|
Name |
Accession |
Description |
Interval |
E-value |
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
7-333 |
5.58e-129 |
|
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: 383.08 E-value: 5.58e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 7 FTPFKIGKMEVKNRLVMSPMGTNSALANGRKTDNEIDYFIERAKGGVGMIIMGCQPLNEKIAQGSMEGYMDSFTVLPSLT 86
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 87 SVCDGVHKYGAKIVCQLTPGtGRNAFPDTLGNPPMSASEIPSAFdPNLMCHALTKEEISKMMDDFKFAAGVAMDAGYDAI 166
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHA-GRQAQPNLTGGPPPAPSAIPSPG-GGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 167 EIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNSGRDLEYSMKILKELE 246
Cdd:cd02803 159 EIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 247 KEGIDAFDIDAGCYETLDYIFPPAYLGESCMSYVCEDARKVVNVPLINAG-THNPESALELIESGNVDFVSFGRALIADP 325
Cdd:cd02803 239 EAGVDALHVSGGSYESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGgIRDPEVAEEILAEGKADLVALGRALLADP 318
|
....*...
gi 2789488066 326 MMPKKLMK 333
Cdd:cd02803 319 DLPNKARE 326
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-370 |
1.50e-127 |
|
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: 380.67 E-value: 1.50e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 1 MSYEKLFTPFKIGKMEVKNRLVMSPMGTNSALANGRKTDNEIDYFIERAKGGVGMIIM-GCQPLNE-KIAQGSMEGYMDS 78
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEDGVPTDLHAAYYAQRARGGAGLIITeATAVSPEgRGYPGQPGIWDDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 79 FtvLPSLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTLGN-PPMSASEIPSAFDPNlMCHALTKEEISKMMDDFKFAAGV 157
Cdd:COG1902 82 Q--IAGLRRVTDAVHAAGGKIFIQLWHA-GRKAHPDLPGGwPPVAPSAIPAPGGPP-TPRALTTEEIERIIEDFAAAARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 158 AMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNSGRDLEY 237
Cdd:COG1902 158 AKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 238 SMKILKELEKEGIDAFDIDAGCYETLDYIfpPAYLGESCMSYVCEDARKVVNVPLI-NAGTHNPESALELIESGNVDFVS 316
Cdd:COG1902 238 SVELAKALEEAGVDYLHVSSGGYEPDAMI--PTIVPEGYQLPFAARIRKAVGIPVIaVGGITTPEQAEAALASGDADLVA 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2789488066 317 FGRALIADPMMPKKLMKNHREDVRPCLRCNeYCIGRIwnhHTKLGCAVNPQAME 370
Cdd:COG1902 316 LGRPLLADPDLPNKAAAGRGDEIRPCIGCN-QCLPTF---YGGASCYVDPRLGR 365
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
6-366 |
3.67e-100 |
|
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: 310.98 E-value: 3.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMGT-NSALANGRKTDNEIDYFIERAKGGVGMIIMGCQPLNEKIAQGSMeGYMDSFTVLP- 83
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMVDNEIEQFPM-PSLPCPTYNPt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 84 ----SLTSVCDGVHKYGAKIVCQLTPGTGRNAFPDTLGN-PPMSASEIPSAFDPNLMCHALTKEEISKMMDDFKFAAGVA 158
Cdd:cd02931 80 afirTAKEMTERVHAYGTKIFLQLTAGFGRVCIPGFLGEdKPVAPSPIPNRWLPEITCRELTTEEVETFVGKFGESAVIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 159 MDAGYDAIEIHA-HAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNS------ 231
Cdd:cd02931 160 KEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSVKSYIKDlrqgal 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 232 --------GRDLEYSMKILKELEKEGIDAFDIDAGCYETLDYIFPPAYLGESCMSYVCEDARKVVNVPLINAG-THNPES 302
Cdd:cd02931 240 pgeefqekGRDLEEGLKAAKILEEAGYDALDVDAGSYDAWYWNHPPMYQKKGMYLPYCKALKEVVDVPVIMAGrMEDPEL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2789488066 303 ALELIESGNVDFVSFGRALIADPMMPKKLMKNHREDVRPCLRCNEYCIGRIWnHHTKLGCAVNP 366
Cdd:cd02931 320 ASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMA-LGGNLSCAVNP 382
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
6-346 |
4.32e-83 |
|
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: 265.25 E-value: 4.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMGTNSAlANGRKTDNEIDYFIERAKGGVGMIIMGCQPLNEK--IAQGSMEGYMDSftVLP 83
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYA-EDGLPSERYIAYHEERARGGAGLIITEGSSVHPSdsPAFGNLNASDDE--IIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 84 SLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTLGNPPMSASEIPSAFDpNLMCHALTKEEISKMMDDFKFAAGVAMDAGY 163
Cdd:cd04734 78 GFRRLAEAVHAHGAVIMIQLTHL-GRRGDGDGSWLPPLAPSAVPEPRH-RAVPKAMEEEDIEEIIAAFADAARRCQAGGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 164 DAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNSGRDLEYSMKILK 243
Cdd:cd04734 156 DGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 244 ELEKEG-IDAFDIDAGCYETLD---YIFPPAYLGESCMSYVCEDARKVVNVPLINAGT-HNPESALELIESGNVDFVSFG 318
Cdd:cd04734 236 RLAAEGlIDYVNVSAGSYYTLLglaHVVPSMGMPPGPFLPLAARIKQAVDLPVFHAGRiRDPAEAEQALAAGHADMVGMT 315
|
330 340
....*....|....*....|....*...
gi 2789488066 319 RALIADPMMPKKLMKNHREDVRPCLRCN 346
Cdd:cd04734 316 RAHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
6-325 |
1.48e-71 |
|
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: 234.70 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMGTNSAlANGRKTDNEIDYFIERAKGGVGMIIM---GCQPlNEKIAQGSMEGYMDSFTvl 82
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSA-EDGVATDWHLVHYGSRALGGAGLVIVeatAVSP-EGRITPGDLGLWNDEQI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 83 PSLTSVCDGVHKYGAKIVCQL----------TP--GTGRNAFPDTLGNPPMSASEIPsaFDPNLMC-HALTKEEISKMMD 149
Cdd:cd02932 77 EALKRIVDFIHSQGAKIGIQLahagrkastaPPweGGGPLLPPGGGGWQVVAPSAIP--FDEGWPTpRELTREEIAEVVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 150 DFKFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRF 229
Cdd:cd02932 155 AFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 230 NSGRDLEYSMKILKELEKEGIDAFDIDAGCYETLDYI-FPPAYlgescMSYVCEDARKVVNVPLINAG--THnPESALEL 306
Cdd:cd02932 235 EGGWDLEDSVELAKALKELGVDLIDVSSGGNSPAQKIpVGPGY-----QVPFAERIRQEAGIPVIAVGliTD-PEQAEAI 308
|
330
....*....|....*....
gi 2789488066 307 IESGNVDFVSFGRALIADP 325
Cdd:cd02932 309 LESGRADLVALGRELLRNP 327
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
6-366 |
2.81e-71 |
|
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: 234.49 E-value: 2.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMGTNsaLANGRKT-DNEIDYFIERAKGGVGMIIMGCQPLNEKIAQGSMEGYMDSFTVLPS 84
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTG--LEELDDGiDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 85 LTSVCDGVHKYGAKIVCQLTpGTGRNAFPDTLgnppMSASEIPSAFDPnLMCHALTKEEISKMMDDFKFAAGVAMDAGYD 164
Cdd:cd02930 79 HRLITDAVHAEGGKIALQIL-HAGRYAYHPLC----VAPSAIRAPINP-FTPRELSEEEIEQTIEDFARCAALAREAGYD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 165 AIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNSGRDLEYSMKILKE 244
Cdd:cd02930 153 GVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 245 LEKEGIDAFDIDAGCYE----TLDYIFPPAylgesCMSYVCEDARKVVNVPLINAGTHN-PESALELIESGNVDFVSFGR 319
Cdd:cd02930 233 LEAAGADILNTGIGWHEarvpTIATSVPRG-----AFAWATAKLKRAVDIPVIASNRINtPEVAERLLADGDADMVSMAR 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2789488066 320 ALIADPMMPKKLMKNHREDVRPCLRCNEYCIGRIWNHHTkLGCAVNP 366
Cdd:cd02930 308 PFLADPDFVAKAAAGRADEINTCIACNQACLDHIFTGQR-ASCLVNP 353
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
5-338 |
4.96e-69 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 228.10 E-value: 4.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 5 KLFTPFKIGKMEVKNRLVMSPMGTNSALANGRK-TDNEIDYFIERAKGGVGMIIMGCQPLNEKiaQGSMEG----YMDSF 79
Cdd:pfam00724 1 KLFEPIKIGNTTLKNRIVMAPMTRLRSLDDGTKaTGLLAEYYSQRSRGPGTLIITEGAFVNPQ--SGGFDNgpriWDDEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 80 tvLPSLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTLGNPPMSASEIPSAFDPNLM-----CHALTKEEISKMMDDFKFA 154
Cdd:pfam00724 79 --IEGWRKLTEAVHKNGSKAGVQLWHL-GREAPMEYRPDLEVDGPSDPFALGAQEFeiaspRYEMSKEEIKQHIQDFVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 155 AGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNSGRD 234
Cdd:pfam00724 156 AKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 235 L-EYSMKIlKELEKEGIDAFDIDAGCYetLDYIFPPAYLGESCMSYVCEDA---RKVVNVPLINAGTHNPESALELIES- 309
Cdd:pfam00724 236 FaETAQFI-YLLAELGVRLPDGWHLAY--IHAIEPRPRGAGPVRTRQQHNTlfvKGVWKGPLITVGRIDDPSVAAEIVSk 312
|
330 340
....*....|....*....|....*....
