|
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 ... |
8-360 |
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: 632.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMHVGLEEAPNGFERMAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEAERHR 87
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 88 VVTRAVHAAGGKIALQILHFGRYAYHPALAAPSALKAPINPFTPHALSSDEVDETIGDFVRCAALAQHAGYDGVEIMGSE 167
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 168 GYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEVIRLAQAIEAAGATI 247
Cdd:cd02930 161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 248 INTGIGWHEARIPTIATKVPRAAYAWVTRQLMGKVGIPLVATNRINTPEVAERLLADGYCDMVSMARPFLADAEFVRKAR 327
Cdd:cd02930 241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 1859084183 328 EGRADEINTCIGCNQACLDHTFSGRITSCLVNP 360
Cdd:cd02930 321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
3-364 |
4.41e-154 |
|
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: 449.62 E-value: 4.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 3 SRYPHLTTPLELGFTSLRNRVLMGSMHVGLEEaPNGF--ERMAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTE 80
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 81 AEAERHRVVTRAVHAAGGKIALQILHFGRYAYHPALA-----APSALKAPINPFTPHALSSDEVDETIGDFVRCAALAQH 155
Cdd:COG1902 81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGgwppvAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 156 AGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEVIR 235
Cdd:COG1902 161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 236 LAQAIEAAGATIINTGIGWHEARiPTIATKVPRAAYAWVTRQLMGKVGIPLVATNRINTPEVAERLLADGYCDMVSMARP 315
Cdd:COG1902 241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1859084183 316 FLADAEFVRKAREGRADEINTCIGCNQaCLDHTFSGriTSCLVNPRACH 364
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 ... |
10-329 |
6.40e-110 |
|
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: 334.93 E-value: 6.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 10 TPLELGFTSLRNRVLMGSMHVGLEEaPNGF--ERMAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEAERHR 87
Cdd:cd02803 2 SPIKIGGLTLKNRIVMAPMTENMAT-EDGTptDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 88 VVTRAVHAAGGKIALQILHFGRYAYHPAL----AAPSALKAPINPFTPHALSSDEVDETIGDFVRCAALAQHAGYDGVEI 163
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQAQPNLTggppPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 164 MGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEVIRLAQAIEAA 243
Cdd:cd02803 161 HGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 244 GATIINTGIGWHEARIPTIA-TKVPRAAYAWVTRQLMGKVGIPLVATNRINTPEVAERLLADGYCDMVSMARPFLADAEF 322
Cdd:cd02803 241 GVDALHVSGGSYESPPPIIPpPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDL 320
|
....*..
gi 1859084183 323 VRKAREG 329
Cdd:cd02803 321 PNKAREG 327
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
8-333 |
1.23e-94 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 295.90 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMhVGLEEAPNGF---ERMAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEAE 84
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 85 RHRVVTRAVHAAGGKIALQILHFGRYAY-----HPALAAPS---ALKAPINPFTP--HALSSDEVDETIGDFVRCAALAQ 154
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREAPmeyrpDLEVDGPSdpfALGAQEFEIASprYEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 155 HAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEVi 234
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 235 rlAQAIEAAGATIINTGIGWHEARIpTIATKVPRAAYAWVTRQLM------GKVGIPLVATNRINTPEVAERLLADGYCD 308
Cdd:pfam00724 240 --AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTRQQHntlfvkGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
|
330 340
....*....|....*....|....*
gi 1859084183 309 MVSMARPFLADAEFVRKAREGRADE 333
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
8-341 |
7.24e-77 |
|
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: 249.45 E-value: 7.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMHVGLEEapNGF--ERMAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEAER 85
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAE--DGLpsERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 86 HRVVTRAVHAAGGKIALQILHFGR-----YAYHPALAaPSALKAPINPFTPHALSSDEVDETIGDFVRCAALAQHAGYDG 160
Cdd:cd04734 79 FRRLAEAVHAHGAVIMIQLTHLGRrgdgdGSWLPPLA-PSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 161 VEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEVIRLAQAI 240
Cdd:cd04734 158 VELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 241 EAAGAT-IINTGIG------WHEARIPTIAtkVPRAAYAWVTRQLMGKVGIPLVATNRINTPEVAERLLADGYCDMVSMA 313
Cdd:cd04734 238 AAEGLIdYVNVSAGsyytllGLAHVVPSMG--MPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMT 315
|
330 340
....*....|....*....|....*...
gi 1859084183 314 RPFLADAEFVRKAREGRADEINTCIGCN 341
Cdd:cd04734 316 RAHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
8-360 |
2.44e-65 |
|
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: 220.46 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMHV-GLEEAPNGF-ERMAAFYAERARGEAGLIVTG-GFAPNE---RGRPAAGGAMLTTEA 81
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFnQRGIDYYVERAKGGTGLIITGvTMVDNEieqFPMPSLPCPTYNPTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 82 EAERHRVVTRAVHAAGGKIALQI-LHFGRYAYhPALA------APSALKAPINPFTPH-ALSSDEVDETIGDFVRCAALA 153
Cdd:cd02931 81 FIRTAKEMTERVHAYGTKIFLQLtAGFGRVCI-PGFLgedkpvAPSPIPNRWLPEITCrELTTEEVETFVGKFGESAVIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 154 QHAGYDGVEIMG-SEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLS----MLDL----- 223
Cdd:cd02931 160 KEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksyIKDLrqgal 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 224 -----VEGGSTLDEVIRLAQAIEAAGATIINTGIG----WHEARIPTIATKvprAAYAWVTRQLMGKVGIPLVATNRINT 294
Cdd:cd02931 240 pgeefQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQKK---GMYLPYCKALKEVVDVPVIMAGRMED 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859084183 295 PEVAERLLADGYCDMVSMARPFLADAEFVRKAREGRADEINTCIGCNQACLDHTFSGRITSCLVNP 360
Cdd:cd02931 317 PELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
8-326 |
1.54e-60 |
|
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: 205.81 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSM-----HVGLeeaPNGFERMaaFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAE 82
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMcqysaEDGV---ATDWHLV--HYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 83 AERHRVVTRAVHAAGGKIALQILHFGRYA--------YHPALA---------APSALKAPINPFTPHALSSDEVDETIGD 145
Cdd:cd02932 76 IEALKRIVDFIHSQGAKIGIQLAHAGRKAstappwegGGPLLPpggggwqvvAPSAIPFDEGWPTPRELTREEIAEVVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 146 FVRCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVE 225
Cdd:cd02932 156 FVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 226 GGSTLDEVIRLAQAIEAAGATIINTGIG--WHEARIPT-IATKVPRAAyawvtrQLMGKVGIPLVATNRINTPEVAERLL 302
Cdd:cd02932 236 GGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIPVgPGYQVPFAE------RIRQEAGIPVIAVGLITDPEQAEAIL 309
|
330 340
....*....|....*....|....
