEAEQHRVVTEAVHREGGRIAMQILHFGRYAyHRDL-------VAPSPLQAPISPF---------PPRELTDAEVE 139
Cdd:cd02933 70 IYTDEQVEGWKKVTDAVHAKGGKIFLQLWHVGRVS-HPSLlpggappVAPSAIAAEGKVFtpagkvpypTPRALTTEEIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 140 RTIDDYARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFiVVYRLSm 219
Cdd:cd02933 149 GIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADR-VGIRLS- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 220 ldlvPGGSTLDEVITLARAVEAAGATIINT-GIGW-H--EARIPTIATSVPRGAYTWVTKRLMGevsvPLVTTNRInTPE 295
Cdd:cd02933 227 ----PFGTFNDMGDSDPEATFSYLAKELNKrGLAYlHlvEPRVAGNPEDQPPDFLDFLRKAFKG----PLIAAGGY-DAE 297
|
330 340 350
....*....|....*....|....*....|....*
gi 1751412095 296 LAEQLLAEGYADMVSMARPMLADPDFVAKAADGRP 330
Cdd:cd02933 298 SAEAALADGKADLVAFGRPFIANPDLVERLKNGAP 332
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
17-337 |
9.13e-60 |
|
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: 204.37 E-value: 9.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 17 TLPNRVLMGSMHVGLEEAEGGFAR-MAEFYAARArGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQHRVVTEAVHRE 95
Cdd:cd04735 12 TLKNRFVMAPMTTYSSNPDGTITDdELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKSK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 96 GGRIAMQILHFGRYAYHR-----DLVAPSPLQAPiSPF--PPRELTDAEVERTIDDYARAARLAQRAGYDGVEIMGSEGY 168
Cdd:cd04735 91 GAKAILQIFHAGRMANPAlvpggDVVSPSAIAAF-RPGahTPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANGY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 169 LINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGE----DFIVVYRLSMLDLVPGGSTLDEVITLARAVEAAGA 244
Cdd:cd04735 170 LIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKhadkDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKGL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 245 TIINTGIGWHEARIPTIATSVPRgAYTWVTKRLMGEvsVPLVTTNRINTPELAEQLLAEGyADMVSMARPMLADPDFVAK 324
Cdd:cd04735 250 DYLHISLWDFDRKSRRGRDDNQT-IMELVKERIAGR--LPLIAVGSINTPDDALEALETG-ADLVAIGRGLLVDPDWVEK 325
|
330
....*....|...
gi 1751412095 325 AADGRPEAINTCI 337
Cdd:cd04735 326 IKEGREDEINLEI 338
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
7-324 |
3.00e-54 |
|
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: 188.95 E-value: 3.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGF-TTLPNRVLMGSMHVGLEEAEGG-FARMAEFYAARARGGVGLIVTGGIA--PNDEGRPH-EGGARLTTEAE 81
Cdd:cd04733 1 LGQPLTLPNgATLPNRLAKAAMSERLADGRGLpTPELIRLYRRWAEGGIGLIITGNVMvdPRHLEEPGiIGNVVLESGED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 82 AEQHRVVTEAVHREGGRIAMQILHFGRYAY---HRDLVAPSPLQAPISPF----PPRELTDAEVERTIDDYARAARLAQR 154
Cdd:cd04733 81 LEAFREWAAAAKANGALIWAQLNHPGRQSPaglNQNPVAPSVALDPGGLGklfgKPRAMTEEEIEDVIDRFAHAARLAQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 155 AGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTLDEVIT 234
Cdd:cd04733 161 AGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEEDALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 235 LARAVEAAGATIINTGIGWHEAriPTIATSVP-----RGAYtWVT--KRLMGEVSVPLVTTNRINTPELAEQLLAEGYAD 307
Cdd:cd04733 241 VVEALEEAGVDLVELSGGTYES--PAMAGAKKestiaREAY-FLEfaEKIRKVTKTPLMVTGGFRTRAAMEQALASGAVD 317
|
330
....*....|....*..
gi 1751412095 308 MVSMARPMLADPDFVAK 324
Cdd:cd04733 318 GIGLARPLALEPDLPNK 334
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
7-330 |
7.70e-54 |
|
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: 188.68 E-value: 7.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMhvGLEEAEGGF--ARMAEFYAARARGGVGLIVTGGIAPNDEGRP-HEGGARLTTEAEAE 83
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPM--TRSFSPGGVpgQDVAAYYRRRAAGGVGLIITEGTAVDHPAASgDPNVPRFHGEDALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 84 QHRVVTEAVHREGGRIAMQILHFGryAYHRDLVAPSPLQAPISP---FPP-----RELTDAEVERTIDDYARAARLAQRA 155
Cdd:cd04747 79 GWKKVVDEVHAAGGKIAPQLWHVG--AMRKLGTPPFPDVPPLSPsglVGPgkpvgREMTEADIDDVIAAFARAAADARRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 156 GYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVPGGSTL----DE 231
Cdd:cd04747 157 GFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTARLadtpDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 232 VITLARAVEAAGATIIN----------------TGIGWHEA--RIPTIATsvprGAYTWVTKRLMGEVSVPLVTTNRInt 293
Cdd:cd04747 237 LEALLAPLVDAGVDIFHcstrrfwepefegselNLAGWTKKltGLPTITV----GSVGLDGDFIGAFAGDEGASPASL-- 310
|
330 340 350
....*....|....*....|....*....|....*..