gi 2789488066 310 GNVDFVSFGRALIADPMMPKKLmKNHRED 338
Cdd:pfam00724 313 GRADLVAMGRPFLADPDLPFKA-KKGRPL 340
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
6-338 |
2.00e-66 |
|
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: 221.70 E-value: 2.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIG-KMEVKNRLVMSPMGTNSALANGRKTDNEIDYFIERAKGgVGMIIMGC---QPlNEKIAQGSMEGYMDSFtv 81
Cdd:cd04735 1 LFEPFTLKnGVTLKNRFVMAPMTTYSSNPDGTITDDELAYYQRRAGG-VGMVITGAtyvSP-SGIGFEGGFSADDDSD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 82 LPSLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTL-GNPPMSASEIpSAFDPNLMC-HALTKEEISKMMDDFKFAAGVAM 159
Cdd:cd04735 77 IPGLRKLAQAIKSKGAKAILQIFHA-GRMANPALVpGGDVVSPSAI-AAFRPGAHTpRELTHEEIEDIIDAFGEATRRAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 160 DAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVP---IL-FRISLDHRFNSGRDL 235
Cdd:cd04735 155 EAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHADkdfILgYRFSPEEPEEPGIRM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 236 EYSMKILKELEKEGIDAFDIDAGCYetldYIFPP--AYLGESCMSYVCEdarKVVN-VPLINAGT-HNPESALELIESGn 311
Cdd:cd04735 235 EDTLALVDKLADKGLDYLHISLWDF----DRKSRrgRDDNQTIMELVKE---RIAGrLPLIAVGSiNTPDDALEALETG- 306
|
330 340
....*....|....*....|....*..
gi 2789488066 312 VDFVSFGRALIADPMMPKKLMKNhRED 338
Cdd:cd04735 307 ADLVAIGRGLLVDPDWVEKIKEG-RED 332
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
5-334 |
1.10e-63 |
|
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: 213.87 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 5 KLFTPFKIGKMEVKNRLVMSPMGTNSALANGRKTDNEIDYFIERAkgGVGMIIM-GCQPlnekIAQGSmeGYMDSftvlP 83
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLTRSRADPDGVPTDLMAEYYAQRA--SAGLIITeATQI----SPQGQ--GYPNT----P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 84 SLTS---------VCDGVHKYGAKIVCQLTPgTGRNAFPDTL--GNPPMSASEIP---SAFDPNLMC-----HALTKEEI 144
Cdd:cd02933 69 GIYTdeqvegwkkVTDAVHAKGGKIFLQLWH-VGRVSHPSLLpgGAPPVAPSAIAaegKVFTPAGKVpyptpRALTTEEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 145 SKMMDDFKFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKD-VPIlfRI 223
Cdd:cd02933 148 PGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADrVGI--RL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 224 SLDHRFNSGRDLE----YSMkILKELEKEGIdAFdidagcyetLDYIFP-PAYLGESCMSYVCEDARKVVNVPLINAGTH 298
Cdd:cd02933 226 SPFGTFNDMGDSDpeatFSY-LAKELNKRGL-AY---------LHLVEPrVAGNPEDQPPDFLDFLRKAFKGPLIAAGGY 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 2789488066 299 NPESALELIESGNVDFVSFGRALIADPMMPKKLMKN 334
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 ... |
6-341 |
4.17e-56 |
|
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: 194.46 E-value: 4.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMgTNSALANGRKTDNEIDYFIERAKGGVGMIIMGCQPLNEKIAQGSMEG-YMDSFTVLPS 84
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPM-TRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVpRFHGEDALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 85 LTSVCDGVHKYGAKIVCQL-----TPGTGRNAFPDTlgnPPMSASEIPSAFDPNLmcHALTKEEISKMMDDFKFAAGVAM 159
Cdd:cd04747 80 WKKVVDEVHAAGGKIAPQLwhvgaMRKLGTPPFPDV---PPLSPSGLVGPGKPVG--REMTEADIDDVIAAFARAAADAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 160 DAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRIS----LDHR---FNSG 232
Cdd:cd04747 155 RLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSqwkqQDYTarlADTP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 233 RDLEysmKILKELEKEGIDAFDIdagcyeTLDYIFPPAYLGeSCMSYVCEdARKVVNVPLINAG-----------THNPE 301
Cdd:cd04747 235 DELE---ALLAPLVDAGVDIFHC------STRRFWEPEFEG-SELNLAGW-TKKLTGLPTITVGsvgldgdfigaFAGDE 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2789488066 302 SA--------LELIESGNVDFVSFGRALIADPMMPKKLMKNHREDVRP 341
Cdd:cd04747 304 GAspasldrlLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDELIP 351
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
5-329 |
3.80e-55 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 191.07 E-value: 3.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 5 KLFTPFKIGKMEVKNRLVMSPMGTNSA-LANGRKTDNEIDYFIERAKGGVGMIIM---GCQPlNEKIAQGSMEGYMDSFt 80
Cdd:PRK13523 2 KLFSPYTIKDVTLKNRIVMSPMCMYSSeNKDGKVTNFHLIHYGTRAAGQVGLVIVeatAVLP-EGRISDKDLGIWDDEH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 81 vLPSLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTlgnPPMSASEIPsaFDPNLMC-HALTKEEISKMMDDFKFAAGVAM 159
Cdd:PRK13523 80 -IEGLHKLVTFIHDHGAKAAIQLAHA-GRKAELEG---DIVAPSAIP--FDEKSKTpVEMTKEQIKETVLAFKQAAVRAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 160 DAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVgkDVPILFRISLDHRFNSGRDLEYSM 239
Cdd:PRK13523 153 EAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPGGLTVQDYV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 240 KILKELEKEGIDAFDIDAGCYETLDyifPPAYLGEScMSYVcEDARKVVNVP-----LINAGTHnpesALELIESGNVDF 314
Cdd:PRK13523 231 QYAKWMKEQGVDLIDVSSGAVVPAR---IDVYPGYQ-VPFA-EHIREHANIAtgavgLITSGAQ----AEEILQNNRADL 301
|
330
....*....|....*
gi 2789488066 315 VSFGRALIADPMMPK 329
Cdd:PRK13523 302 IFIGRELLRNPYFPR 316
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
6-334 |
9.11e-53 |
|
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: 184.71 E-value: 9.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTP--FKIGKmEVKNRLVMSPMGTNSALANGRKTDNEIDYFIERAKGGVGMIIMG---CQP--LNEKIAQGSMEGymDS 78
Cdd:cd04733 1 LGQPltLPNGA-TLPNRLAKAAMSERLADGRGLPTPELIRLYRRWAEGGIGLIITGnvmVDPrhLEEPGIIGNVVL--ES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 79 FTVLPSLTSVCDGVHKYGAKIVCQLT-PGtgRNAfPDTLGNPPMSASEI--PSAFDPNL-MCHALTKEEISKMMDDFKFA 154
Cdd:cd04733 78 GEDLEAFREWAAAAKANGALIWAQLNhPG--RQS-PAGLNQNPVAPSVAldPGGLGKLFgKPRAMTEEEIEDVIDRFAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 155 AGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRI-SLDHRfNSGR 233
Cdd:cd04733 155 ARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLnSADFQ-RGGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 234 DLEYSMKILKELEKEGIDAFDIDAGCYEtldyifPPAYLGESCMS------Y---VCEDARKVVNVPL-INAGTHNPESA 303
Cdd:cd04733 234 TEEDALEVVEALEEAGVDLVELSGGTYE------SPAMAGAKKEStiareaYfleFAEKIRKVTKTPLmVTGGFRTRAAM 307
|
330 340 350
....*....|....*....|....*....|.