gi 1859084183 303 ADGYCDMVSMARPFLADAEFVRKA 326
Cdd:cd02932 310 ESGRADLVALGRELLRNPYWPLHA 333
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
8-338 |
1.63e-55 |
|
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: 192.81 E-value: 1.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLEL--GFTsLRNRVLMGSMHVGLEEaPNGF--ERMAAFYAERARGeAGLIVTGGFAPNERGRPAAGGAMLTTEAEA 83
Cdd:cd04735 1 LFEPFTLknGVT-LKNRFVMAPMTTYSSN-PDGTitDDELAYYQRRAGG-VGMVITGATYVSPSGIGFEGGFSADDDSDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 84 ERHRVVTRAVHAAGGKIALQILHFGRYAyHPALA------APSALKAPiNPF--TPHALSSDEVDETIGDFVRCAALAQH 155
Cdd:cd04735 78 PGLRKLAQAIKSKGAKAILQIFHAGRMA-NPALVpggdvvSPSAIAAF-RPGahTPRELTHEEIEDIIDAFGEATRRAIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 156 AGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGT----NFIVIYRLSMLDLVEGGSTLD 231
Cdd:cd04735 156 AGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKhadkDFILGYRFSPEEPEEPGIRME 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 232 EVIRLAQAIEAAGATIINTGIGWHEARIPTIATKVPRAAYAwVTRQLMGKvgIPLVATNRINTPEVAERLLADGYcDMVS 311
Cdd:cd04735 236 DTLALVDKLADKGLDYLHISLWDFDRKSRRGRDDNQTIMEL-VKERIAGR--LPLIAVGSINTPDDALEALETGA-DLVA 311
|
330 340
....*....|....*....|....*..
gi 1859084183 312 MARPFLADAEFVRKAREGRADEINTCI 338
Cdd:cd04735 312 IGRGLLVDPDWVEKIKEGREDEINLEI 338
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
7-329 |
2.36e-53 |
|
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: 186.52 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 7 HLTTPLELGFTSLRNRVLMGSM--------HVgleeaPNgfERMAAFYAERArgEAGLIVTGGFAPNERGRPAAGGAMLT 78
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrsradpdGV-----PT--DLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 79 TEAEAERHRVVTRAVHAAGGKIALQILHFGRYAyHPALA-------APSALKAPINPFT---------PHALSSDEVDET 142
Cdd:cd02933 72 TDEQVEGWKKVTDAVHAKGGKIFLQLWHVGRVS-HPSLLpggappvAPSAIAAEGKVFTpagkvpyptPRALTTEEIPGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 143 IGDFVRCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIyRLS--- 219
Cdd:cd02933 151 VADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADRVGI-RLSpfg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 220 ----MLDlvegGSTLDEVIRLAQAIEAAgatiintGIGW-H--EARIPTIATKVPRAAYAWVTRQLMGkvgiPLVATNRI 292
Cdd:cd02933 230 tfndMGD----SDPEATFSYLAKELNKR-------GLAYlHlvEPRVAGNPEDQPPDFLDFLRKAFKG----PLIAAGGY 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 1859084183 293 nTPEVAERLLADGYCDMVSMARPFLADAEFVRKAREG 329
Cdd:cd02933 295 -DAESAEAALADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
8-334 |
7.49e-53 |
|
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: 185.98 E-value: 7.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMhvGLEEAPNGF--ERMAAFYAERARGEAGLIVTGGFAPnerGRPAAGGA----MLTTEA 81
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPM--TRSFSPGGVpgQDVAAYYRRRAAGGVGLIITEGTAV---DHPAASGDpnvpRFHGED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 82 EAERHRVVTRAVHAAGGKIALQILHFG-----RYAYHPALAA--PSALKAPINPFTpHALSSDEVDETIGDFVRCAALAQ 154
Cdd:cd04747 76 ALAGWKKVVDEVHAAGGKIAPQLWHVGamrklGTPPFPDVPPlsPSGLVGPGKPVG-REMTEADIDDVIAAFARAAADAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 155 HAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTL---- 230
Cdd:cd04747 155 RLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTARLadtp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 231 DEVIRLAQAIEAAGATIIN----------------TGIGWHEA--RIPTIAT------KVPRAAYAwvtrqlmgkvGIPL 286
Cdd:cd04747 235 DELEALLAPLVDAGVDIFHcstrrfwepefegselNLAGWTKKltGLPTITVgsvgldGDFIGAFA----------GDEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1859084183 287 VATNRIntpEVAERLLADGYCDMVSMARPFLADAEFVRKAREGRADEI 334
Cdd:cd04747 305 ASPASL---DRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDEL 349
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
8-329 |
1.60e-49 |
|
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: 176.24 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGF-TSLRNRVLMGSMHVGL---EEAPNgfERMAAFYAERARGEAGLIVTGGFA--PNERGRP-AAGGAMLTTE 80
Cdd:cd04733 1 LGQPLTLPNgATLPNRLAKAAMSERLadgRGLPT--PELIRLYRRWAEGGIGLIITGNVMvdPRHLEEPgIIGNVVLESG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 81 AEAERHRVVTRAVHAAGGKIALQILHFGRYAYHPALAAPSALKAPINP-------FTPHALSSDEVDETIGDFVRCAALA 153
Cdd:cd04733 79 EDLEAFREWAAAAKANGALIWAQLNHPGRQSPAGLNQNPVAPSVALDPgglgklfGKPRAMTEEEIEDVIDRFAHAARLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 154 QHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGGSTLDEV 233
Cdd:cd04733 159 QEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 234 IRLAQAIEAAGATIINTGIGWHEAriPTIATKVP-----RAAY----AWVTRQlmgKVGIPLVATNRINTPEVAERLLAD 304
Cdd:cd04733 239 LEVVEALEEAGVDLVELSGGTYES--PAMAGAKKestiaREAYflefAEKIRK---VTKTPLMVTGGFRTRAAMEQALAS 313
|
330 340
....*....|....*....|....*
gi 1859084183 305 GYCDMVSMARPFLADAEFVRKAREG 329
Cdd:cd04733 314 GAVDGIGLARPLALEPDLPNKLLAG 338
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
8-338 |
2.40e-40 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 150.62 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMGSMHVGLEEAPNGFER--MAAFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEAER 85
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTnfHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 86 HRVVTRAVHAAGGKIALQILHFGRYAYHPALA-APSALKAPINPFTPHALSSDEVDETIGDFVRCAALAQHAGYDGVEIM 164
Cdd:PRK13523 83 LHKLVTFIHDHGAKAAIQLAHAGRKAELEGDIvAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 165 GSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIViyRLSMLDLVEGGSTLDEVIRLAQAIEAAG 244
Cdd:PRK13523 163 GAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVWDGPLFV--RISASDYHPGGLTVQDYVQYAKWMKEQG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 245 ATIINTGIG-WHEARIPTI-ATKVPraaYAWVTRQlmgKVGIPLVATNRINTPEVAERLLADGYCDMVSMARPFLADAEF 322
Cdd:PRK13523 241 VDLIDVSSGaVVPARIDVYpGYQVP---FAEHIRE---HANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNPYF 314
|
330
....*....|....*.