gi 1751412095 294 pELAEQLLAEGYADMVSMARPMLADPDFVAKAADGRP 330
Cdd:cd04747 311 -DRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRL 346
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
5-326 |
1.88e-45 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 173.20 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 5 PHLLTPLDLGFTTLPNRVLMGSMhvGLEEAEGGFArmAEF----YAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEA 80
Cdd:PRK08255 397 PPMFTPFRLRGLTLKNRVVVSPM--AMYSAVDGVP--GDFhlvhLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 81 EAEQHRVVTEAVHREGG-RIAMQILHFGRYAYHR---------------DLVAPSPLQ-APISPFPpRELTDAEVERTID 143
Cdd:PRK08255 473 QEAAWKRIVDFVHANSDaKIGIQLGHSGRKGSTRlgwegidepleegnwPLISASPLPyLPGSQVP-REMTRADMDRVRD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 144 DYARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLV 223
Cdd:PRK08255 552 DFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 224 PGGSTLDEVITLARAVEAAGATIIN--TGIGWHEARiPTIAtsvpRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLL 301
Cdd:PRK08255 632 EGGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYG----RMYQTPFADRIRNEAGIATIAVGAISEADHVNSII 706
|
330 340
....*....|....*....|....*
gi 1751412095 302 AEGYADMVSMARPMLADPDFVAKAA 326
Cdd:PRK08255 707 AAGRADLCALARPHLADPAWTLHEA 731
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
7-326 |
7.41e-44 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 160.63 E-value: 7.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMHVGLEEAEGGFARMAEF--YAARARGGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAEQ 84
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTNFHLihYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 85 HRVVTEAVHREGGRIAMQILHFGRYA-YHRDLVAPSPLqapisPF-----PPRELTDAEVERTIDDYARAARLAQRAGYD 158
Cdd:PRK13523 83 LHKLVTFIHDHGAKAAIQLAHAGRKAeLEGDIVAPSAI-----PFdekskTPVEMTKEQIKETVLAFKQAAVRAKEAGFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 159 GVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREaVGEDFIVVyRLSMLDLVPGGSTLDEVITLARA 238
Cdd:PRK13523 158 VIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKE-VWDGPLFV-RISASDYHPGGLTVQDYVQYAKW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 239 VEAAGATIINTGIGwheARIPTiATSVPRGAYTWVTKRLMGEVSVPLVTTNRINTPELAEQLLAEGYADMVSMARPMLAD 318
Cdd:PRK13523 236 MKEQGVDLIDVSSG---AVVPA-RIDVYPGYQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRN 311
|
....*...
gi 1751412095 319 PDFVAKAA 326
Cdd:PRK13523 312 PYFPRIAA 319
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
2-364 |
9.06e-41 |
|
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: 152.89 E-value: 9.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 2 SRYPHLLTPLDLGFTTLPNRVL-------MGSMHVGLeeaeggfarMAEFYAARARGGVGLIVTG--GIAPNDEGRPHEG 72
Cdd:cd02929 3 PRHDILFEPIKIGPVTARNRFYqvphcngMGYRKPSA---------QAAMRGIKAEGGWGVVNTEqcSIHPSSDDTPRIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 73 gARLTTEAEAEQHRVVTEAVHREGGRIAMQILHFGRYAYHRD--LVAPSPLQAP-----ISPFPPRELTDAEVERTIDDY 145
Cdd:cd02929 74 -ARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPNREsrETPLGPSQLPsefptGGPVQAREMDKDDIKRVRRWY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 146 ARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVYRLSMLDLVP- 224
Cdd:cd02929 153 VDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIGp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 225 -GGSTLDEVITLaraVEAAGATI----INTG--IGWHE-ARIPTIATSVPrgaytWVT--KRLMGEvsvPLVTTNRINTP 294
Cdd:cd02929 233 gGIESEGEGVEF---VEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEP-----YIKfvKQVTSK---PVVGVGRFTSP 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 295 ELAEQLLAEGYADMVSMARPMLADPDFVAKAADGRPEAINTCIGCNqACLDHTFSGQITSCLVNPRACHE 364
Cdd:cd02929 302 DKMVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
7-330 |
5.29e-34 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 133.31 E-value: 5.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 7 LLTPLDLGFTTLPNRVLMGSMhVGLEEAEGG---FARMAEFYAARArgGVGLIVTGGIAPNDEGRPHEGGARLTTEAEAE 83
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMAPL-TRLRSIEPGdipTPLMAEYYRQRA--SAGLIISEATQISAQAKGYAGAPGLHSPEQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 84 QHRVVTEAVHREGGRIAMQILHFGRYAyHRDL-------VAPSPLQAP--------------ISPFPPRELTDAEVERTI 142
Cdd:PRK10605 80 AWKKITAGVHAEGGHIAVQLWHTGRIS-HASLqpggqapVAPSAINAGtrtslrdengqairVETSTPRALELEEIPGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 143 DDYARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFIVVyRLSMLDL 222
Cdd:PRK10605 159 NDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRIGI-RISPLGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 223 VPG-GSTLDEvitlaravEAAGATIINT----GIGWHEARIPTIATSVPrgaYTWVTKRLMGEVSVPLVTTNRINTPELA 297
Cdd:PRK10605 238 FNNvDNGPNE--------EADALYLIEQlgkrGIAYLHMSEPDWAGGEP---YSDAFREKVRARFHGVIIGAGAYTAEKA 306
|
330 340 350
....*....|....*....|....*....|...
gi 1751412095 298 EQLLAEGYADMVSMARPMLADPDFVAKAADGRP 330
Cdd:PRK10605 307 ETLIGKGLIDAVAFGRDYIANPDLVARLQRKAE 339
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
5-324 |
1.13e-33 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 133.06 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 5 PHLLTPLDLGFTTLPNRVLMGSMHVGleEAEGGF--ARMAEFYAARARGGvGLIVTGG--IAPNDEGRPHEGGarLTTEA 80
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRC--RALNGIpnAALAEYYAQRSTPG-GFLISEGtlISPTAPGFPHVPG--IYSDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 81 EAEQHRVVTEAVHREGGRIAMQILHFGR---YAYHRDLVAP-SPLQAPIS-------------PFP-PRELTDAEVERTI 142
Cdd:PLN02411 85 QVEAWKKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISerwrilmpdgsygKYPkPRALETSEIPEVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 143 DDYARAARLAQRAGYDGVEIMGSEGYLINEFIATRTNHRTDRWGGSYENRMRFPVEIVRRVREAVGEDFiVVYRLSmldl 222
Cdd:PLN02411 165 EHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVRVS---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 223 vPGGSTLDEV----ITLARAV-EAAGATIINTGigwheARIPTIATSVPRgaYTWVTKRLMG-----EVSVPLVTTNRIN 292
Cdd:PLN02411 240 -PAIDHLDATdsdpLNLGLAVvERLNKLQLQNG-----SKLAYLHVTQPR--YTAYGQTESGrhgseEEEAQLMRTLRRA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1751412095 293 -----------TPELAEQLLAEGYADMVSMARPMLADPDFVAK 324
Cdd:PLN02411 312 yqgtfmcsggfTRELGMQAVQQGDADLVSYGRLFISNPDLVLR 354
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
376-636 |
2.74e-23 |
|
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: 100.86 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEI-GGQLNVARKVPGKQEFDETLRYFRTRLAELA---------VDVR 445
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADLYKRKEevvkklnngIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 446 LDTHVTA-----------DDVSG------HDEVVVATGVTPRTPDIPGVDHPsVLGYLDVLRDG-----APVGERVAILG 503
Cdd:pfam07992 81 LGTEVVSidpgakkvvleELVDGdgetitYDRLVIATGARPRLPPIPGVELN-VGFLVRTLDSAealrlKLLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 504 AGGIGFDVAEFLTDGGDKahenpetyfrqwgVDLDYRAPggltaperpapprtvHLLQRKTSKVGAGLGKttgwihrtEL 583
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE-------------VTLIEALD---------------RLLRAFDEEISAALEK--------AL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1751412095 584 RHRGVTMVPGVRYDRID-DAGLHLTIDGESTVLEVDTVVLCTGQEPRRDLYEAL 636
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIIgDGDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAA 257
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
363-512 |
4.93e-23 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 102.56 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 363 HETELVLAPTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGqLNV----ARKVPgkqefDETLRYFRTRLA 438
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG-LLRygipEFRLP-----KDIVDREVERLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 439 ELAVDVRLDTHV----TADDV-SGHDEVVVATGVT-PRTPDIPGVDHPSVLGYLDVLR--------DGAPVGERVAILGA 504
Cdd:PRK11749 202 KLGVEIRTNTEVgrdiTLDELrAGYDAVFIGTGAGlPRFLGIPGENLGGVYSAVDFLTrvnqavadYDLPVGKRVVVIGG 281
|
....*...