gi 2789488066 304 LELIESGNVDFVSFGRALIADPMMPKKLMKN 334
Cdd:cd04733 308 EQALASGAVDGIGLARPLALEPDLPNKLLAG 338
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
3-371 |
1.18e-47 |
|
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: 171.77 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 3 YEKLFTPFKIGKMEVKNRLVMSP----MGTN--SALANGRKTdneidyfieRAKGGVGMIIMG-CQplnekIAQGSMEGY 75
Cdd:cd02929 5 HDILFEPIKIGPVTARNRFYQVPhcngMGYRkpSAQAAMRGI---------KAEGGWGVVNTEqCS-----IHPSSDDTP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 76 MDSFTV-----LPSLTSVCDGVHKYGAKIVCQLTPGtGRNAFPDTLGNPPMSASEIPSAFDPN--LMCHALTKEEISKMM 148
Cdd:cd02929 71 RISARLwddgdIRNLAAMTDAVHKHGALAGIELWHG-GAHAPNRESRETPLGPSQLPSEFPTGgpVQAREMDKDDIKRVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 149 DDFKFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHR 228
Cdd:cd02929 150 RWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 229 FNSGRD--LEYSMKILkELEKEGIDAFDIDAGCYE--TLDYIFPPAYLGESCMSYVcedaRKVVNVPLINAGTH-NPESA 303
Cdd:cd02929 230 IGPGGIesEGEGVEFV-EMLDELPDLWDVNVGDWAndGEDSRFYPEGHQEPYIKFV----KQVTSKPVVGVGRFtSPDKM 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2789488066 304 LELIESGNVDFVSFGRALIADPMMPKKLMKNHREDVRPCLRCNeYCIGRiWNHHTKLGCAVNPQAMEE 371
Cdd:cd02929 305 VEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISG-DEGGVPMRCTQNPTAGEE 370
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
4-334 |
9.40e-41 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 152.19 E-value: 9.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 4 EKLFTPFKIGKMEVKNRLVMSPMGTNSALANGR-KTDNEIDYFIERAkgGVGMIIMGCQPLNekiAQGsmEGYMDSftvl 82
Cdd:PRK10605 1 EKLFSPLKVGAITAPNRVFMAPLTRLRSIEPGDiPTPLMAEYYRQRA--SAGLIISEATQIS---AQA--KGYAGA---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 83 PSLTS---------VCDGVHKYGAKIVCQLTpGTGRNAF----PDtlGNPPMSASEIPSAFDPNL-------------MC 136
Cdd:PRK10605 70 PGLHSpeqiaawkkITAGVHAEGGHIAVQLW-HTGRISHaslqPG--GQAPVAPSAINAGTRTSLrdengqairvetsTP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 137 HALTKEEISKMMDDFKFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKD 216
Cdd:PRK10605 147 RALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGAD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 217 vPILFRISLDHRFN---SGRD-LEYSMKILKELEKEGIDAFdidagcyetldYIFPPAYLGESCMSYVCEDA-RKVVNVP 291
Cdd:PRK10605 227 -RIGIRISPLGTFNnvdNGPNeEADALYLIEQLGKRGIAYL-----------HMSEPDWAGGEPYSDAFREKvRARFHGV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2789488066 292 LINAGTHNPESALELIESGNVDFVSFGRALIADPMMPKKLMKN 334
Cdd:PRK10605 295 IIGAGAYTAEKAETLIGKGLIDAVAFGRDYIANPDLVARLQRK 337
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
6-258 |
2.95e-35 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 142.39 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 6 LFTPFKIGKMEVKNRLVMSPMGTNSAlANGRKTDNEIDYFIERAKGGVGMII--MGCQPLNEKIAQGSMEGYMDSFTVlp 83
Cdd:PRK08255 399 MFTPFRLRGLTLKNRVVVSPMAMYSA-VDGVPGDFHLVHLGARALGGAGLVMteMTCVSPEGRITPGCPGLYNDEQEA-- 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 84 SLTSVCDGVHKYG-AKIVCQL----TPGTGRNAF-----PDTLGN-PPMSASEIPsaFDP-NLMCHALTKEEISKMMDDF 151
Cdd:PRK08255 476 AWKRIVDFVHANSdAKIGIQLghsgRKGSTRLGWegidePLEEGNwPLISASPLP--YLPgSQVPREMTRADMDRVRDDF 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 152 KFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIREVVGKDVPILFRISLDHRFNS 231
Cdd:PRK08255 554 VAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEG 633
|
250 260
....*....|....*....|....*..
gi 2789488066 232 GRDLEYSMKILKELEKEGIDAFDIDAG 258
Cdd:PRK08255 634 GNTPDDAVEIARAFKAAGADLIDVSSG 660
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
1-334 |
4.94e-32 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 128.43 E-value: 4.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 1 MSYEKLFTPFKIGKMEVKNRLVMSPMGTNSALaNGRKTDNEIDYFIERAKGGvGMIIMgcqplnekiaqgsmEGYMDS-- 78
Cdd:PLN02411 7 NSNETLFSPYKMGRFDLSHRVVLAPMTRCRAL-NGIPNAALAEYYAQRSTPG-GFLIS--------------EGTLISpt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 79 ---FTVLPSLTS---------VCDGVHKYGAKIVCQLTpGTGRNAF----PDtlGNPPMSASEIPSAFDPNLMC------ 136
Cdd:PLN02411 71 apgFPHVPGIYSdeqveawkkVVDAVHAKGSIIFCQLW-HVGRASHqvyqPG--GAAPISSTNKPISERWRILMpdgsyg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 137 -----HALTKEEISKMMDDFKFAAGVAMDAGYDAIEIHAHAGYLIDQFLSPVWNKRTDEYGGSPENNTRFAKDIYHAIRE 211
Cdd:PLN02411 148 kypkpRALETSEIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 212 VVGKDvPILFRIS--LDHRFNSGRD-LEYSMKILkelekEGIDAFDIDAGCYETLDYIFPPAYLG-----------ESCM 277
Cdd:PLN02411 228 AIGAD-RVGVRVSpaIDHLDATDSDpLNLGLAVV-----ERLNKLQLQNGSKLAYLHVTQPRYTAygqtesgrhgsEEEE 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2789488066 278 SYVCEDARKVVNVPLINAGTHNPESALELIESGNVDFVSFGRALIADPMMPKKLMKN 334
Cdd:PLN02411 302 AQLMRTLRRAYQGTFMCSGGFTRELGMQAVQQGDADLVSYGRLFISNPDLVLRFKLN 358
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-625 |
1.39e-30 |
|
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: 122.04 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEDH-----------LGGTMGDI----CTAKFKTNIKQLTKWYQVQLEKLP 448
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyggcvlskaLLGAAEAPeiasLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 449 ------ID-----IHLNTTITGDEEILkTCDYIIVSTGALPSTPAIPGID---GDNVVNIVEAHRNESLIKGNKIVVCGG 514
Cdd:pfam07992 82 gtevvsIDpgakkVVLEELVDGDGETI-TYDRLVIATGARPRLPPIPGVElnvGFLVRTLDSAEALRLKLLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 515 GASGLDGAIeMAEEMHKDVTVVEMLPEMGKdvFFINKISLF--NKLAQNHVQLMTNTKV--VVIDETGLTVEESGVEKhL 590
Cdd:pfam07992 161 GYIGVELAA-ALAKLGKEVTLIEALDRLLR--AFDEEISAAleKALEKNGVEVRLGTSVkeIIGDGDGVEVILKDGTE-I 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2789488066 591 EADTIISAFGMRPNTKLADQLKEKYP----------MKTRV-----IGDC 625
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDerggivvdeyLRTSVpgiyaAGDC 286
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
385-606 |
1.26e-25 |
|
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: 110.56 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKeDHLGGT--------------------------------------MGDICT 426
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTclnvgcipskallhaaevahearhaaefgisagapsvdWAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 427 AKFKTnIKQLTKWYQVQLEKLPIDIHL--------NT-TITGDEEIlkTCDYIIVSTGALPSTPAIPGIDGDNVVNIVEA 497
Cdd:COG1249 85 RKDKV-VDRLRGGVEELLKKNGVDVIRgrarfvdpHTvEVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 498 HRNESLIKgnKIVVCGGGASGLdgaiEMAEEMHK---DVTVVEM----LPEMGKDvffinkIS--LFNKLAQNHVQLMTN 568
Cdd:COG1249 162 LELEELPK--SLVVIGGGYIGL----EFAQIFARlgsEVTLVERgdrlLPGEDPE------ISeaLEKALEKEGIDILTG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2789488066 569 TKVVVIDETG----LTVEESGVEKHLEADTIISAFGMRPNTK 606
Cdd:COG1249 230 AKVTSVEKTGdgvtVTLEDGGGEEAVEADKVLVATGRRPNTD 271
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
404-625 |
3.66e-23 |
|
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: 100.66 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 404 EGHHVTLFEKEDHLGGtmgDICT-----AKFKTNIKQLTKWYQVQLEKLPIDIHLNT------------TITGDEEIlkT 466
Cdd:COG0446 4 PDAEITVIEKGPHHSY---QPCGlpyyvGGGIKDPEDLLVRTPESFERKGIDVRTGTevtaidpeaktvTLRDGETL--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 467 CDYIIVSTGALPSTPAIPGIDGDNVV---NIVEAHRNESLI---KGNKIVVCGGGASGLdgaiEMAEEMHK---DVTVVE 537
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFtlrTLDDADALREALkefKGKRAVVIGGGPIGL----ELAEALRKrglKVTLVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 538 M----LPEMGKDVffinKISLFNKLAQNHVQLMTNTKVV-VIDETGLTVE-ESGVEkhLEADTIISAFGMRPNTKLADQL 611
Cdd:COG0446 155 RaprlLGVLDPEM----AALLEEELREHGVELRLGETVVaIDGDDKVAVTlTDGEE--IPADLVVVAPGVRPNTELAKDA 228
|
250 260 270
....*....|....*....|....*....|.
gi 2789488066 612 K------------EKypMKTRV-----IGDC 625
Cdd:COG0446 229 GlalgergwikvdET--LQTSDpdvyaAGDC 257
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
382-610 |
9.66e-23 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 100.99 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 382 PQNVVVIGAGPGGMEAAR--VAALEGHHVTLFEKEDH-----------LGGTMGDictakfktniKQLT----KWYqvql 444
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEelRKLDPDGEITVIGAEPHppynrpplskvLAGETDE----------EDLLlrpaDFY---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 445 EKLPIDIHLNTTITG-----------DEEILkTCDYIIVSTGALPSTPAIPGIDGDNVVNI-----VEAHRnESLIKGNK 508
Cdd:COG1251 67 EENGIDLRLGTRVTAidraartvtlaDGETL-PYDKLVLATGSRPRVPPIPGADLPGVFTLrtlddADALR-AALAPGKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 509 IVVCGGGASGLDGAiEMAEEMHKDVTVVEMLP---------EMGKdvfFINKislfnKLAQNHVQLMTNTKVVVI--DET 577
Cdd:COG1251 145 VVVIGGGLIGLEAA-AALRKRGLEVTVVERAPrllprqldeEAGA---LLQR-----LLEALGVEVRLGTGVTEIegDDR 215
|
250 260 270
....*....|....*....|....*....|....