gi 1859084183 323 VRKAregrADEINTCI 338
Cdd:PRK13523 315 PRIA----AKELGFEI 326
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
6-320 |
3.01e-36 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 145.47 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 6 PHLTTPLELGFTSLRNRVLMG--SMHVGLEEAPNGFERMaaFYAERARGEAGLIVTGGFAPNERGRPAAGGAMLTTEAEA 83
Cdd:PRK08255 397 PPMFTPFRLRGLTLKNRVVVSpmAMYSAVDGVPGDFHLV--HLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 84 ERHRVVTRAVHA-AGGKIALQILHFGRYAY---------HP------ALAAPSALKAPINPFTPHALSSDEVDETIGDFV 147
Cdd:PRK08255 475 AAWKRIVDFVHAnSDAKIGIQLGHSGRKGStrlgwegidEPleegnwPLISASPLPYLPGSQVPREMTRADMDRVRDDFV 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 148 RCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSMLDLVEGG 227
Cdd:PRK08255 555 AAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGG 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 228 STLDEVIRLAQAIEAAGATIIN--TGIGWHEARiPTIAT--KVPraaYAWVTRQlmgKVGIPLVATNRINTPEVAERLLA 303
Cdd:PRK08255 635 NTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYGRmyQTP---FADRIRN---EAGIATIAVGAISEADHVNSIIA 707
|
330
....*....|....*..
gi 1859084183 304 DGYCDMVSMARPFLADA 320
Cdd:PRK08255 708 AGRADLCALARPHLADP 724
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
1-365 |
7.60e-36 |
|
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: 139.03 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 1 MTSRYPHLTTPLELGFTSLRNRVL-------MGSMHVGLeeapngferMAAFYAERARGEAGLIVTG----GFAPNERGR 69
Cdd:cd02929 1 RDPRHDILFEPIKIGPVTARNRFYqvphcngMGYRKPSA---------QAAMRGIKAEGGWGVVNTEqcsiHPSSDDTPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 70 PAAggaMLTTEAEAERHRVVTRAVHAAGGKIALQILHFG-----RYAYHPALAaPSALK---APINPFTPHALSSDEVDE 141
Cdd:cd02929 72 ISA---RLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGahapnRESRETPLG-PSQLPsefPTGGPVQAREMDKDDIKR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 142 TIGDFVRCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFIVIYRLSML 221
Cdd:cd02929 148 VRRWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 222 DLV--EGGSTLDEVIRLaqaIEAAGATI----INTG--IGWHE-ARIPTIATKVPraayaWVT--RQLMGKvgiPLVATN 290
Cdd:cd02929 228 ELIgpGGIESEGEGVEF---VEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEP-----YIKfvKQVTSK---PVVGVG 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859084183 291 RINTPEVAERLLADGYCDMVSMARPFLADAEFVRKAREGRADEINTCIGCNqACLDHTFSGRITSCLVNPRACHE 365
Cdd:cd02929 297 RFTSPDKMVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
8-329 |
2.15e-31 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 125.99 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 8 LTTPLELGFTSLRNRVLMG------SMHVGLEEAPngfeRMAAFYAERArgEAGLIVTGGFAPNERGRPAAGGAMLTTEA 81
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMApltrlrSIEPGDIPTP----LMAEYYRQRA--SAGLIISEATQISAQAKGYAGAPGLHSPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 82 EAERHRVVTRAVHAAGGKIALQILHFGRYAYHP------ALAAPSALKAP--------------INPFTPHALSSDEVDE 141
Cdd:PRK10605 77 QIAAWKKITAGVHAEGGHIAVQLWHTGRISHASlqpggqAPVAPSAINAGtrtslrdengqairVETSTPRALELEEIPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 142 TIGDFVRCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRV-----RERVGtnfIVIY 216
Cdd:PRK10605 157 IVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGiaewgADRIG---IRIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 217 RLSMLDLVEGGStlDEvirlaqaiEAAGATIINT----GIGWHEARIPTIATKVP-RAAYAWVTRQLMGKVGIPLVATnr 291
Cdd:PRK10605 234 PLGTFNNVDNGP--NE--------EADALYLIEQlgkrGIAYLHMSEPDWAGGEPySDAFREKVRARFHGVIIGAGAY-- 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 1859084183 292 inTPEVAERLLADGYCDMVSMARPFLADAEFVRKAREG 329
Cdd:PRK10605 302 --TAEKAETLIGKGLIDAVAFGRDYIANPDLVARLQRK 337
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
1-219 |
4.14e-26 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 111.10 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 1 MTSRYPHLTTPLELGFTSLRNRVLMGSMHVGleEAPNGF--ERMAAFYAERARgEAGLIVTGG--FAPNERGRPAAGGam 76
Cdd:PLN02411 5 QGNSNETLFSPYKMGRFDLSHRVVLAPMTRC--RALNGIpnAALAEYYAQRST-PGGFLISEGtlISPTAPGFPHVPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 77 LTTEAEAERHRVVTRAVHAAGGKIALQILHFGR---YAYHPALAAP-SALKAPIN---------------PfTPHALSSD 137
Cdd:PLN02411 80 IYSDEQVEAWKKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISerwrilmpdgsygkyP-KPRALETS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 138 EVDETIGDFVRCAALAQHAGYDGVEIMGSEGYLINEFVAARTNHRDDAWGGAYESRIRFPVEIVRRVRERVGTNFiVIYR 217
Cdd:PLN02411 159 EIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVR 237
|
..