gi 1751412095 505 GGIGFDVA 512
Cdd:PRK11749 282 GNTAMDAA 289
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
370-512 |
3.43e-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: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 370 APTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPgkqEF---DETLRYFRTRLAELAVDVRL 446
Cdd:COG0493 116 PAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRYG--IP---EFrlpKDVLDREIELIEALGVEFRT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 447 DTHV----TADDV-SGHDEVVVATGVT-PRTPDIPGVDHPSVLGYLDVLRD----GAP-----VGERVAILGAGGIGFDV 511
Cdd:COG0493 191 NVEVgkdiTLDELlEEFDAVFLATGAGkPRDLGIPGEDLKGVHSAMDFLTAvnlgEAPdtilaVGKRVVVIGGGNTAMDC 270
|
.
gi 1751412095 512 A 512
Cdd:COG0493 271 A 271
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
371-628 |
8.10e-19 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 88.51 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 371 PTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDTHV 450
Cdd:PRK12770 14 PPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFG--IPEFRIPIERVREGVKELEEAGVVFHTRTKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 451 TADD--------------------VSGHDEVVVATGV-TPRTPDIPGVDHPSV--------------LGYLDVLRDGAPV 495
Cdd:PRK12770 92 CCGEplheeegdefverivsleelVKKYDAVLIATGTwKSRKLGIPGEDLPGVysaleylfriraakLGYLPWEKVPPVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 496 GERVAILGAGGIGFDVA-EFLTDGGDKahenpetyfrqwgVDLDYRApgglTAPERPAPPRTVHLLQRKTSKvgaglgkt 574
Cdd:PRK12770 172 GKKVVVVGAGLTAVDAAlEAVLLGAEK-------------VYLAYRR----TINEAPAGKYEIERLIARGVE-------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751412095 575 tgWI-HRTELRHRGVTMVPGVRYDRI-----DDAGLHLT--IDGESTVLEVDTVVLCTGQEP 628
Cdd:PRK12770 227 --FLeLVTPVRIIGEGRVEGVELAKMrlgepDESGRPRPvpIPGSEFVLEADTVVFAIGEIP 286
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
376-512 |
3.66e-18 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 88.39 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNV---ARKVPgKQEFDETLRyfrtRLAELAVDVRLDTHVtA 452
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYgipAYRLP-REVLDAEIQ----RILDLGVEVRLGVRV-G 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751412095 453 DDVS------GHDEVVVATGV-TPRTPDIPGVDHPSVLGYLDVLRD---GAP--VGERVAILGAGGIGFDVA 512
Cdd:PRK12771 212 EDITleqlegEFDAVFVAIGAqLGKRLPIPGEDAAGVLDAVDFLRAvgeGEPpfLGKRVVVIGGGNTAMDAA 283
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
375-643 |
4.32e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 86.73 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAERGHD--VTLFDAasEIGGQLNvarKVP------GKQEFDETLRYFRTRLAELAVDVRL 446
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDgeITVIGA--EPHPPYN---RPPlskvlaGETDEEDLLLRPADFYEENGIDLRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 447 DTHVTADDVSGH------------DEVVVATGVTPRTPDIPGVDHPSVLGY-----LDVLRDGAPVGERVAILGAGGIGF 509
Cdd:COG1251 76 GTRVTAIDRAARtvtladgetlpyDKLVLATGSRPRVPPIPGADLPGVFTLrtlddADALRAALAPGKRVVVIGGGLIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 510 DVAEFLtdggdkahenpetyfRQWGVDldyrapggltaperpapprtVHLLQRKTSKVGAGLGKTTGWIHRTELRHRGVT 589
Cdd:COG1251 156 EAAAAL---------------RKRGLE--------------------VTVVERAPRLLPRQLDEEAGALLQRLLEALGVE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751412095 590 MVPGVRYDRIDDA----GLHLTiDGEstVLEVDTVVLCTGQEPRRDLyeaLVAAGRTV 643
Cdd:COG1251 201 VRLGTGVTEIEGDdrvtGVRLA-DGE--ELPADLVVVAIGVRPNTEL---ARAAGLAV 252
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
370-641 |
1.42e-16 |
|
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: 82.22 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 370 APTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG----------QLNVARKV---PGKQEF---------D 427
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglRLDTPSHLyslPFFPNWsddpdfptgD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 428 ETLRYFRtRLAE---LAVDVRLDTHVTA---DDVSGH-------------DEVVVATGV--TPRTPDIPGVD-------H 479
Cdd:COG2072 81 EILAYLE-AYADkfgLRRPIRFGTEVTSarwDEADGRwtvttddgetltaRFVVVATGPlsRPKIPDIPGLEdfageqlH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 480 PSvlGYldvlRDGAPV-GERVAILGAGGIGFDVAEFLTDGGDKAH---ENP------ETYFRQWGVDLDYrapGGLTAPE 549
Cdd:COG2072 160 SA--DW----RNPVDLaGKRVLVVGTGASAVQIAPELARVAAHVTvfqRTPpwvlprPNYDPERGRPANY---LGLEAPP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 550 RPAPPRTVHLLQRKTSKV--GAGLGK--------------TTGWIHRteLRHRGVTMVPGvRYDRIDDAGLHLTiDGesT 613
Cdd:COG2072 231 ALNRRDARAWLRRLLRAQvkDPELGLltpdyppgckrpllSTDYYEA--LRRGNVELVTG-GIERITEDGVVFA-DG--T 304
|
330 340
....*....|....*....|....*...