gi 2789488066 578 GLTVE-ESGveKHLEADTIISAFGMRPNTKLADQ 610
Cdd:COG1251 216 VTGVRlADG--EELPADLVVVAIGVRPNTELARA 247
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
385-644 |
1.14e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 99.04 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKeDHLGGtmgdictakfktnikQLTKWYQV---------------------Q 443
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGG---------------QLATTKEIenypgfpegisgpelaerlreQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 444 LEKLPIDIHLN--TTITGDEEILK---------TCDYIIVSTGALPSTPAIPGID---GDNVVNIVEAHRNesLIKGNKI 509
Cdd:COG0492 67 AERFGAEILLEevTSVDKDDGPFRvttddgteyEAKAVIIATGAGPRKLGLPGEEefeGRGVSYCATCDGF--FFRGKDV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 510 VVCGGGASGLDGAIEMAEEmHKDVTVVEMlpemgKDVFFINKISLfNKLAQN-HVQLMTNTKVVVI--DE--TGLTVE-- 582
Cdd:COG0492 145 VVVGGGDSALEEALYLTKF-ASKVTLIHR-----RDELRASKILV-ERLRANpKIEVLWNTEVTEIegDGrvEGVTLKnv 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2789488066 583 ESGVEKHLEADTIISAFGMRPNTKLADQ----LKEKYP------MKTRV-----IGDC--YKLGKIGEAVREGFFAASS 644
Cdd:COG0492 218 KTGEEKELEVDGVFVAIGLKPNTELLKGlgleLDEDGYivvdedMETSVpgvfaAGDVrdYKYRQAATAAGEGAIAALS 296
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
367-607 |
6.42e-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: 99.05 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 367 QAMEEVRFKLEKTEDP--QNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM--GdIctAKFKTNiKQLTKWYQV 442
Cdd:COG0493 104 KAFEEGWVKPPPPAPRtgKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLryG-I--PEFRLP-KDVLDREIE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 443 QLEKLPIDIHLNTTITGD---EEILKTCDYIIVSTGA-LPSTPAIPGIDGDNVVNIVE-------AHRNESLI-KGNKIV 510
Cdd:COG0493 180 LIEALGVEFRTNVEVGKDitlDELLEEFDAVFLATGAgKPRDLGIPGEDLKGVHSAMDfltavnlGEAPDTILaVGKRVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 511 VCGGGASGLD--------GAiemaeemhKDVTVVEMLP--EMGKDVFfinKISlfnkLAQNH---VQLMTNTKVVVIDE- 576
Cdd:COG0493 260 VIGGGNTAMDcartalrlGA--------ESVTIVYRRTreEMPASKE---EVE----EALEEgveFLFLVAPVEIIGDEn 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2789488066 577 ---TGLTVEE-----------------SGVEKHLEADTIISAFGMRPNTKL 607
Cdd:COG0493 325 grvTGLECVRmelgepdesgrrrpvpiEGSEFTLPADLVILAIGQTPDPSG 375
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
385-606 |
4.49e-20 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 93.67 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKeDHLGGT--------------------------------------MGDIct 426
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEK-EKLGGTclnrgcipskallhaaeradearhsedfgikaenvgidFKKV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 427 AKFKTN-IKQLTKWYQVQLEKLPIDI-----------HLNTTITGDEEILkTCDYIIVSTGALPSTpaIPGI--DGDNVV 492
Cdd:PRK06416 84 QEWKNGvVNRLTGGVEGLLKKNKVDIirgeaklvdpnTVRVMTEDGEQTY-TAKNIILATGSRPRE--LPGIeiDGRVIW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 493 NIVEAHRNESLIKgnKIVVCGGGASGldgaIEMAEEMHK---DVTVVEMLPEM--GKDvffiNKISlfnKLAQNH----- 562
Cdd:PRK06416 161 TSDEALNLDEVPK--SLVVIGGGYIG----VEFASAYASlgaEVTIVEALPRIlpGED----KEIS---KLAERAlkkrg 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2789488066 563 VQLMTNTKVVVIDETG----LTVEESGVEKHLEADTIISAFGMRPNTK 606
Cdd:PRK06416 228 IKIKTGAKAKKVEQTDdgvtVTLEDGGKEETLEADYVLVAVGRRPNTE 275
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
368-609 |
7.01e-19 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 89.85 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 368 AMEEVRFKLEKTED-PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM--GdIctAKFKTnIKQLTKWYQVQL 444
Cdd:PRK11749 125 AMETGWVLFKRAPKtGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLryG-I--PEFRL-PKDIVDREVERL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 445 EKLPIDIHLNTTITGD---EEILKTCDYIIVSTGA-LPSTPAIPGIDGDNVVNIVE-------AHRNESLIKGNKIVVCG 513
Cdd:PRK11749 201 LKLGVEIRTNTEVGRDitlDELRAGYDAVFIGTGAgLPRFLGIPGENLGGVYSAVDfltrvnqAVADYDLPVGKRVVVIG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 514 GGASGLDGAIEM----AEEmhkdVTVV------EMlPEMGKDVffinkislfnKLAQNH-VQLMTNTKVVVI--DETGLT 580
Cdd:PRK11749 281 GGNTAMDAARTAkrlgAES----VTIVyrrgreEM-PASEEEV----------EHAKEEgVEFEWLAAPVEIlgDEGRVT 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2789488066 581 -------------------VEESGVEKHLEADTIISAFGMRPNTKLAD 609
Cdd:PRK11749 346 gvefvrmelgepdasgrrrVPIEGSEFTLPADLVIKAIGQTPNPLILS 393
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
382-609 |
1.51e-17 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 84.80 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 382 PQNVVVIGAGPGGMEAARvaALE-----GHHVTLFEKEDH----------LGGTM--GDICtakfkTNIKQLTKWYQVQL 444
Cdd:COG1252 1 MKRIVIVGGGFAGLEAAR--RLRkklggDAEVTLIDPNPYhlfqpllpevAAGTLspDDIA-----IPLRELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 445 -----EKlpIDIHLNTTITGDEEILkTCDYIIVSTGALPSTPAIPGIdGDNVV-----------------NIVEAHRNES 502
Cdd:COG1252 74 iqgevTG--IDPEARTVTLADGRTL-SYDYLVIATGSVTNFFGIPGL-AEHALplktledalalrerllaAFERAERRRL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 503 LikgnKIVVCGGGASGLDGAIEMAEEMHK------------DVTVVEM----LPEMGKDVffinKISLFNKLAQNHVQLM 566
Cdd:COG1252 150 L----TIVVVGGGPTGVELAGELAELLRKllrypgidpdkvRITLVEAgpriLPGLGEKL----SEAAEKELEKRGVEVH 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2789488066 567 TNTKVVVIDETGLTVEEsgvEKHLEADTIISAFGMRPNTKLAD 609
Cdd:COG1252 222 TGTRVTEVDADGVTLED---GEEIPADTVIWAAGVKAPPLLAD 261
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
384-606 |
2.39e-17 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 85.00 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEdHLGGT---------------------------MGdICTAKFKTNIKQL 436
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKE-YLGGTclnvgciptkallhsaevydeikhakdLG-IEVENVSVDWEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 437 TKWYQVQLEKLPIDIHL----N--TTITGDEEILK---------------TCDYIIVSTGALPSTPAIP-GIDGDNVVNI 494
Cdd:TIGR01350 81 QKRKNKVVKKLVGGVSGllkkNkvTVIKGEAKFLDpgtvsvtgengeetlEAKNIIIATGSRPRSLPGPfDFDGKVVITS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 495 VEAHRNESLIKgnKIVVCGGGASGldgaIEMAEEMHK---DVTVVEMLPE----MGKDVffiNKIsLFNKLAQNHVQLMT 567
Cdd:TIGR01350 161 TGALNLEEVPE--SLVIIGGGVIG----IEFASIFASlgsKVTVIEMLDRilpgEDAEV---SKV-LQKALKKKGVKILT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2789488066 568 NTKVVVI--DETGLTVEESGVE-KHLEADTIISAFGMRPNTK 606
Cdd:TIGR01350 231 NTKVTAVekNDDQVTYENKGGEtETLTGEKVLVAVGRKPNTE 272
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
385-642 |
3.44e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 81.38 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKeDHLGGT---------------------------MGdICTAKFKTNIKQLT 437
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGGTclnvgcipskaliaaaeafheakhaeeFG-IHADGPKIDFKKVM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 438 KW------------YQVQLEKLPID--------IHLNTTITGDEEIlkTCDYIIVSTGAlpSTPAIPG---IDGDNVVNI 494
Cdd:PRK06292 84 ARvrrerdrfvggvVEGLEKKPKIDkikgtarfVDPNTVEVNGERI--EAKNIVIATGS--RVPPIPGvwlILGDRLLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 495 VEAHRNESLIKgnKIVVCGGGASGLdgaiEMAEEMHK---DVTVVEM----LPEMGKDVffinkISLFNKLAQNHVQLMT 567
Cdd:PRK06292 160 DDAFELDKLPK--SLAVIGGGVIGL----ELGQALSRlgvKVTVFERgdriLPLEDPEV-----SKQAQKILSKEFKIKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 568 NTKVVVIDETG---LTVEESGVEKH-LEADTIISAFGMRPNT------KLADQLKEK-YP-----MKTRV-----IGDCY 626
Cdd:PRK06292 229 GAKVTSVEKSGdekVEELEKGGKTEtIEADYVLVATGRRPNTdglgleNTGIELDERgRPvvdehTQTSVpgiyaAGDVN 308
|
330
....*....|....*....