gi 1859084183 218 LS 219
Cdd:PLN02411 238 VS 239
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
370-631 |
5.70e-21 |
|
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: 95.97 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 370 IRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGqfnvakkvpgkeefneTLRY----FR---------- 435
Cdd:COG0493 115 PPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG----------------LLRYgipeFRlpkdvldrei 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 436 RQIELRGVTLHLNTR----ATAEMLLqREFDEVVIATGI-VPRTPPIDGVGHAR---ALGYLDVLRDGK------AVGRN 501
Cdd:COG0493 179 ELIEALGVEFRTNVEvgkdITLDELL-EEFDAVFLATGAgKPRDLGIPGEDLKGvhsAMDFLTAVNLGEapdtilAVGKR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 502 VAIVGAGGIGFDVAeYLAHREGAEHV------DADRFfaewgvdPsyANAGGLRHARPEpAARQIHLLQRKASkVGDGLG 575
Cdd:COG0493 258 VVVIGGGNTAMDCA-RTALRLGAESVtivyrrTREEM-------P--ASKEEVEEALEE-GVEFLFLVAPVEI-IGDENG 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1859084183 576 KTTG-WIHRTALKARgvgmssavtyrriDDDGFH--VTIDGVEQTLPVDNVVICAGQEP 631
Cdd:COG0493 326 RVTGlECVRMELGEP-------------DESGRRrpVPIEGSEFTLPADLVILAIGQTP 371
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
364-527 |
4.21e-20 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 93.71 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 364 HETELVIRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG-------QFNVAKKVPGKEEfnetlryfrR 436
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllrygipEFRLPKDIVDREV---------E 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 437 QIELRGVTLHLNTR----ATAEMLLQrEFDEVVIATGI-VPRTPPIDGVGHA---RALGYLDVLRDGKA-----VGRNVA 503
Cdd:PRK11749 199 RLLKLGVEIRTNTEvgrdITLDELRA-GYDAVFIGTGAgLPRFLGIPGENLGgvySAVDFLTRVNQAVAdydlpVGKRVV 277
|
170 180
....*....|....*....|....
gi 1859084183 504 IVGAGGIGFDVAEyLAHREGAEHV 527
Cdd:PRK11749 278 VIGGGNTAMDAAR-TAKRLGAESV 300
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
377-639 |
1.63e-18 |
|
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: 86.60 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEI-GGQFNVAKKVPGKEEFNETLRYFRRQIEL---------RGVTLH 446
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 447 LNTRAT------AEMLLQR---------EFDEVVIATGIVPRTPPIDGVgHARALGYLDVLRDGKA-----VGRNVAIVG 506
Cdd:pfam07992 81 LGTEVVsidpgaKKVVLEElvdgdgetiTYDRLVIATGARPRLPPIPGV-ELNVGFLVRTLDSAEAlrlklLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 507 AGGIGFDVAEYLAHregaehvdadrffaewgvdpsyanagglrharpepAARQIHLLQRkASKVGDGLGKTTGWIHRTAL 586
Cdd:pfam07992 160 GGYIGVELAAALAK-----------------------------------LGKEVTLIEA-LDRLLRAFDEEISAALEKAL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1859084183 587 KARGVGMSSAVTYRRIDDDGFHVT-IDGVEQTLPVDNVVICAGQEPLRELAEQL 639
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIIGDGDGVEvILKDGTEIDADLVVVAIGRRPNTELLEAA 257
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
371-527 |
2.67e-17 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 85.22 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 371 RPARQR--KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG-------QFNVAKKVPGKEefnetlryfRRQIELR 441
Cdd:PRK12810 136 DPPVKRtgKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipDFKLEKEVIDRR---------IELMEAE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 442 GVTLHLNTRA----TAEMLLQrEFDEVVIATGI-VPRTPPI-----DGVgHArALGYL-----DVLRDGK-----AVGRN 501
Cdd:PRK12810 207 GIEFRTNVEVgkdiTAEELLA-EYDAVFLGTGAyKPRDLGIpgrdlDGV-HF-AMDFLiqntrRVLGDETepfisAKGKH 283
|
170 180
....*....|....*....|....*..