gi 1751412095 614 VLEVDTVVLCTGQEPRRDLYEALVAAGR 641
Cdd:COG2072 305 EHEVDVIVWATGFRADLPWLAPLDVRGR 332
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
378-521 |
6.42e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.01 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 378 IAVVGAGPAGLACAVSAAERGHDVTLFDaASEIGGQLNVARKV---PGkqeFDETL------RYFRTRLAELAVDVRLD- 447
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLATTKEIenyPG---FPEGIsgpelaERLREQAERFGAEILLEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 448 -THVTADD----VSGHDE-------VVVATGVTPRTPDIPGVDHPSVLG-YLDVLRDGAP-VGERVAILGAGGIGFDVAE 513
Cdd:COG0492 79 vTSVDKDDgpfrVTTDDGteyeakaVIIATGAGPRKLGLPGEEEFEGRGvSYCATCDGFFfRGKDVVVVGGGDSALEEAL 158
|
....*...
gi 1751412095 514 FLTDGGDK 521
Cdd:COG0492 159 YLTKFASK 166
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
371-510 |
4.28e-15 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 78.28 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 371 PTRRR-KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVarkvpGKQEFDETLRYFRTRLAELA---VDVRL 446
Cdd:PRK12810 138 PVKRTgKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRY-----GIPDFKLEKEVIDRRIELMEaegIEFRT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 447 DTHV----TADD-VSGHDEVVVATGVT-PRTPDIPGVDHPSV---LGYL-----DVLRDGA-----PVGERVAILGAGGI 507
Cdd:PRK12810 213 NVEVgkdiTAEElLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfaMDFLiqntrRVLGDETepfisAKGKHVVVIGGGDT 292
|
...
gi 1751412095 508 GFD 510
Cdd:PRK12810 293 GMD 295
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
371-512 |
6.86e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 78.27 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 371 PTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDTHV 450
Cdd:PRK13984 279 PEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHLNTRV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751412095 451 tADDVS------GHDEVVVATGVT-PRTPDIPGVDHPSVLGYLDVLR--------DGA--PVGERVAILGAGGIGFDVA 512
Cdd:PRK13984 357 -GKDIPleelreKHDAVFLSTGFTlGRSTRIPGTDHPDVIQALPLLReirdylrgEGPkpKIPRSLVVIGGGNVAMDIA 434
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
400-651 |
1.43e-14 |
|
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: 75.23 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 400 DVTLFDAASEIGGQ-----LNVARkvpGKQEFDETLRYFRTRLAELAVDVRLDTHVTADDVSGH------------DEVV 462
Cdd:COG0446 7 EITVIEKGPHHSYQpcglpYYVGG---GIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKtvtlrdgetlsyDKLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 463 VATGVTPRTPDIPGVDHPSV-----LGYLDVLRD--GAPVGERVAILGAGGIGFDVAEfltdggdkahenpetYFRQWG- 534
Cdd:COG0446 84 LATGARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAE---------------ALRKRGl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 535 -VDLDYRAPggltaperpapprtvHLLQRKTSKVGAGLGKttgwihrtELRHRGVTMVPGVRYDRID-DAGLHLTI-DGE 611
Cdd:COG0446 149 kVTLVERAP---------------RLLGVLDPEMAALLEE--------ELREHGVELRLGETVVAIDgDDKVAVTLtDGE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1751412095 612 stVLEVDTVVLCTGQEPRRDLyeaLVAAGRTVHLIGGADV 651
Cdd:COG0446 206 --EIPADLVVVAPGVRPNTEL---AKDAGLALGERGWIKV 240
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
363-635 |
6.75e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 74.28 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 363 HETELVLAPTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLnvarkVPGKQEF----DETLRYFRTRLA 438
Cdd:PRK12831 128 NGIDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVL-----VYGIPEFrlpkETVVKKEIENIK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 439 ELAVDVRLDT----HVTADDV---SGHDEVVVATGV-TPRTPDIPGVDHPSVL-------------GYLDVLRDGAPVGE 497
Cdd:PRK12831 203 KLGVKIETNVvvgkTVTIDELleeEGFDAVFIGSGAgLPKFMGIPGENLNGVFsanefltrvnlmkAYKPEYDTPIKVGK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 498 RVAILGAGGIGFDVAEFLTDGGDKAHenpetyfrqwgvdLDYRApgglTAPERPAPPRTVH-------LLQRKTSKVGAg 570
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVH-------------IVYRR----SEEELPARVEEVHhakeegvIFDLLTNPVEI- 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751412095 571 LGKTTGWihrtelrhrgvtmVPGVRYDRI-----DDAGLH--LTIDGESTVLEVDTVVLCTGQEPRRDLYEA 635
Cdd:PRK12831 345 LGDENGW-------------VKGMKCIKMelgepDASGRRrpVEIEGSEFVLEVDTVIMSLGTSPNPLISST 403
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
376-512 |
9.93e-12 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 68.23 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLnvarkVPGKQEF-------DETLRYFRTRLAELAVDVRLDT 448
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVL-----KYGIPEFrlpkkivDVEIENLKKLGVKFETDVIVGK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 449 HVTADDV--SGHDEVVVATGV-TPRTPDIPGVDHPSVLG---YL------DVLRDGA--PV--GERVAILGAGGIGFDVA 512
Cdd:PRK12778 507 TITIEELeeEGFKGIFIASGAgLPNFMNIPGENSNGVMSsneYLtrvnlmDAASPDSdtPIkfGKKVAVVGGGNTAMDSA 586
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
378-629 |
6.32e-10 |
|
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: 62.03 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 378 IAVVGAGPAGLACAVSAAERGHDVTLFDAaSEIGG------------------QLNVARKVPG----------------- 422
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskallhaaeVAHEARHAAEfgisagapsvdwaalma 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 423 -KQEFDETLRYFRTRLAELA----------------VDVRLDTHVTADDVsghdevVVATGVTPRTPDIPGVDHPSVLGY 485
Cdd:COG1249 85 rKDKVVDRLRGGVEELLKKNgvdvirgrarfvdphtVEVTGGETLTADHI------VIATGSRPRVPPIPGLDEVRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 486 LDVLR-DGAPvgERVAILGAGGIGfdvAEFltdggdkAHenpetYFRQWGVDLD--YRAPggltaperpapprtvHLLQR 562
Cdd:COG1249 159 DEALElEELP--KSLVVIGGGYIG---LEF-------AQ-----IFARLGSEVTlvERGD---------------RLLPG 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751412095 563 KTSKVGAGLGKttgwihrtELRHRGVTMVPGVRYDRIDDAG----LHLTIDGESTVLEVDTVVLCTGQEPR 629
Cdd:COG1249 207 EDPEISEALEK--------ALEKEGIDILTGAKVTSVEKTGdgvtVTLEDGGGEEAVEADKVLVATGRRPN 269
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
376-512 |
9.83e-10 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 61.67 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDThVTADDV 455
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYG--IPRFRLPESVIDADIAPLRAMGAEFRFNT-VFGRDI 270
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751412095 456 S------GHDEVVVATGVT-PRTPDIPGVDHPSVLGYLDVLRDGA-----PVGERVAILGAGGIGFDVA 512
Cdd:PRK12814 271 TleelqkEFDAVLLAVGAQkASKMGIPGEELPGVISGIDFLRNVAlgtalHPGKKVVVIGGGNTAIDAA 339
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
372-510 |
1.48e-09 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 61.20 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 372 TRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDTHVT 451
Cdd:PRK12809 307 VPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG--IPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 452 -----ADDVSGHDEVVVATGVTP-RTPDIPGVDHPSVLGYLDVL----RD--GAP----------VGERVAILGAGGIGF 509
Cdd:PRK12809 385 rditfSDLTSEYDAVFIGVGTYGmMRADLPHEDAPGVIQALPFLtahtRQlmGLPeseeypltdvEGKRVVVLGGGDTTM 464
|
.