gi 2789488066 627 klGKI---GEAVREGFFAA 642
Cdd:PRK06292 309 --GKPpllHEAADEGRIAA 325
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
385-646 |
1.20e-14 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 76.74 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG--TMGdIctAKFKtnikqLTKWyQV-----QLEKLPIDIHLNTTI 457
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllRYG-I--PDFK-----LEKE-VIdrrieLMEAEGIEFRTNVEV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 458 TGD---EEILKTCDYIIVSTGA-----LPstpaIPGIDGDNV----------VNIVEAHRNESLI--KGNKIVVCGGGAS 517
Cdd:PRK12810 217 GKDitaEELLAEYDAVFLGTGAykprdLG----IPGRDLDGVhfamdfliqnTRRVLGDETEPFIsaKGKHVVVIGGGDT 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 518 GLD--------GAiemaeemhKDVTVVEMLPEMGKDVFFINKISLFNKL-----AQNH-VQLM--TNTKVVVIDE---TG 578
Cdd:PRK12810 293 GMDcvgtairqGA--------KSVTQRDIMPMPPSRRNKNNPWPYWPMKlevsnAHEEgVEREfnVQTKEFEGENgkvTG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 579 LTV-----------EESGVEKHLEADTIISAFGMR-PNTKLADQLK-----------EKYPMKTRVI-----GDCYKlgk 630
Cdd:PRK12810 365 VKVvrtelgegdfePVEGSEFVLPADLVLLAMGFTgPEAGLLAQFGveldergrvaaPDNAYQTSNPkvfaaGDMRR--- 441
|
330 340
....*....|....*....|.
gi 2789488066 631 iGE-----AVREGFFAASSLD 646
Cdd:PRK12810 442 -GQslvvwAIAEGRQAARAID 461
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
369-646 |
1.25e-14 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 75.80 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 369 MEEVRFKL---EKTED-PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMgdictaKF--------KTNIKQL 436
Cdd:PRK12770 1 MDGMKFAFmckEKPPPtGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM------LFgipefripIERVREG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 437 TKwyqvQLEKLPIDIHLNTTITGD------------------EEILKTCDYIIVSTGALPS-TPAIPGIDGDNVVNIVE- 496
Cdd:PRK12770 75 VK----ELEEAGVVFHTRTKVCCGeplheeegdefverivslEELVKKYDAVLIATGTWKSrKLGIPGEDLPGVYSALEy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 497 -----AHR-----NESL--IKGNKIVVCGGGASGLDGAIEMAEEMHKDVTVV---------------EMLPEMGkdVFFI 549
Cdd:PRK12770 151 lfrirAAKlgylpWEKVppVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAyrrtineapagkyeiERLIARG--VEFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 550 NKISLFNKLAQNHVQL--MTNTKVVVIDETGL--TVEESGVEKHLEADTIISAFGMRPNTKLADQL-------------K 612
Cdd:PRK12770 229 ELVTPVRIIGEGRVEGveLAKMRLGEPDESGRprPVPIPGSEFVLEADTVVFAIGEIPTPPFAKEClgielnrkgeivvD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2789488066 613 EKYpMKTR----VIGDCYkLG--KIGEAVREGFFAASSLD 646
Cdd:PRK12770 309 EKH-MTSRegvfAAGDVV-TGpsKIGKAIKSGLRAAQSIH 346
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
375-480 |
5.92e-13 |
|
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: 70.04 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 375 KLEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGdictakfktniKQLTKWYQVQLEKLPIDIHLN 454
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFD-----------EEISAALEKALEKNGVEVRLG 213
|
90 100 110
....*....|....*....|....*....|....*...
gi 2789488066 455 TT---ITGDEEILKT---------CDYIIVSTGALPST 480
Cdd:pfam07992 214 TSvkeIIGDGDGVEVilkdgteidADLVVVAIGRRPNT 251
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
385-646 |
5.39e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 65.56 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMgDICTAKFKTNIKQLTKWYQVqLEKLPIDIHLNTTITGD---E 461
Cdd:PRK13984 286 VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVM-RYGIPSYRLPDEALDKDIAF-IEALGVKIHLNTRVGKDiplE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 462 EILKTCDYIIVSTG-ALPSTPAIPGIDGDNVVN---IVEAHRNESLIKG------NKIVVCGGGASGLDGAIEMA----- 526
Cdd:PRK13984 364 ELREKHDAVFLSTGfTLGRSTRIPGTDHPDVIQalpLLREIRDYLRGEGpkpkipRSLVVIGGGNVAMDIARSMArlqkm 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 527 EEMHKDVTVVEM---LPEMGKDVFFINK-----ISLFNKLAQNHVqLMTNTKVV---------VIDETGL---TVEESGv 586
Cdd:PRK13984 444 EYGEVNVKVTSLertFEEMPADMEEIEEgleegVVIYPGWGPMEV-VIENDKVKgvkfkkcveVFDEEGRfnpKFDESD- 521
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2789488066 587 EKHLEADTIISAFGMRPNTK-LADQLKEKYPM-KTRVI---------------GDCYKLGKIGEAVREGFFAASSLD 646
Cdd:PRK13984 522 QIIVEADMVVEAIGQAPDYSyLPEELKSKLEFvRGRILtneygqtsipwlfagGDIVHGPDIIHGVADGYWAAEGID 598
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
385-600 |
7.16e-11 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 65.28 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM--GdICTAKFKTNIKQltkwYQVQ-LEKLPIDIHLNTTITGD- 460
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMryG-IPAYRLPREVLD----AEIQrILDLGVEVRLGVRVGEDi 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 461 --EEILKTCDYIIVSTGA-LPSTPAIPGIDGDNVVNIVEAHRN----ESLIKGNKIVVCGGGASGLD--------GAiem 525
Cdd:PRK12771 215 tlEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVLDAVDFLRAvgegEPPFLGKRVVVIGGGNTAMDaartarrlGA--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 526 aeemhKDVTVV------EM--LP-------EMGKDVFFINKISLFNKLAQNHVQLMTNTKVV-VIDETGLTVEESGVEKH 589
Cdd:PRK12771 292 -----EEVTIVyrrtreDMpaHDeeieealREGVEINWLRTPVEIEGDENGATGLRVITVEKmELDEDGRPSPVTGEEET 366
|
250
....*....|.
gi 2789488066 590 LEADTIISAFG 600
Cdd:PRK12771 367 LEADLVVLAIG 377
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
365-480 |
7.32e-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: 63.68 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 365 NPQAMEEVRFKLeKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGdictakfktniKQLTKWYQVQL 444
Cdd:COG0446 108 TLDDADALREAL-KEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLD-----------PEMAALLEEEL 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2789488066 445 EKLPIDIHLNTTI-------------TGDEEIlkTCDYIIVSTGALPST 480
Cdd:COG0446 176 REHGVELRLGETVvaidgddkvavtlTDGEEI--PADLVVVAPGVRPNT 222
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
375-604 |
1.07e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 64.27 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 375 KLEKTEDPQN--VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM--GdicTAKFKTNIKQLTKWYQVQLEKLPID 450
Cdd:PRK12831 131 DLSETEEKKGkkVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLvyG---IPEFRLPKETVVKKEIENIKKLGVK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 451 IHLNT----TITGDeEILKTCDY--IIVSTGA-LPSTPAIPGIDGDNV---------VNIVEAHRNES---LIKGNKIVV 511
Cdd:PRK12831 208 IETNVvvgkTVTID-ELLEEEGFdaVFIGSGAgLPKFMGIPGENLNGVfsanefltrVNLMKAYKPEYdtpIKVGKKVAV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 512 CGGGASGLDGAiEMAEEMHKDVTVV-----EMLPEMGKDVFFINKISLfnklaqnHVQLMTNTKVVVIDETGLT------ 580
Cdd:PRK12831 287 VGGGNVAMDAA-RTALRLGAEVHIVyrrseEELPARVEEVHHAKEEGV-------IFDLLTNPVEILGDENGWVkgmkci 358
|
250 260 270
....*....|....*....|....*....|....*....