gi 1859084183 502 VAIVGAGGIGFD-VAEylAHREGAEHV 527
Cdd:PRK12810 284 VVVIGGGDTGMDcVGT--AIRQGAKSV 308
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
377-630 |
3.72e-17 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 85.31 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQfnvakkvpgkeefnetLRY----FR----------RQIELRG 442
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGM----------------MRYgipaYRlprevldaeiQRILDLG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 443 VTLHLNTR----ATAEMlLQREFDEVVIATGI-VPRTPPIDGVGHARALGYLDVLR-----DGKAVGRNVAIVGAGGIGF 512
Cdd:PRK12771 202 VEVRLGVRvgedITLEQ-LEGEFDAVFVAIGAqLGKRLPIPGEDAAGVLDAVDFLRavgegEPPFLGKRVVVIGGGNTAM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 513 DVAEyLAHREGAEHV------DADRFFAEwgvdpsyanagglrHARPEPAAR---QIHLLQRKASKVGDGLGKTTGWIHR 583
Cdd:PRK12771 281 DAAR-TARRLGAEEVtivyrrTREDMPAH--------------DEEIEEALRegvEINWLRTPVEIEGDENGATGLRVIT 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1859084183 584 TALKArgvgmssavtyrrIDDDGFHVTIDGVEQTLPVDNVVICAGQE 630
Cdd:PRK12771 346 VEKME-------------LDEDGRPSPVTGEEETLEADLVVLAIGQD 379
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
371-527 |
1.80e-14 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 75.41 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 371 RPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQfnVAKKVPGKEEFNETLRYFRRQIELRGVTLHLNTR 450
Cdd:PRK12770 13 KPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGL--MLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 451 ATAEMLLQRE------------------FDEVVIATGI-VPRTPPIDGVG--------------HARALGYLDVLRDGKA 497
Cdd:PRK12770 91 VCCGEPLHEEegdefverivsleelvkkYDAVLIATGTwKSRKLGIPGEDlpgvysaleylfriRAAKLGYLPWEKVPPV 170
|
170 180 190
....*....|....*....|....*....|
gi 1859084183 498 VGRNVAIVGAGGIGFDVAeYLAHREGAEHV 527
Cdd:PRK12770 171 EGKKVVVVGAGLTAVDAA-LEAVLLGAEKV 199
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
376-638 |
2.00e-14 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 75.56 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAERGHV--VTLYeaGAEIGGQFN---VAKKVPGKEEFNETLRYFRRQIELRGVTLHLNTR 450
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDgeITVI--GAEPHPPYNrppLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 451 ATA-------------EMLlqrEFDEVVIATGIVPRTPPIDGVGHARALGY-----LDVLRDGKAVGRNVAIVGAGGIGF 512
Cdd:COG1251 79 VTAidraartvtladgETL---PYDKLVLATGSRPRVPPIPGADLPGVFTLrtlddADALRAALAPGKRVVVIGGGLIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 513 DVAEYLAHRegaehvdadrffaewGVDPSYAnagglrHARPEPAARQihllqrkaskvgdgLGKTTGWIHRTALKARGVG 592
Cdd:COG1251 156 EAAAALRKR---------------GLEVTVV------ERAPRLLPRQ--------------LDEEAGALLQRLLEALGVE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1859084183 593 MSSAVTYRRIDDDGfHVTidGVE----QTLPVDNVVICAGQEPLRELAEQ 638
Cdd:COG1251 201 VRLGTGVTEIEGDD-RVT--GVRladgEELPADLVVVAIGVRPNTELARA 247
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
379-639 |
3.09e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 70.92 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 379 IAVVGAGPAGLGFAITAAERGHVVTLYEAGaEIGGQFNVAKKV---PGKEEF---NETLRYFRRQIELRGVTLHLnTRAT 452
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQLATTKEIenyPGFPEGisgPELAERLREQAERFGAEILL-EEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 453 AEMLLQREF------------DEVVIATGIVPRTPPIDGVGHARALG-YLDVLRDG-KAVGRNVAIVGAGGIGFDVAEYL 518
Cdd:COG0492 81 SVDKDDGPFrvttddgteyeaKAVIIATGAGPRKLGLPGEEEFEGRGvSYCATCDGfFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 519 AHRegAEHVDadrffaewgvdpsyanaggLRHARPEPAARQIHLLQ-RKASKVgdglgkttGWIHRTALKA-RGVGMSSA 596
Cdd:COG0492 161 TKF--ASKVT-------------------LIHRRDELRASKILVERlRANPKI--------EVLWNTEVTEiEGDGRVEG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1859084183 597 VTYRRIDddgfhvtiDGVEQTLPVDNVVICAGQEPLRELAEQL 639
Cdd:COG0492 212 VTLKNVK--------TGEEKELEVDGVFVAIGLKPNTELLKGL 246
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
364-638 |
2.89e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 69.28 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 364 HETELVIRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG-------QFNVAKKVPGKEEFNEtlryfrr 436
Cdd:PRK12831 128 NGIDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlvygipEFRLPKETVVKKEIEN------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 437 qIELRGVTLHLNT----RATAEMLLQRE-FDEVVIATGI-VPRTPPIDGV---GHARALGYLDVLRDGKA---------- 497
Cdd:PRK12831 201 -IKKLGVKIETNVvvgkTVTIDELLEEEgFDAVFIGSGAgLPKFMGIPGEnlnGVFSANEFLTRVNLMKAykpeydtpik 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 498 VGRNVAIVGAGGIGFDVAEyLAHREGAE-HVDADRffaewGVDPSYANAGGLRHARPEpaARQIHLLQRKASKVGDglgk 576
Cdd:PRK12831 280 VGKKVAVVGGGNVAMDAAR-TALRLGAEvHIVYRR-----SEEELPARVEEVHHAKEE--GVIFDLLTNPVEILGD---- 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1859084183 577 TTGWIHRTALKARGVGMSSAVTYRRIdddgfhVTIDGVEQTLPVDNVVICAGQEPLRELAEQ 638
Cdd:PRK12831 348 ENGWVKGMKCIKMELGEPDASGRRRP------VEIEGSEFVLEVDTVIMSLGTSPNPLISST 403
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
402-521 |
4.12e-11 |
|
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: 64.83 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 402 VTLYEAGAEIGGQ-----FNVAKkvpGKEEFNETLRYFRRQIELRGVTLHLNTRATAemlLQRE-------------FDE 463
Cdd:COG0446 8 ITVIEKGPHHSYQpcglpYYVGG---GIKDPEDLLVRTPESFERKGIDVRTGTEVTA---IDPEaktvtlrdgetlsYDK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859084183 464 VVIATGIVPRTPPIDG-----VGHARALGYLDVLRD--GKAVGRNVAIVGAGGIGFDVAEYLAHR 521
Cdd:COG0446 82 LVLATGARPRPPPIPGldlpgVFTLRTLDDADALREalKEFKGKRAVVIGGGPIGLELAEALRKR 146
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
370-519 |
5.44e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 65.56 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 370 IRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNVAkkVPGKEEFNETLRYFRRQIELRGVTLHLNT 449
Cdd:PRK13984 277 DEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHLNT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 450 RATAE---MLLQREFDEVVIATGI-VPRTPPIDGVGHARALGYLDVLR--------DGKA--VGRNVAIVGAGGIGFDVA 515
Cdd:PRK13984 355 RVGKDiplEELREKHDAVFLSTGFtLGRSTRIPGTDHPDVIQALPLLReirdylrgEGPKpkIPRSLVVIGGGNVAMDIA 434
|
....