gi 1751412095 510 D 510
Cdd:PRK12809 465 D 465
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
377-412 |
7.12e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 58.36 E-value: 7.12e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
379-416 |
1.26e-08 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 57.37 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1751412095 379 AVVGAGPAGLACAVSAAERGHDVTLFDAASEIG--------GQLNV 416
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGrkilisggGRCNF 46
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
374-412 |
1.26e-08 |
|
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: 57.56 E-value: 1.26e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
36-313 |
2.07e-08 |
|
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: 54.90 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 36 GGFARMAEFYAARARGGVGLIVTGGIAPNDEgrpheggarlttEAEAEQHRVVTEAVHREGGRIAMQILHfgryayhrdl 115
Cdd:cd04722 9 GPSGDPVELAKAAAEAGADAIIVGTRSSDPE------------EAETDDKEVLKEVAAETDLPLGVQLAI---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 116 vapsplqapispfppreltdaevERTIDDYARAARLAQRAGYDGVEIMGSEGYlinefiatrtnhrtdrwggsyenRMRF 195
Cdd:cd04722 67 -----------------------NDAAAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LARE 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 196 PVEIVRRVREAVGeDFIVVYRLSMLDLVpggstldevitLARAVEAAGATIINTGIGWHEARIPTIATSVprgayTWVTK 275
Cdd:cd04722 101 DLELIRELREAVP-DVKVVVKLSPTGEL-----------AAAAAEEAGVDEVGLGNGGGGGGGRDAVPIA-----DLLLI 163
|
250 260 270
....*....|....*....|....*....|....*...
gi 1751412095 276 RLMGEVSVPLVTTNRINTPELAEQLLAEGyADMVSMAR 313
Cdd:cd04722 164 LAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
375-414 |
2.18e-08 |
|
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: 56.76 E-value: 2.18e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQL 414
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
376-416 |
2.84e-08 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 56.44 E-value: 2.84e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIG--------GQLNV 416
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRCNV 49
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
380-435 |
3.34e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 50.61 E-value: 3.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751412095 380 VVGAGPAGLACAVSAAERGHDVTLFDAASEIGGqlNVARKVPGKQEFDETLRYFRT 435
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG--NAYSYRVPGYVFDYGAHIFHG 54
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
374-412 |
4.82e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 56.01 E-value: 4.82e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
373-471 |
1.13e-07 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 54.38 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 373 RRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLnvarkvpgkqeFDETL-RYFRTRLAELAVDVRLDTHVT 451
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ-----------LDEEAgALLQRLLEALGVEVRLGTGVT 208
|
90 100 110
....*....|....*....|....*....|....
gi 1751412095 452 ADDVSGH--------------DEVVVATGVTPRT 471
Cdd:COG1251 209 EIEGDDRvtgvrladgeelpaDLVVVAIGVRPNT 242
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
375-625 |
1.19e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 54.37 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAER---GHDVTLFDAASE----------IGGQLNVAR-KVPgkqeFDETLRY--FRTRLA 438
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYhlfqpllpevAAGTLSPDDiAIP----LRELLRRagVRFIQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 439 ElAVDVRLDTH-VTADDvsGH----DEVVVATGVTPRTPDIPGVD---------------HPSVLGYLDVLRDGAPVgeR 498
Cdd:COG1252 77 E-VTGIDPEARtVTLAD--GRtlsyDYLVIATGSVTNFFGIPGLAehalplktledalalRERLLAAFERAERRRLL--T 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 499 VAILGAGGIGFDVA-EfltdggdkahenpetyfrqwgvdLDYRAPGGLTAPERPAPPRTVHLLQRkTSKVGAGLGKTTGW 577
Cdd:COG1252 152 IVVVGGGPTGVELAgE-----------------------LAELLRKLLRYPGIDPDKVRITLVEA-GPRILPGLGEKLSE 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1751412095 578 IHRTELRHRGVTMVPGVRYDRIDDAGLHLTiDGEStvLEVDTVVLCTG 625
Cdd:COG1252 208 AAEKELEKRGVEVHTGTRVTEVDADGVTLE-DGEE--IPADTVIWAAG 252
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
360-631 |
1.34e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 54.87 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 360 RACHETELVLAPTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLN-VARKVPgkqefdeTLRYFRTRLA 438
Cdd:COG1148 125 KAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFP-------GLDCPQCILE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 439 ELAVDVR--------LDTHVTadDVSGHD---EVVVATGvtPRTPdipgvdhpsvlgylDVLRDGApvgervAILGAGGI 507
Cdd:COG1148 198 PLIAEVEanpnitvyTGAEVE--EVSGYVgnfTVTIKKG--PREE--------------IEIEVGA------IVLATGFK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 508 GFDVAEFLTDGGDKaHENPETyfrqwGVDLDYR-APGGLTAPERPAPPRTVHLLQ----RKT-------SKV--GAGLgK 573
Cdd:COG1148 254 PYDPTKLGEYGYGK-YPNVIT-----NLELERLlAAGKILRPSDGKEPKSVAFIQcvgsRDEenglpycSRVccMYAL-K 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 574 TTGWIH---------------RT---------ELRHRGVTMVPGvRYDRI---DDAGLHL----TIDGESTVLEVDTVVL 622
Cdd:COG1148 327 QALYLKeknpdadvyifyrdiRTygkyeefyrRAREDGVRFIRG-RVAEIeedEGGKLVVtvedTLLGEPVEIEADLVVL 405
|
....*....