gi 2789488066 581 ---------------VEESGVEKHLEADTIISAFGMRPN 604
Cdd:PRK12831 359 kmelgepdasgrrrpVEIEGSEFVLEVDTVIMSLGTSPN 397
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
383-510 |
1.38e-10 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 64.11 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGDICTaKFKTN------IKQLTKwyQVQLEKLpIDIHLNTT 456
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK-TFPGLdcpqciLEPLIA--EVEANPN-ITVYTGAE 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2789488066 457 IT----------------GDEEILKTCDYIIVSTGALPSTPAIPGIDG----DNVVNIVEAhrnESLIKGNKIV 510
Cdd:COG1148 217 VEevsgyvgnftvtikkgPREEIEIEVGAIVLATGFKPYDPTKLGEYGygkyPNVITNLEL---ERLLAAGKIL 287
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
385-536 |
4.05e-10 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 62.19 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT-------------MGDICTAKFKTNIKQLTKW--------YQVQ 443
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypglrldtPSHLYSLPFFPNWSDDPDFptgdeilaYLEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 444 LEK---LPIDIHLNTTITG---DEE----ILKT-------CDYIIVSTGAL--PSTPAIPGIDGDNVVNIveaH----RN 500
Cdd:COG2072 89 YADkfgLRRPIRFGTEVTSarwDEAdgrwTVTTddgetltARFVVVATGPLsrPKIPDIPGLEDFAGEQL---HsadwRN 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2789488066 501 ESLIKGNKIVVCGGGASGLDGAIEMAEEmHKDVTVV 536
Cdd:COG2072 166 PVDLAGKRVLVVGTGASAVQIAPELARV-AAHVTVF 200
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
385-646 |
1.14e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 61.28 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM--GdicTAKFKTNIKQLTKwyQVQ-LEKLPIDIHLNTTITGD- 460
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMryG---IPRFRLPESVIDA--DIApLRAMGAEFRFNTVFGRDi 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 461 --EEILKTCDYIIVSTGA-LPSTPAIPGIDGDNVVNIVEAHRNESLIK----GNKIVVCGGGASGLDGAiemAEEMHKDV 533
Cdd:PRK12814 271 tlEELQKEFDAVLLAVGAqKASKMGIPGEELPGVISGIDFLRNVALGTalhpGKKVVVIGGGNTAIDAA---RTALRLGA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 534 TVVEMLPEMGKDVFFINKISLFNKLAQNhVQLMTNTKVVVI--DETGLTV----------EESGVEK---------HLEA 592
Cdd:PRK12814 348 ESVTILYRRTREEMPANRAEIEEALAEG-VSLRELAAPVSIerSEGGLELtaikmqqgepDESGRRRpvpvegsefTLQA 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2789488066 593 DTIISAFGMRPNTKLADQ-----------LKEKYPMKTRVI-----GDCYKLGKIG-EAVREGFFAASSLD 646
Cdd:PRK12814 427 DTVISAIGQQVDPPIAEAagigtsrngtvKVDPETLQTSVAgvfagGDCVTGADIAiNAVEQGKRAAHAID 497
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
384-605 |
8.04e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 58.29 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKeDHLGGT-----------MgdICTAK----------------------FK 430
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIER-GLLGGTcvntgcvptktL--IASARaahlarraaeygvsvggpvsvdFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 431 TnIKQ------------LTKWYQvqlEKLPIDIHLNT-------TITGDEEILkTCDYIIVSTGALPSTPAIPGIDgdnv 491
Cdd:PRK06370 84 A-VMArkrrirarsrhgSEQWLR---GLEGVDVFRGHarfespnTVRVGGETL-RAKRIFINTGARAAIPPIPGLD---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 492 vnIVEAHRNESLIKGNKI----VVCGGGASGLdgaiEMAEEMHK---DVTVVEM----LPEMGKDVffiNKIsLFNKLAQ 560
Cdd:PRK06370 155 --EVGYLTNETIFSLDELpehlVIIGGGYIGL----EFAQMFRRfgsEVTVIERgprlLPREDEDV---AAA-VREILER 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2789488066 561 NHVQLMTNTKVVVIDETG----LTVEESGVEKHLEADTIISAFGMRPNT 605
Cdd:PRK06370 225 EGIDVRLNAECIRVERDGdgiaVGLDCNGGAPEITGSHILVAVGRVPNT 273
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
376-480 |
1.56e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 57.07 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 376 LEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDH-----LGGTMGDICTAKfktnikqltkwyqvqLEKLPID 450
Cdd:COG1251 136 RAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRllprqLDEEAGALLQRL---------------LEALGVE 200
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2789488066 451 IHLNTT---ITGDEEILK---------TCDYIIVSTGALPST 480
Cdd:COG1251 201 VRLGTGvteIEGDDRVTGvrladgeelPADLVVVAIGVRPNT 242
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
449-610 |
1.76e-08 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 56.85 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 449 IDIHLNTTITGDEEIlktcDY--IIVSTGAlpsTPAIPGIDGDNVV---NIVEAHR--NESLIKGNKIVVCGGGASGLDG 521
Cdd:PRK04965 84 IDAEAQVVKSQGNQW----QYdkLVLATGA---SAFVPPIPGRELMltlNSQQEYRaaETQLRDAQRVLVVGGGLIGTEL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 522 AIEMAEEmHKDVTVVE--------MLPEmgkdvfFINkISLFNKLAQNHVQLMTNTKVVVIDETGLTVE---ESGveKHL 590
Cdd:PRK04965 157 AMDLCRA-GKAVTLVDnaasllasLMPP------EVS-SRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRatlDSG--RSI 226
|
170 180
....*....|....*....|
gi 2789488066 591 EADTIISAFGMRPNTKLADQ 610
Cdd:PRK04965 227 EVDAVIAAAGLRPNTALARR 246
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
387-421 |
3.58e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 50.61 E-value: 3.58e-08
10 20 30
....*....|....*....|....*....|....*
gi 2789488066 387 VIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM 421
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
385-606 |
5.61e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 55.70 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEK------EDHLGGTmgdiCT-------------AKFKTNIKQLTKWYQVQLE 445
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGT----CLnvgcipskallasSEEFENAGHHFADHGIHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 446 KLPIDI-----HLNTT-------------------------------------ITGDEEILKTCDYIIVSTGalpSTP-A 482
Cdd:PRK06327 83 GVKIDVakmiaRKDKVvkkmtggieglfkknkitvlkgrgsfvgktdagyeikVTGEDETVITAKHVIIATG---SEPrH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 483 IPGI--DGDNVVNIVEAHRNESLIKgnKIVVCGGGASGLdgaiEMAEEMHK---DVTVVEMLPE--MGKDVffinKIS-- 553
Cdd:PRK06327 160 LPGVpfDNKIILDNTGALNFTEVPK--KLAVIGAGVIGL----ELGSVWRRlgaEVTILEALPAflAAADE----QVAke 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2789488066 554 LFNKLAQNHVQLMTNTKV--VVIDETGLTV---EESGVEKHLEADTIISAFGMRPNTK 606
Cdd:PRK06327 230 AAKAFTKQGLDIHLGVKIgeIKTGGKGVSVaytDADGEAQTLEVDKLIVSIGRVPNTD 287
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
385-608 |
6.01e-08 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 55.43 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAA----RVAalEGHHVTLFEKEDHLG-GTMG-DICTAKFKTNIKQLTKWYQVQLEKLPIDIHLNTTIT 458
Cdd:PRK09564 3 IIIIGGTAAGMSAAakakRLN--KELEITVYEKTDIVSfGACGlPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 459 G---------------DEEILKTCDYIIVSTGALPSTPAIPGIDGDNV---------VNIVEAHRNESlIKgnKIVVCGG 514
Cdd:PRK09564 81 KvdaknktitvknlktGSIFNDTYDKLMIATGARPIIPPIKNINLENVytlksmedgLALKELLKDEE-IK--NIVIIGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 515 GASGldgaIEMAEEMH---KDVTVVEMLPEMGKDVF---FINKISlfNKLAQNHVQLMTNTKVVVIDetgltvEESGVEK 588
Cdd:PRK09564 158 GFIG----LEAVEAAKhlgKNVRIIQLEDRILPDSFdkeITDVME--EELRENGVELHLNEFVKSLI------GEDKVEG 225
|
250 260
....*....|....*....|....*.