gi 1859084183 516 EYLA 519
Cdd:PRK13984 435 RSMA 438
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
377-631 |
7.63e-11 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 65.53 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG-------QFNVAKKVPgKEEFnETLRYFRRQIE---LRGVTLh 446
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGvlkygipEFRLPKKIV-DVEI-ENLKKLGVKFEtdvIVGKTI- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 447 lntraTAEMLLQREFDEVVIATGI-VPRTPPIDG---VGHARALGYL------DVLRDGKA----VGRNVAIVGAGGIGF 512
Cdd:PRK12778 509 -----TIEELEEEGFKGIFIASGAgLPNFMNIPGensNGVMSSNEYLtrvnlmDAASPDSDtpikFGKKVAVVGGGNTAM 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 513 DVAEyLAHREGAEHVDADRFFAEwgvDPSYANAGGLRHARPEpaARQIHLLQRKASKVGDglgkTTGWIHRTALKARGVG 592
Cdd:PRK12778 584 DSAR-TAKRLGAERVTIVYRRSE---EEMPARLEEVKHAKEE--GIEFLTLHNPIEYLAD----EKGWVKQVVLQKMELG 653
|
250 260 270
....*....|....*....|....*....|....*....
gi 1859084183 593 MSSAVTYRRidddgfHVTIDGVEQTLPVDNVVICAGQEP 631
Cdd:PRK12778 654 EPDASGRRR------PVAIPGSTFTVDVDLVIVSVGVSP 686
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
377-527 |
1.46e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 61.28 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGqfnvakkvpgkeefneTLRY----FR----------RQIELRG 442
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG----------------MMRYgiprFRlpesvidadiAPLRAMG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 443 VTLHLNTR-----ATAEmlLQREFDEVVIATGIVPRT----PPIDGVGHARALGYLDVLRDGKAV--GRNVAIVGAGGIG 511
Cdd:PRK12814 258 AEFRFNTVfgrdiTLEE--LQKEFDAVLLAVGAQKASkmgiPGEELPGVISGIDFLRNVALGTALhpGKKVVVIGGGNTA 335
|
170
....*....|....*.
gi 1859084183 512 FDVAEyLAHREGAEHV 527
Cdd:PRK12814 336 IDAAR-TALRLGAESV 350
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
371-528 |
3.20e-08 |
|
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: 56.41 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 371 RPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG-------------------QF------NVAKKVPGKE 425
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpshlySLpffpnwSDDPDFPTGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 426 EFNETLRYFRRQIELRGvTLHLNTRATAEML--------------LQREFDEVVIATGI--VPRTPPIDGVG-------H 482
Cdd:COG2072 81 EILAYLEAYADKFGLRR-PIRFGTEVTSARWdeadgrwtvttddgETLTARFVVVATGPlsRPKIPDIPGLEdfageqlH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1859084183 483 ARALGYLDVLRdgkavGRNVAIVGAGGIGFDVAEYLAHRegAEHVD 528
Cdd:COG2072 160 SADWRNPVDLA-----GKRVLVVGTGASAVQIAPELARV--AAHVT 198
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
35-314 |
6.38e-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: 53.36 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 35 APNGFERMAAFYAERARGEAGLIVTGGFAPNergrpaaggamlTTEAEAERHRVVTRAVHAAGGKIALQILHfgryayHP 114
Cdd:cd04722 7 AGGPSGDPVELAKAAAEAGADAIIVGTRSSD------------PEEAETDDKEVLKEVAAETDLPLGVQLAI------ND 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 115 ALAAPSALkapinpftphalssdevdetigdfvrcAALAQHAGYDGVEIMGSEGYlinefvaartnhrddawggayesRI 194
Cdd:cd04722 69 AAAAVDIA---------------------------AAAARAAGADGVEIHGAVGY-----------------------LA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 195 RFPVEIVRRVRERVGtNFIVIYRLSMLDLVEggstldevirlAQAIEAAGATIINTGIGWHEARIPTIATKVpraayAWV 274
Cdd:cd04722 99 REDLELIRELREAVP-DVKVVVKLSPTGELA-----------AAAAEEAGVDEVGLGNGGGGGGGRDAVPIA-----DLL 161
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1859084183 275 TRQLMGKVGIPLVATNRINTPEVAERLLADGyCDMVSMAR 314
Cdd:cd04722 162 LILAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
378-413 |
2.48e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 53.74 E-value: 2.48e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1859084183 378 RIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
359-481 |
6.83e-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: 51.55 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 359 NPRACHETELvIRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNvakkvpgkEEFNETLryfRRQI 438
Cdd:pfam07992 136 LVRTLDSAEA-LRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFD--------EEISAAL---EKAL 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1859084183 439 ELRGVTLHLNTRATA--------EMLL----QREFDEVVIATGIVPRTPPIDGVG 481
Cdd:pfam07992 204 EKNGVEVRLGTSVKEiigdgdgvEVILkdgtEIDADLVVVAIGRRPNTELLEAAG 258
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
376-413 |
1.59e-06 |
|
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: 50.99 E-value: 1.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
379-511 |
2.40e-06 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 50.47 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 379 IAVVGAGPAGLGFAITAAERGHVVTLYEAGaEIGG------------------QFNVAKKVP------GKEEFN-ETLRY 433
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGGtclnvgcipskallhaaeVAHEARHAAefgisaGAPSVDwAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 434 FRRQI--ELRGVTLHLNTRATAEMLLQR-----------------EFDEVVIATGIVPRTPPIDGVGHARALGYLDVLRD 494
Cdd:COG1249 85 RKDKVvdRLRGGVEELLKKNGVDVIRGRarfvdphtvevtggetlTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALEL 164
|
170
....*....|....*..
gi 1859084183 495 gKAVGRNVAIVGAGGIG 511
Cdd:COG1249 165 -EELPKSLVVIGGGYIG 180
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
377-412 |
4.42e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 49.50 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIG 412
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
381-414 |
5.75e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 44.44 E-value: 5.75e-06
10 20 30
....*....|....*....|....*....|....