gi 1751412095 623 CTGQEPRRD 631
Cdd:COG1148 406 ATGMVPSED 414
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
377-465 |
2.13e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 48.74 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQlnvarkvpgkqeFDETL-RYFRTRLAELAVDVRLDTHVTADDV 455
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG------------FDPEIaKILQEKLEKNGIEFLLNTTVEAIEG 68
|
90
....*....|
gi 1751412095 456 SGHDEVVVAT 465
Cdd:pfam00070 69 NGDGVVVVLT 78
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
449-632 |
2.45e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 54.06 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 449 HVTADDVSGHDEVVVATGVTPRTPDIPGVDHPSVLGY-----LDVLRDGAPVGERVAILGAGGIGFDVAEFLtdggdkah 523
Cdd:TIGR02374 88 ITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAAVIGGGLLGLEAAVGL-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 524 enpetyfRQWGVDLD--YRAPGgltaperpapprtvhLLQRKtskvgagLGKTTGWIHRTELRHRGVTMVPG------VR 595
Cdd:TIGR02374 160 -------QNLGMDVSviHHAPG---------------LMAKQ-------LDQTAGRLLQRELEQKGLTFLLEkdtveiVG 210
|
170 180 190
....*....|....*....|....*....|....*..
gi 1751412095 596 YDRIDdaGLHLTiDGEStvLEVDTVVLCTGQEPRRDL 632
Cdd:TIGR02374 211 ATKAD--RIRFK-DGSS--LEADLIVMAAGIRPNDEL 242
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
376-510 |
4.24e-07 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 53.21 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDTHVTADD- 454
Cdd:PRK12769 328 KRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFG--IPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDIs 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751412095 455 ----VSGHDEVVVATGvTPRT--PDIPGVDHPSVLGYLDVL------------RDGAP----VGERVAILGAGGIGFD 510
Cdd:PRK12769 406 leslLEDYDAVFVGVG-TYRSmkAGLPNEDAPGVYDALPFLiantkqvmgleeLPEEPfintAGLNVVVLGGGDTAMD 482
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
369-412 |
5.03e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 52.62 E-value: 5.03e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1751412095 369 LAPTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:COG1231 1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
374-412 |
7.92e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 51.42 E-value: 7.92e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
374-471 |
8.88e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 51.16 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQlnvarkvpgkqeFDETLRYF-RTRLAELAVDVRLDTHVTA 452
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA------------FDEEISAAlEKALEKNGVEVRLGTSVKE 218
|
90 100 110
....*....|....*....|....*....|...
gi 1751412095 453 DDVSGH--------------DEVVVATGVTPRT 471
Cdd:pfam07992 219 IIGDGDgvevilkdgteidaDLVVVAIGRRPNT 251
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
374-412 |
1.02e-06 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 51.66 E-value: 1.02e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERgHDVTLFDAASEIGG 412
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
372-660 |
1.05e-06 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 51.49 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 372 TRRRKRIAVVGAGPAGLACAVSAAERGH---DVTLFDAASEIG-GQ----------LNV--------------------A 417
Cdd:COG4529 2 TGARKRIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELGrGVaystdspehlLNVpagrmsafpddpdhflrwlrE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 418 RKVPGKQEFDETL--------RYFRTRLAEL----------------AVDVRLDTH----VTADDVSGH-DEVVVATG-V 467
Cdd:COG4529 82 NGARAAPAIDPDAfvprrlfgEYLRERLAEAlarapagvrlrhiraeVVDLERDDGgyrvTLADGETLRaDAVVLATGhP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 468 TPRTPDIPGVDHPSVLG--Y-LDVLrDGAPVGERVAILGAGGIGFDVAEFLTDGGDKAH--------ENPETYFRQWGVD 536
Cdd:COG4529 162 PPAPPPGLAAGSPRYIAdpWpPGAL-ARIPPDARVLIIGTGLTAIDVVLSLAARGHRGPitalsrrgLLPRAHPPGAPLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 537 LDYRAPGGL-TAPERPAPPRTVHLLQ--RKTSKVGAGLGKT--------------------------------TGW-IHR 580
Cdd:COG4529 241 LKFLTPEALeELPLFFAARTARDLLRalRADLAEAEAGGVDwravidalrpvlqalwaalsaeerrrflrhlrPYWdVHR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 581 -----------TELRHRG-VTMVPG-VRYDRIDDAGLHLTIDGESTVLEVDTVVLCTGQEPR---------RDLYEALVA 638
Cdd:COG4529 321 hrmppesaarlLALIAAGrLEVLAGrLEDIEAAEGGFVVTGAGDGETLEVDVVINATGPEPDlrrdadpllRSLLARGLA 400
|
410 420
....*....|....*....|..
gi 1751412095 639 AGRTVHLigGADVAAELDAKRA 660
Cdd:COG4529 401 RPDPLGL--GLDVDPDGRVLDA 420
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
376-471 |
3.98e-06 |
|
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: 49.42 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNvarkvpgkqefDETLRYFRTRLAELAVDVRLDTHVTADDV 455
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLD-----------PEMAALLEEELREHGVELRLGETVVAIDG 193
|
90 100
....*....|....*....|....*....
gi 1751412095 456 SGH-------------DEVVVATGVTPRT 471
Cdd:COG0446 194 DDKvavtltdgeeipaDLVVVAPGVRPNT 222
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
374-451 |
4.86e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 49.13 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAAsEIG--------GQLNVARKVPGKQEFDETLRYFRTRLAELAVDVR 445
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasgrnaGQLRPGLAALADRALVRLAREALDLWRELAAELG 79
|
....*.