gi 2789488066 589 ------HLEADTIISAFGMRPNTKLA 608
Cdd:PRK09564 226 vvtdkgEYEADVVIVATGVKPNTEFL 251
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
375-483 |
6.28e-08 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 55.43 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 375 KLEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHlggtmgdICTAKFKtniKQLTKWYQVQLEKLPIDIHLN 454
Cdd:PRK09564 142 ELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDR-------ILPDSFD---KEITDVMEEELRENGVELHLN 211
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2789488066 455 ---TTITGDE--EILKT------CDYIIVSTGALPSTPAI 483
Cdd:PRK09564 212 efvKSLIGEDkvEGVVTdkgeyeADVVIVATGVKPNTEFL 251
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-458 |
9.36e-08 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 49.90 E-value: 9.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGdictakfktniKQLTKWYQVQLEKLPIDIHLNTTIT 458
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFD-----------PEIAKILQEKLEKNGIEFLLNTTVE 64
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
385-419 |
1.77e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 54.09 E-value: 1.77e-07
10 20 30
....*....|....*....|....*....|....*
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
376-491 |
2.01e-07 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 53.94 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 376 LEKTEDPQNVVVIGAGPGGMEAARV-AALeGHHVTLFEKEDHLGGTMgDictakfktniKQLTKWYQVQLEKLPIDIHLN 454
Cdd:COG1249 162 LELEELPKSLVVIGGGYIGLEFAQIfARL-GSEVTLVERGDRLLPGE-D----------PEISEALEKALEKEGIDILTG 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2789488066 455 TTIT---------------GDEEILKTCDYIIVSTGalpSTPAIPGIDGDNV 491
Cdd:COG1249 230 AKVTsvektgdgvtvtledGGGEEAVEADKVLVATG---RRPNTDGLGLEAA 278
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
382-419 |
2.54e-07 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 53.30 E-value: 2.54e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2789488066 382 PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
385-610 |
3.72e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 53.29 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGG---MEAARVAALEGHHVTLFEKEDHLG-GTMGDICTAKFKTNIKQLT----KWYqvqlEKLPIDIHLNTT 456
Cdd:TIGR02374 1 LVLVGNGMAGhrcIEEVLKLNRHMFEITIFGEEPHPNyNRILLSSVLQGEADLDDITlnskDWY----EKHGITLYTGET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 457 ITG---DEEILKTC-------DYIIVSTGALPSTPAIPGIDGDNV--------VNIVEAHRNESLikgnKIVVCGGGASG 518
Cdd:TIGR02374 77 VIQidtDQKQVITDagrtlsyDKLILATGSYPFILPIPGADKKGVyvfrtiedLDAIMAMAQRFK----KAAVIGGGLLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 519 LDGAIEMaEEMHKDVTVVEMLPE-MGKDVFFINKISLFNKLAQNHVQLMTNTKVVVIdetgltVEESGVEK-------HL 590
Cdd:TIGR02374 153 LEAAVGL-QNLGMDVSVIHHAPGlMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEI------VGATKADRirfkdgsSL 225
|
250 260
....*....|....*....|
gi 2789488066 591 EADTIISAFGMRPNTKLADQ 610
Cdd:TIGR02374 226 EADLIVMAAGIRPNDELAVS 245
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
385-613 |
3.72e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.21 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM----------GDICTAKFKtNIKQLTkwyqVQLEKlpiDIHLN 454
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLkygipefrlpKKIVDVEIE-NLKKLG----VKFET---DVIVG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 455 TTITGDEEILKTCDYIIVSTGA-LPSTPAIPGIDGDNV---------VNIVEAHRNES---LIKGNKIVVCGGGASGLDG 521
Cdd:PRK12778 506 KTITIEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVmssneyltrVNLMDAASPDSdtpIKFGKKVAVVGGGNTAMDS 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 522 A-------IEMA--------EEMHKDVTVVEMLPEMG-KDVFFINKISLF----NKLAQNHVQLMtntKVVVIDETGL-- 579
Cdd:PRK12778 586 ArtakrlgAERVtivyrrseEEMPARLEEVKHAKEEGiEFLTLHNPIEYLadekGWVKQVVLQKM---ELGEPDASGRrr 662
|
250 260 270
....*....|....*....|....*....|....
gi 2789488066 580 TVEESGVEKHLEADTIISAFGMRPNTKLADQLKE 613
Cdd:PRK12778 663 PVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPG 696
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
385-606 |
6.48e-07 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 52.08 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT---MGDICTAKFKTNIKQLTKW--------YQVQLEKLPIDI-- 451
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGcthTGTIPSKALREAVLRLIGFnqnplyssYRVKLRITFADLla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 452 HLNTTIT------------------------------------GDEEILkTCDYIIVSTGALPSTPAIPGIDGDNVVN-- 493
Cdd:PRK05249 88 RADHVINkqvevrrgqyernrvdliqgrarfvdphtvevecpdGEVETL-TADKIVIATGSRPYRPPDVDFDHPRIYDsd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 494 -IVEAHRnesLIKgnKIVVCGGG------AS---GLDgaiemaeemHKdVTVVE----MLPemgkdvfFINK---ISLFN 556
Cdd:PRK05249 167 sILSLDH---LPR--SLIIYGAGvigceyASifaALG---------VK-VTLINtrdrLLS-------FLDDeisDALSY 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2789488066 557 KLAQNHVQLMTNTKVVVIDETG---LTVEESGveKHLEADTIISAFGMRPNTK 606
Cdd:PRK05249 225 HLRDSGVTIRHNEEVEKVEGGDdgvIVHLKSG--KKIKADCLLYANGRTGNTD 275
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
380-432 |
7.64e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 52.20 E-value: 7.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2789488066 380 EDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGtmgdIC-TAKFKTN 432
Cdd:PRK07208 2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG----ISrTVTYKGN 51
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
508-591 |
8.37e-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: 47.20 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 508 KIVVCGGGASGLdgaiEMAEEMHK---DVTVVEMLPEMGKdvFFINKIS--LFNKLAQNHVQLMTNTKVvvideTGLTVE 582
Cdd:pfam00070 1 RVVVVGGGYIGL----ELAGALARlgsKVTVVERRDRLLP--GFDPEIAkiLQEKLEKNGIEFLLNTTV-----EAIEGN 69
|
....*....
gi 2789488066 583 ESGVEKHLE 591
Cdd:pfam00070 70 GDGVVVVLT 78
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
384-429 |
1.51e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 51.04 E-value: 1.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGDICTAKF 429
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
383-520 |
2.35e-06 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 50.79 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG--TMGdicTAKFKTNiKQLTKWYQVQLEKLPIDIHLNTTITGD 460
Cdd:PRK12809 311 EKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGmlTFG---IPPFKLD-KTVLSQRREIFTAMGIDFHLNCEIGRD 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2789488066 461 ---EEILKTCDYIIVSTGALPSTPA-IPGIDGDNVVN---IVEAHRNESL------------IKGNKIVVCGGGASGLD 520
Cdd:PRK12809 387 itfSDLTSEYDAVFIGVGTYGMMRAdLPHEDAPGVIQalpFLTAHTRQLMglpeseeypltdVEGKRVVVLGGGDTTMD 465
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
385-421 |
4.75e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 49.53 E-value: 4.75e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM 421
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
383-419 |
6.41e-06 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 49.09 E-value: 6.41e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEkEDHLGG 419
Cdd:PRK07845 2 TRIVIIGGGPGGYEAALVAAQLGADVTVIE-RDGLGG 37
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
385-419 |
7.34e-06 |
|
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: 48.81 E-value: 7.34e-06
10 20 30
....*....|....*....|....*....|....*
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
384-420 |
1.39e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 48.19 E-value: 1.39e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
381-421 |
1.94e-05 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 47.18 E-value: 1.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2789488066 381 DPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM 421
Cdd:COG3380 2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRM 42
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
373-476 |
2.17e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 47.05 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 373 RFKLEKTEDPQNVVVIGAGPGGMEAA--------RVAALEGH-----HVTLFEKEDHLGGTMGDictakfktnikQLTKW 439
Cdd:COG1252 140 AFERAERRRLLTIVVVGGGPTGVELAgelaellrKLLRYPGIdpdkvRITLVEAGPRILPGLGE-----------KLSEA 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2789488066 440 YQVQLEKLPIDIHLNTTITG-DEEILKT-------CDYIIVSTGA 476
Cdd:COG1252 209 AEKELEKRGVEVHTGTRVTEvDADGVTLedgeeipADTVIWAAGV 253
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
379-420 |
3.06e-05 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 46.99 E-value: 3.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2789488066 379 TEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:PRK12842 6 NELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
383-609 |
3.75e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 46.70 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGME-AARVAALEGH-HVTLFEKED-----------HLGGTMGD------ICTAKFKTNiKQLT-KWYQv 442
Cdd:PRK13512 2 PKIIVVGAVAGGATcASQIRRLDKEsDIIIFEKDRdmsfancalpyYIGEVVEDrkyalaYTPEKFYDR-KQITvKTYH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 443 qlEKLPIDIHlNTTIT-----GDEEILKTCDYIIVSTGAlpsTPAIPGIDGDNVV---NIVEAHRNESLIKGN---KIVV 511
Cdd:PRK13512 80 --EVIAINDE-RQTVTvlnrkTNEQFEESYDKLILSPGA---SANSLGFESDITFtlrNLEDTDAIDQFIKANqvdKALV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 512 CGGGASGLdgaiEMAEEMHK---DVTVV----EMLPEMGKDvffINKIsLFNKLAQNHVQLMTNTKVVVIDETGLTVEES 584
Cdd:PRK13512 154 VGAGYISL----EVLENLYErglHPTLIhrsdKINKLMDAD---MNQP-ILDELDKREIPYRLNEEIDAINGNEVTFKSG 225
|
250 260
....*....|....*....|....*
gi 2789488066 585 GVEKHleaDTIISAFGMRPNTKLAD 609
Cdd:PRK13512 226 KVEHY---DMIIEGVGTHPNSKFIE 247
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
434-607 |
4.56e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 45.68 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 434 KQLTKWYQVQLEKLPIDIHLNTTIT-----GDEEILKT------CDYIIVSTG--ALPSTPAIPgidgDNVV---NIVEA 497
Cdd:pfam13738 75 NEYAEYLRRVADHFELPINLFEEVTsvkkeDDGFVVTTskgtyqARYVIIATGefDFPNKLGVP----ELPKhysYVKDF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 498 HRneslIKGNKIVVCGGGASGLDGAIEMAeEMHKDVTVV---EMLPEMGKDVffinKISL-------FNKLAQN-HVQLM 566
Cdd:pfam13738 151 HP----YAGQKVVVIGGYNSAVDAALELV-RKGARVTVLyrgSEWEDRDSDP----SYSLspdtlnrLEELVKNgKIKAH 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2789488066 567 TNTKVVVIDETGLT--VEESGVEKHLEADTIISAFGMRPNTKL 607
Cdd:pfam13738 222 FNAEVKEITEVDVSykVHTEDGRKVTSNDDPILATGYHPDLSF 264
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
383-419 |
5.10e-05 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 46.01 E-value: 5.10e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:PLN02172 11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
385-418 |
5.70e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.03 E-value: 5.70e-05
10 20 30
....*....|....*....|....*....|....