gi 1859084183 381 VVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQ 414
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
376-413 |
6.32e-06 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 49.08 E-value: 6.32e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
376-644 |
7.52e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 48.59 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAER---GHVVT-------------LYEAGAeiggqfnvakkvpGKEEFNETLRYFRRQIE 439
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKlggDAEVTlidpnpyhlfqplLPEVAA-------------GTLSPDDIAIPLRELLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 440 LRGVTLHLNT---------RATAEMLLQREFDEVVIATGIVPRTPPIDGVG----------HARALG--YLDVLRDGKAV 498
Cdd:COG1252 68 RAGVRFIQGEvtgidpearTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAehalplktleDALALRerLLAAFERAERR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 499 GR-NVAIVGAGGIGFDVA----EYLAHREGAEHVDADRFfaewgvdpsyanagglrharpepaarQIHLLQRkASKVGDG 573
Cdd:COG1252 148 RLlTIVVVGGGPTGVELAgelaELLRKLLRYPGIDPDKV--------------------------RITLVEA-GPRILPG 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859084183 574 LGKTTGWIHRTALKARGVG--MSSAVTyrRIDDDGFHVTiDGveQTLPVDNVVICAG---QEPLRELAEQLEAAGR 644
Cdd:COG1252 201 LGEKLSEAAEKELEKRGVEvhTGTRVT--EVDADGVTLE-DG--EEIPADTVIWAAGvkaPPLLADLGLPTDRRGR 271
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
380-412 |
8.26e-06 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 48.51 E-value: 8.26e-06
10 20 30
....*....|....*....|....*....|...
gi 1859084183 380 AVVGAGPAGLGFAITAAERGHVVTLYEAGAEIG 412
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
377-474 |
1.31e-05 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 47.50 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNvakkvpgkEEFNETLryfRRQIELRGVTLHLNTRATA--- 453
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLD--------PEMAALL---EEELREHGVELRLGETVVAidg 193
|
90 100
....*....|....*....|....*....
gi 1859084183 454 ----EMLLQR----EFDEVVIATGIVPRT 474
Cdd:COG0446 194 ddkvAVTLTDgeeiPADLVVVAPGVRPNT 222
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
375-413 |
1.34e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.96 E-value: 1.34e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1859084183 375 QRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:PRK07208 3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
378-453 |
1.41e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 43.73 E-value: 1.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1859084183 378 RIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNvakkvpgkeefNETLRYFRRQIELRGVTLHLNTRATA 453
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFD-----------PEIAKILQEKLEKNGIEFLLNTTVEA 65
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
373-474 |
1.75e-05 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 47.44 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 373 ARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGA--------EIGGQFnvakkvpgkeefnetlryFRRQIELRGVT 444
Cdd:COG1251 139 LAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPrllprqldEEAGAL------------------LQRLLEALGVE 200
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1859084183 445 LHLNTRATA--------EMLL----QREFDEVVIATGIVPRT 474
Cdd:COG1251 201 VRLGTGVTEiegddrvtGVRLadgeELPADLVVVAIGVRPNT 242
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
375-413 |
2.14e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 47.54 E-value: 2.14e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1859084183 375 QRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
361-450 |
3.55e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.78 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 361 RACHETELVIRPARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFN-VAKKVPGKEEFNETLRYFRRQIE 439
Cdd:COG1148 125 KAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPGLDCPQCILEPLIAEVE 204
|
90
....*....|..
gi 1859084183 440 L-RGVTLHLNTR 450
Cdd:COG1148 205 AnPNITVYTGAE 216
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
375-513 |
4.54e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 46.56 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 375 QRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNVAkkVPgKEEFNETLRYFRRQI-ELRGVTLHLNTRATA 453
Cdd:PRK12809 309 RSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG--IP-PFKLDKTVLSQRREIfTAMGIDFHLNCEIGR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 454 EML---LQREFDEVVIATG----IVPRTPPIDGVGHARALGYLDV-LRDGKAV------------GRNVAIVGAGGIGFD 513
Cdd:PRK12809 386 DITfsdLTSEYDAVFIGVGtygmMRADLPHEDAPGVIQALPFLTAhTRQLMGLpeseeypltdveGKRVVVLGGGDTTMD 465
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
376-413 |
1.30e-04 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 44.72 E-value: 1.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1859084183 376 RKRIAVVGAGPAGLgfaiTAAE---RGHVVTLYEAGAEIGG 413
Cdd:COG2907 3 RMRIAVIGSGISGL----TAAWllsRRHDVTLFEANDRLGG 39
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
374-535 |
3.75e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 43.37 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 374 RQRKRIAVVGAGPAGLgfaiTAA----ERGHVVTLYEAG------------------AEIGGQFnvakkVPGK------- 424
Cdd:COG1231 5 ARGKDVVIVGAGLAGL----AAArelrKAGLDVTVLEARdrvggrvwtlrfgddglyAELGAMR-----IPPShtnllal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 425 -EEFNETLRYFRRQ-----IELRGVTLHLNTRATAEMLLQREFDEVV--IATGIVPRTPPIDGVGHARALGYLDVLRDGK 496
Cdd:COG1231 76 aRELGLPLEPFPNEngnalLYLGGKRVRAGEIAADLRGVAELLAKLLraLAAALDPWAHPAAELDRESLAEWLRRNGASP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1859084183 497 AVGRNVAIVGAGGIG-----FDVAEYLAHREGAEHVDADRFFAE 535
Cdd:COG1231 156 SARRLLGLLGAGEYGadpdeLSLLDLLRYAASAGGGAQQFRIVG 199
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
377-474 |
4.20e-04 |
|
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: 43.15 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNvakkvpgkEEFNETLRyfrRQIELRGVTLHLNTRATA--- 453
Cdd:COG1249 169 KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGED--------PEISEALE---KALEKEGIDILTGAKVTSvek 237
|
90 100 110
....*....|....*....|....*....|...
gi 1859084183 454 ------------EMLLQREFDEVVIATGIVPRT 474
Cdd:COG1249 238 tgdgvtvtledgGGEEAVEADKVLVATGRRPNT 270
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
377-522 |
4.78e-04 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 43.11 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAA--ERGHVVTLYEA------GA-----EIGGQF----NVAKKVPgkEEFNETlryfrrQIE 439
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKrlNKELEITVYEKtdivsfGAcglpyFVGGFFddpnTMIARTP--EEFIKS------GID 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 440 LRGVTLHLNTRATAEMLLQRE----------FDEVVIATGIVPRTPPIDGVgHARALGYLDVLRDGKAVG--------RN 501
Cdd:PRK09564 73 VKTEHEVVKVDAKNKTITVKNlktgsifndtYDKLMIATGARPIIPPIKNI-NLENVYTLKSMEDGLALKellkdeeiKN 151
|
170 180
....*....|....*....|.