gi 1751412095 446 LDTHVT 451
Cdd:COG0665 80 IDCDFR 85
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
377-444 |
6.51e-06 |
|
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: 48.55 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIG--------GQLNVARKVPGKQEFD----ETLRYFRTRLAELAVDV 444
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSELArlalEALDLWEELEEELGIDC 80
|
|
| YwnB |
COG2910 |
Putative NADH-flavin reductase [General function prediction only]; |
377-550 |
9.13e-06 |
|
Putative NADH-flavin reductase [General function prediction only];
Pssm-ID: 442154 [Multi-domain] Cd Length: 205 Bit Score: 47.16 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGA-GPAGLACAVSAAERGHDVTLFdaaseiggqlnvARKvPGKqefdetLRYFRTRLAELAVDVrLDTHVTADDV 455
Cdd:COG2910 1 KIAVIGAtGRVGSLIVREALARGHEVTAL------------VRN-PEK------LPDEHPGLTVVVGDV-LDPAAVAEAL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 456 SGHDEVVVATGvtPRTPDIPGVDHPSVLGYLDVLRdGAPVgERVAILGAGGIGFDVAEFLTDGGD---------KAHENP 526
Cdd:COG2910 61 AGADAVVSALG--AGGGNPTTVLSDGARALIDAMK-AAGV-KRLIVVGGAGSLDVAPGLGLDTPGfpaalkpaaAAKAAA 136
|
170 180
....*....|....*....|....
gi 1751412095 527 ETYFRQWGVDLDYRAPGGLTAPER 550
Cdd:COG2910 137 EELLRASDLDWTIVRPAALTDGER 160
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
376-474 |
1.16e-05 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 48.15 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEiggqlnvarkvpgKQEFDETLRyfrtrlaELAVDVRLDTHvTADDV 455
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA-------------PELAAAELE-------APGVEVVLGEH-PEELL 63
|
90
....*....|....*....
gi 1751412095 456 SGHDEVVVATGVTPRTPDI 474
Cdd:COG0771 64 DGADLVVKSPGIPPDHPLL 82
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
370-469 |
1.25e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 47.82 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 370 APTRRRKRIAVVGAGPAG--LACAVSAAERGH-----------DVTLFDAASEIGGqlnvarkvpgkqEFDETLR-YFRT 435
Cdd:COG1252 144 AERRRLLTIVVVGGGPTGveLAGELAELLRKLlrypgidpdkvRITLVEAGPRILP------------GLGEKLSeAAEK 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1751412095 436 RLAELAVDVRLDTHVT---ADDV---SGH----DEVVVATGVTP 469
Cdd:COG1252 212 ELEKRGVEVHTGTRVTevdADGVtleDGEeipaDTVIWAAGVKA 255
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
377-523 |
1.75e-05 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 47.80 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASeIGGQ-LNV-----------------ARKVP----------------- 421
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERGP-LGGTcVNVgcvpskmllraaevahyARKPPfgglaatvavdfgelle 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 422 GKQEFDETLRY--FRTRLAELAVDVRLDTHVTADD----------VSGHDEVVVATGVTPRTPDIPGVDHpsvLGYLDVL 489
Cdd:TIGR02053 81 GKREVVEELRHekYEDVLSSYGVDYLRGRARFKDPktvkvdlgreVRGAKRFLIATGARPAIPPIPGLKE---AGYLTSE 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1751412095 490 RDGA--PVGERVAILGAGGIGFDVAEFLTDGGDKAH 523
Cdd:TIGR02053 158 EALAldRIPESLAVIGGGAIGVELAQAFARLGSEVT 193
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
375-412 |
2.62e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.19 E-value: 2.62e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:PRK07208 4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
378-414 |
4.08e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 46.45 E-value: 4.08e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1751412095 378 IAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQL 414
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
375-413 |
4.79e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 46.78 E-value: 4.79e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQ 413
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
378-414 |
7.58e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 45.74 E-value: 7.58e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1751412095 378 IAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQL 414
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGAT 38
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
377-462 |
8.29e-05 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 45.03 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASeiggqlnvarkvpgkQEFDETLRYFRTRLAELAvDVRLDTHVTADDVS 456
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADP---------------AAAAAAPAYIAGRLEDLA-AFDLLDGEAPDAVL 67
|
....*.
gi 1751412095 457 GHDEVV 462
Cdd:PRK06129 68 ARIRVT 73
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
376-421 |
1.05e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 45.30 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNvARKVP 421
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLN-KGKSP 45
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
374-411 |
1.08e-04 |
|
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: 44.93 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIG 411
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
370-413 |
1.16e-04 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1751412095 370 APTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQ 413
Cdd:PLN02487 70 AYKGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGK 113
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
385-512 |
1.55e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 44.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 385 PAGLACAVSAA----------ERGHDV----------TLFDAA--SEIGGQLNVARKVPGKQEF----------DETLRY 432
Cdd:pfam13738 1 PAGIGCAIALKkagledylilEKGNIGnsfyrypthmTFFSPSftSNGFGIPDLNAISPGTSPAftfnrehpsgNEYAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 433 FRTRLAELAVDVRLDTHVTAddVSGHDE---------------VVVATGV--TPRTPDIPgvDHPSVLGYldvLRDGAPV 495
Cdd:pfam13738 81 LRRVADHFELPINLFEEVTS--VKKEDDgfvvttskgtyqaryVIIATGEfdFPNKLGVP--ELPKHYSY---VKDFHPY 153
|
170
....*....|....*...
gi 1751412095 496 -GERVAILGAGGIGFDVA 512
Cdd:pfam13738 154 aGQKVVVIGGYNSAVDAA 171
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
376-414 |
2.39e-04 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 43.86 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFD----AASEI----GGQL 414
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDrhryAAMETsfanGGQL 48
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
380-412 |
3.10e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 43.67 E-value: 3.10e-04
10 20 30
....*....|....*....|....*....|...
gi 1751412095 380 VVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:COG1053 8 VVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
377-410 |
3.51e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 43.52 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|....