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLG 418
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
382-419 |
9.68e-05 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 45.23 E-value: 9.68e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2789488066 382 PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
382-419 |
9.69e-05 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 45.11 E-value: 9.69e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2789488066 382 PQNVVVIGAGPGGMEAARVaaLEGHH-VTLFEKEDHLGG 419
Cdd:COG2907 3 RMRIAVIGSGISGLTAAWL--LSRRHdVTLFEANDRLGG 39
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
385-418 |
1.15e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 44.62 E-value: 1.15e-04
10 20 30
....*....|....*....|....*....|....
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLG 418
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
375-425 |
1.38e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 44.76 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2789488066 375 KLEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEkedhlGGTMGDIC 425
Cdd:PRK13748 91 KHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIE-----RGTIGGTC 136
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
383-608 |
1.89e-04 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 44.15 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGMEAA---RVAALEGHhVTLFEKEDHLG---GTMGDICTAKFKTNIKQL--TKWYQVQLEKLPIDIHLN 454
Cdd:PRK09754 4 KTIIIVGGGQAAAMAAaslRQQGFTGE-LHLFSDERHLPyerPPLSKSMLLEDSPQLQQVlpANWWQENNVHLHSGVTIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 455 TTITGDEEILKT------CDYIIVSTGAlpSTPAIPGID--GDNVVNIV---EAHR-NESLIKGNKIVVCGGGASGLDGA 522
Cdd:PRK09754 83 TLGRDTRELVLTngeswhWDQLFIATGA--AARPLPLLDalGERCFTLRhagDAARlREVLQPERSVVIVGAGTIGLELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 523 iEMAEEMHKDVTVVEMLPE-MGKDVFFINKISLFNKLAQNHVQLMTNTKVV-VIDETGLTVEESGVEKhLEADTIISAFG 600
Cdd:PRK09754 161 -ASATQRRCKVTVIELAATvMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEhVVDGEKVELTLQSGET-LQADVVIYGIG 238
|
....*...
gi 2789488066 601 MRPNTKLA 608
Cdd:PRK09754 239 ISANDQLA 246
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
385-420 |
2.25e-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: 44.05 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
384-605 |
2.46e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 43.97 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 384 NVVVIGAGPGGME-AARVAALeGHHVTLFEKEDHL-GGTMGDICTAKFKTNI----KQLTkWYQVQLEKLPIDIHL---- 453
Cdd:PRK07251 5 DLIVIGFGKAGKTlAAKLASA-GKKVALVEESKAMyGGTCINIGCIPTKTLLvaaeKNLS-FEQVMATKNTVTSRLrgkn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 454 --------------------NTTI---TGDEEILKTCDYIIVSTGALPSTPAIPGI-DGDNVVNIVEAHRNESLIKgnKI 509
Cdd:PRK07251 83 yamlagsgvdlydaeahfvsNKVIevqAGDEKIELTAETIVINTGAVSNVLPIPGLaDSKHVYDSTGIQSLETLPE--RL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 510 VVCGGGASGLDGAiEMAEEMHKDVTVVEMLPEmgkdvFFINKISLFNKLAQNH-----VQLMTNTKVVVIDETGLTVEES 584
Cdd:PRK07251 161 GIIGGGNIGLEFA-GLYNKLGSKVTVLDAAST-----ILPREEPSVAALAKQYmeedgITFLLNAHTTEVKNDGDQVLVV 234
|
250 260
....*....|....*....|.
gi 2789488066 585 GVEKHLEADTIISAFGMRPNT 605
Cdd:PRK07251 235 TEDETYRFDALLYATGRKPNT 255
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
149-327 |
3.86e-04 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 42.48 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 149 DDFKFAAGVAMDAGYDAIEI----------HAHAG-YLIDQflspvwnkrtdeyggsPENntrfAKDIYHAIREVVGKDV 217
Cdd:cd02801 67 ETLAEAAKIVEELGADGIDLnmgcpspkvtKGGAGaALLKD----------------PEL----VAEIVRAVREAVPIPV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 218 PILFRISLDHRFNSgrdleysMKILKELEKEGIDAFdidagcyeTL-------DYIfPPAYLgescmSYVcEDARKVVNV 290
Cdd:cd02801 127 TVKIRLGWDDEEET-------LELAKALEDAGASAL--------TVhgrtreqRYS-GPADW-----DYI-AEIKEAVSI 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 2789488066 291 PLI-NAGTHNPESALELIESGNVDFVSFGRALIADPMM 327
Cdd:cd02801 185 PVIaNGDIFSLEDALRCLEQTGVDGVMIGRGALGNPWL 222
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
384-420 |
4.94e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 43.17 E-value: 4.94e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 384 NVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
385-420 |
5.78e-04 |
|
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: 42.66 E-value: 5.78e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
385-415 |
6.12e-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: 42.23 E-value: 6.12e-04
10 20 30
....*....|....*....|....*....|.
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKED 415
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAP 36
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
383-480 |
1.25e-03 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 41.26 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGtmgdictakfktnikqlTKWYQVQLEKLP-IDIHLNTTI---- 457
Cdd:COG0492 142 KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-----------------SKILVERLRANPkIEVLWNTEVteie 204
|
90 100 110
....*....|....*....|....*....|....*..
gi 2789488066 458 --------------TGDEEILKtCDYIIVSTGALPST 480
Cdd:COG0492 205 gdgrvegvtlknvkTGEEKELE-VDGVFVAIGLKPNT 240
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
376-483 |
1.52e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 41.32 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 376 LEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTM----GDICTAKFKTNIKQLTKwYQVQ-LEKLPID 450
Cdd:PRK06292 163 FELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEdpevSKQAQKILSKEFKIKLG-AKVTsVEKSGDE 241
|
90 100 110
....*....|....*....|....*....|...
gi 2789488066 451 IHLNTTITGDEEILKTcDYIIVSTGALPSTPAI 483
Cdd:PRK06292 242 KVEELEKGGKTETIEA-DYVLVATGRRPNTDGL 273
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
383-483 |
1.84e-03 |
|
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: 41.22 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 383 QNVVVIGAGPGGMEAARVAALEGHHVTLFEKedhlggtmgdictakfktniKQLTKWYQVQLEKLPIDIHLNttiTGDEE 462
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDD--------------------RPAPELAAAELEAPGVEVVLG---EHPEE 61
|
90 100
....*....|....*....|.
gi 2789488066 463 ILKTCDYIIVSTGALPSTPAI 483
Cdd:COG0771 62 LLDGADLVVKSPGIPPDHPLL 82
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
379-420 |
1.89e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 41.17 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2789488066 379 TEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGT 420
Cdd:PRK07843 4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGS 45
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
385-419 |
1.89e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 41.06 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 385 VVVIGAGPGGMEAARvaALE--GHHVTLFEKEDHLGG 419
Cdd:COG1231 10 VVIVGAGLAGLAAAR--ELRkaGLDVTVLEARDRVGG 44
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
382-413 |
2.75e-03 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 40.47 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|..
gi 2789488066 382 PQNVVVIGAGPGGMEAARVAALEGHHVTLFEK 413
Cdd:cd05305 168 PAKVVILGAGVVGENAARVALGLGAEVTVLDI 199
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
385-419 |
3.65e-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: 40.07 E-value: 3.65e-03
10 20 30
....*....|....*....|....*....|....*
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG 419
Cdd:pfam01266 2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
376-480 |
4.27e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 40.19 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 376 LEKTEDPQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLggtmgdicTAKFKTNIKQLTkwyQVQLEKLPIDIHLNT 455
Cdd:PRK06370 165 FSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL--------LPREDEDVAAAV---REILEREGIDVRLNA 233
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2789488066 456 TI-----TGDEEILK----------TCDYIIVSTGALPST 480
Cdd:PRK06370 234 ECirverDGDGIAVGldcnggapeiTGSHILVAVGRVPNT 273
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
385-520 |
4.87e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 40.12 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGG--TMGdicTAKFKTNIKQLTKWYQVqLEKLPIDIHLNTTITGD-- 460
Cdd:PRK12769 330 VAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGllTFG---IPAFKLDKSLLARRREI-FSAMGIEFELNCEVGKDis 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2789488066 461 -EEILKTCDYIIVSTGALPSTPA-IPGIDGDNV-------------VNIVEAHRNESLI--KGNKIVVCGGGASGLD 520
Cdd:PRK12769 406 lESLLEDYDAVFVGVGTYRSMKAgLPNEDAPGVydalpfliantkqVMGLEELPEEPFIntAGLNVVVLGGGDTAMD 482
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
382-418 |
7.51e-03 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 39.25 E-value: 7.51e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2789488066 382 PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLG 418
Cdd:PRK08163 4 VTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
382-435 |
8.38e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.49 E-value: 8.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2789488066 382 PQNVVVIGAGPGGMEAARVAALEGHHVTLFEKEDHLGGTMGDICTAKFKTNIKQ 435
Cdd:smart01002 20 PAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQ 73
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
385-418 |
8.97e-03 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 38.69 E-value: 8.97e-03
10 20 30
....*....|....*....|....*....|....*
gi 2789488066 385 VVVIGAGPGGMEAARVAALEGHHVTLF-EKEDHLG 418
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLItHNTDTIA 36
|
|
| |