gi 1859084183 502 VAIVGAGGIGFDVAEYLAHRE 522
Cdd:PRK09564 152 IVIIGAGFIGLEAVEAAKHLG 172
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
376-414 |
4.90e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 43.70 E-value: 4.90e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQ 414
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
377-477 |
5.77e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 42.81 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIggqfnvakkVPGKEEFNETLRyfRRQIELRGVTLHLNTRATA--- 453
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI---------LPREEPSVAALA--KQYMEEDGITFLLNAHTTEvkn 226
|
90 100 110
....*....|....*....|....*....|..
gi 1859084183 454 ---EMLLQRE-----FDEVVIATGIVPRTPPI 477
Cdd:PRK07251 227 dgdQVLVVTEdetyrFDALLYATGRKPNTEPL 258
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
376-413 |
6.36e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 6.36e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1859084183 376 RKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:COG3380 3 MPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
357-413 |
9.33e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 42.51 E-value: 9.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1859084183 357 LVNPRACHETELVIRP--ARQRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:PRK12779 285 LVNPNANERFAGRISPwaAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGG 343
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
377-469 |
1.10e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 42.04 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 377 KRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQFNVAkkVPGKeEFNETLRYFRRQI-ELRGVTLHLNTRATAEM 455
Cdd:PRK12769 328 KRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFG--IPAF-KLDKSLLARRREIfSAMGIEFELNCEVGKDI 404
|
90
....*....|....*..
gi 1859084183 456 L---LQREFDEVVIATG 469
Cdd:PRK12769 405 SlesLLEDYDAVFVGVG 421
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
199-310 |
1.38e-03 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 40.64 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 199 EIVRRVRERVGtnfiviyRLSMLDLveggSTLDEVIRLAQAieaaGATIINTGI-GWHEARiptiaTKVPRAAYAWVtRQ 277
Cdd:cd04729 113 ELIKRIHEEYN-------CLLMADI----STLEEALNAAKL----GFDIIGTTLsGYTEET-----AKTEDPDFELL-KE 171
|
90 100 110
....*....|....*....|....*....|...
gi 1859084183 278 LMGKVGIPLVATNRINTPEVAERLLADGyCDMV 310
Cdd:cd04729 172 LRKALGIPVIAEGRINSPEQAAKALELG-ADAV 203
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
194-310 |
2.49e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 40.67 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 194 IRFPVEIVRRVRERVGTNFiviyRLsMLDlVEGGSTLDEVIRLAQAIEAAgatiintGIGWHEARIPTiatkVPRAAYAW 273
Cdd:cd03316 172 LREDLARVRAVREAVGPDV----DL-MVD-ANGRWDLAEAIRLARALEEY-------DLFWFEEPVPP----DDLEGLAR 234
|
90 100 110
....*....|....*....|....*....|....*..
gi 1859084183 274 VTRQLmgkvGIPLVATNRINTPEVAERLLADGYCDMV 310
Cdd:cd03316 235 LRQAT----SVPIAAGENLYTRWEFRDLLEAGAVDII 267
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
198-310 |
2.51e-03 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 40.58 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 198 VEIVRRVRERVGTNFIViyrlsMLDlVEGGSTLDEVIRLAQAIEAAGatiintgIGWHEAriPTIATKVprAAYAWVTRQ 277
Cdd:COG4948 169 VERVRAVREAVGPDARL-----RVD-ANGAWTLEEAIRLLRALEDLG-------LEWIEQ--PLPAEDL--EGLAELRRA 231
|
90 100 110
....*....|....*....|....*....|...
gi 1859084183 278 lmgkVGIPLVATNRINTPEVAERLLADGYCDMV 310
Cdd:COG4948 232 ----TPVPIAADESLTSRADFRRLIEAGAVDIV 260
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
367-472 |
2.71e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 40.50 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 367 ELVIRPARQRK-RIAVVGAGPAGLGFAITAAERGHV-------------VTLYEAGAEIGGqfnvakkvpgkeEFNETLR 432
Cdd:COG1252 139 AAFERAERRRLlTIVVVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRILP------------GLGEKLS 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1859084183 433 -YFRRQIELRGVTLHLNTRATA----EMLLQR----EFDEVVIATGIVP 472
Cdd:COG1252 207 eAAEKELEKRGVEVHTGTRVTEvdadGVTLEDgeeiPADTVIWAAGVKA 255
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
379-414 |
3.67e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 40.28 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1859084183 379 IAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQ 414
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
439-674 |
4.96e-03 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 40.20 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 439 ELRGVTLHLNTRATAEMLLQRE----------FDEVVIATGIVPRTPPIDGVGHARALGY-----LDVLRDGKAVGRNVA 503
Cdd:TIGR02374 65 EKHGITLYTGETVIQIDTDQKQvitdagrtlsYDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 504 IVGAGGIGFDVAEYLAHREGAEHV--DADRFFAEwGVDpsyANAGGLRHARPEPAARQIHLLQRKASKVGDGLGKTTGWI 581
Cdd:TIGR02374 145 VIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAK-QLD---QTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859084183 582 HRTALKARGVGMSSAVTYRridddgfhvTIDGVEQTLPVDNVVI----CAGQEP-LRELAEQLEAAGRKVHVIGGAYEAA 656
Cdd:TIGR02374 221 DGSSLEADLIVMAAGIRPN---------DELAVSAGIKVNRGIIvndsMQTSDPdIYAVGECAEHNGRVYGLVAPLYEQA 291
|
250 260
....*....|....*....|....
gi 1859084183 657 ELDAKR------AIHQGTTLAATL 674
Cdd:TIGR02374 292 KVLADHicgvecEEYEGSDLSAKL 315
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
378-413 |
5.47e-03 |
|
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: 39.69 E-value: 5.47e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1859084183 378 RIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGG 413
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
378-413 |
6.20e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 39.75 E-value: 6.20e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1859084183 378 RIAVVGAGPAGLGFAITAAERGHVVTLYEAGAeIGG 413
Cdd:PRK13748 100 HVAVIGSGGAAMAAALKAVEQGARVTLIERGT-IGG 134
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
378-414 |
6.24e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 39.78 E-value: 6.24e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1859084183 378 RIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIGGQ 414
Cdd:PLN02487 77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGK 113
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
375-412 |
6.73e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 39.15 E-value: 6.73e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1859084183 375 QRKRIAVVGAGPAGLGFAITAAERGHVVTLYEAGAEIG 412
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| |