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEI 410
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
374-423 |
4.48e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 43.22 E-value: 4.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASeIGGQ-LNVArKVPGK 423
Cdd:PRK13748 97 RPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGT-IGGTcVNVG-CVPSK 145
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
356-414 |
5.90e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 43.28 E-value: 5.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751412095 356 LVNPRACHETELVLAP--TRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQL 414
Cdd:PRK12779 285 LVNPNANERFAGRISPwaAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVL 345
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
360-407 |
6.81e-04 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 42.93 E-value: 6.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1751412095 360 RACHETElvlAPTRRRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAA 407
Cdd:PRK08132 11 RPHADQD---ADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDD 55
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
383-411 |
7.46e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 41.88 E-value: 7.46e-04
10 20
....*....|....*....|....*....
gi 1751412095 383 AGPAGLACAVSAAERGHDVTLFDAASEIG 411
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
377-510 |
8.49e-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: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVArkVPGKQEFDETLRYFRTRLAELAVDVRLDTHV----TA 452
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYG--IPSFRLPRDIIDREVQRLVDIGVKIETNKVIgktfTV 509
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751412095 453 DDV---SGHDEVVVATGV-TPRTPDIPG------------VDHPSVLG-----YLDVlrdGAPVGERVAILGAGGIGFD 510
Cdd:PRK12775 510 PQLmndKGFDAVFLGVGAgAPTFLGIPGefagqvysanefLTRVNLMGgdkfpFLDT---PISLGKSVVVIGAGNTAMD 585
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
369-412 |
1.01e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 42.16 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1751412095 369 LAPTRRR---KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:PLN02172 1 MAPAQNPinsQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
374-411 |
1.51e-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: 41.76 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1751412095 374 RRKRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIG 411
Cdd:PRK01747 259 KARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
368-474 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 368 VLAPTRRRKRIAVVGAGPAG--LACAVSAAerGHDVTLFDAASEIGGQlnvarkvpgkqeFDETLR-YFRTRLAELAVDV 444
Cdd:COG1249 161 ALELEELPKSLVVIGGGYIGleFAQIFARL--GSEVTLVERGDRLLPG------------EDPEISeALEKALEKEGIDI 226
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1751412095 445 RLDT------------HVTADDVSGH-----DEVVVATGVTPRTPDI 474
Cdd:COG1249 227 LTGAkvtsvektgdgvTVTLEDGGGEeaveaDKVLVATGRRPNTDGL 273
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
376-502 |
2.42e-03 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 40.40 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVARkvpgkqefdETLRYFRtrlaelavDVRLDTHVTA-DD 454
Cdd:COG0240 1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETR---------ENPRYLP--------GVKLPENLRAtSD 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751412095 455 ----VSGHDEVVVAT----------GVTPR-TPDIP------GVDHPSVLGYLDVLRDGAPVGERVAIL 502
Cdd:COG0240 64 leeaLAGADLVLLAVpsqalrevleQLAPLlPPGAPvvsatkGIEPGTGLLMSEVIAEELPGALRIAVL 132
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
380-412 |
2.43e-03 |
|
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: 41.11 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|...
gi 1751412095 380 VVGAGPAGLACAVSAAERGHDVTLFDAASEIGG 412
Cdd:TIGR02734 3 VIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
376-513 |
3.03e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 40.41 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAA--ERGHDVTLFDAASEIG-GQLNVARKVPGkqEFDETLRYF-RT--RLAELAVDVRLDTH 449
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKrlNKELEITVYEKTDIVSfGACGLPYFVGG--FFDDPNTMIaRTpeEFIKSGIDVKTEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 450 VTADDVSG-----------------HDEVVVATGVTPRTPDIPGVDHPSVLGyLDVLRDGAPVGE--------RVAILGA 504
Cdd:PRK09564 79 VVKVDAKNktitvknlktgsifndtYDKLMIATGARPIIPPIKNINLENVYT-LKSMEDGLALKEllkdeeikNIVIIGA 157
|
....*....
gi 1751412095 505 GGIGFDVAE 513
Cdd:PRK09564 158 GFIGLEAVE 166
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
377-410 |
3.31e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 40.26 E-value: 3.31e-03
10 20 30
....*....|....*....|....*....|....
gi 1751412095 377 RIAVVGAGPAGLACAVSAAERGHDVTLFDAASEI 410
Cdd:PRK07538 2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPEL 35
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
380-411 |
3.47e-03 |
|
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: 39.99 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|..
gi 1751412095 380 VVGAGPAGLACAVSAAERGHDVTLFDAASEIG 411
Cdd:TIGR02032 5 VVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| sdhA |
PRK08641 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
375-404 |
4.02e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236319 [Multi-domain] Cd Length: 589 Bit Score: 40.34 E-value: 4.02e-03
10 20 30
....*....|....*....|....*....|
gi 1751412095 375 RKRIAVVGAGPAGLACAVSAAERGHDVTLF 404
Cdd:PRK08641 3 KGKVIVVGGGLAGLMATIKAAEAGVHVDLF 32
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
376-405 |
6.00e-03 |
|
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 397677 [Multi-domain] Cd Length: 186 Bit Score: 38.38 E-value: 6.00e-03
10 20 30
....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFD 405
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVD 30
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
376-465 |
6.45e-03 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 39.28 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751412095 376 KRIAVVGAGPAGLACAVSAAERGHDVTLFDAASEIGGQLNVARkvpgkqefdETLRYFRtrlaelavDVRLDTHVTA--- 452
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADR---------ENPRYLP--------GIKLPDNLRAttd 64
|
90
....*....|....*
gi 1751412095 453 --DDVSGHDEVVVAT 465
Cdd:PRK00094 65 laEALADADLILVAV 79
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
380-413 |
7.72e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 39.39 E-value: 7.72e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1751412095 380 VVGAGPAGLACAVSAAERGHDVTLFDAASE--IGGQ 413
Cdd:COG3573 10 VVGAGLAGLVAAAELADAGRRVLLLDQEPEanLGGQ 45
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
386-524 |
8.54e-03 |
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Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 39.01 E-value: 8.54e-03
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gi 1751412095 386 AGLACAVSAAERGHDVTLFDAASEIGGQLNvARKVPGkQEFDETLRYFR---TRLAELAVDVRLDTHVTADDVSGHDEVV 462
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGGRIR-TVRDDG-FLIELGAMWFHgaqPPLLALLKELGLEDRLVLPDPAPFYTVL 79
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90 100 110 120 130 140
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gi 1751412095 463 VATGVTPRTpDIPGVDHP--SVLGYLDVLRDGAPVGERVAILGAGGigfdVAEFLTDGGDKAHE 524
Cdd:pfam01593 80 FAGGRRYPG-DFRRVPAGweGLLEFGRLLSIPEKLRLGLAALASDA----LDEFDLDDFSLAES 138
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