|
Name |
Accession |
Description |
Interval |
E-value |
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
2-354 |
0e+00 |
|
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.
Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 612.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 2 LEQKLQLPHTELRNRLVMGSMHTGLEEGWHNRKRLRAFYEARAKGGTGLIITGGYSPNIRGKLSPFASTFNSFYDVIKHK 81
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 82 AYTDAVHQHGGKICLQLLHAGRYAYHPFNQAPSSIQAPINPYKPKEMSLGSIKKTIKDFANSAKLAEKAGYDGVEIMGSE 161
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 162 GYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVKQQALALEQAGVDI 241
Cdd:cd02930 161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 242 FNTGIGWHEARVPTIASMVPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLISMARPLLADPEFFNKYV 321
Cdd:cd02930 241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 2249646788 322 NNKSEQINICIGCNQGCLDHVFKNKRATCLVNP 354
Cdd:cd02930 321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
2-357 |
1.70e-133 |
|
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: 396.08 E-value: 1.70e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 2 LEQKLQLPHTELRNRLVMGSMHTGL-EEGWHNRKRLRAFYEARAKGGTGLIITGGYSPNIRGKLSPFASTFNSFYDVIKH 80
Cdd:COG1902 7 LFSPLTLGGLTLKNRIVMAPMTRGRaDEDGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQIAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGGKICLQLLHAGRYAYHPFNQ-----APSSIQAPINPYKPKEMSLGSIKKTIKDFANSAKLAEKAGYDGV 155
Cdd:COG1902 87 RRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGgwppvAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKEAGFDGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 156 EIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVKQQALALE 235
Cdd:COG1902 167 EIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVELAKALE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 236 QAGVDIFNTGIGWHEARvPTIASMVPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLISMARPLLADPE 315
Cdd:COG1902 247 EAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPLLADPD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2249646788 316 FFNKYVNNKSEQINICIGCNQgCLDHVFknKRATCLVNPQAA 357
Cdd:COG1902 326 LPNKAAAGRGDEIRPCIGCNQ-CLPTFY--GGASCYVDPRLG 364
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
4-319 |
2.18e-106 |
|
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: 325.30 E-value: 2.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 4 QKLQLPHTELRNRLVMGSMHTGL-EEGWHNRKRLRAFYEARAKGGTGLIITGGYSPNIRGKLSPFASTFNSFYDVIKHKA 82
Cdd:cd02803 2 SPIKIGGLTLKNRIVMAPMTENMaTEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 83 YTDAVHQHGGKICLQLLHAGRYAYHPFN----QAPSSIQAPINPYKPKEMSLGSIKKTIKDFANSAKLAEKAGYDGVEIM 158
Cdd:cd02803 82 LTEAVHAHGAKIFAQLAHAGRQAQPNLTggppPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEIH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 159 GSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVKQQALALEQAG 238
Cdd:cd02803 162 GAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 239 VDIFNTGIGWHEARVPTIASM-VPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLISMARPLLADPEFF 317
Cdd:cd02803 242 VDALHVSGGSYESPPPIIPPPyVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDLP 321
|
..
gi 2249646788 318 NK 319
Cdd:cd02803 322 NK 323
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
4-335 |
1.59e-85 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.
Pssm-ID: 240085 [Multi-domain] Cd Length: 343 Bit Score: 271.79 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 4 QKLQLPHTELRNRLVMGSMHTGLEEGWHNRKRLRAFYEARAKGGTGLIITGGYSPNIRGklSPFASTFNSFYD-VIKH-K 81
Cdd:cd04734 3 SPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSD--SPAFGNLNASDDeIIPGfR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 82 AYTDAVHQHGGKICLQLLHAGRYAYHPFN----QAPSSIQAPINPYKPKEMSLGSIKKTIKDFANSAKLAEKAGYDGVEI 157
Cdd:cd04734 81 RLAEAVHAHGAVIMIQLTHLGRRGDGDGSwlppLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 158 MGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVKQQALALEQA 237
Cdd:cd04734 161 QAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 238 G-VDIFNTGIG---WHEARVPTIASM-VPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLISMARPLLA 312
Cdd:cd04734 241 GlIDYVNVSAGsyyTLLGLAHVVPSMgMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAHIA 320
|
330 340
....*....|....*....|...
gi 2249646788 313 DPEFFNKYVNNKSEQINICIGCN 335
Cdd:cd04734 321 DPHLVAKAREGREDDIRPCIGCN 343
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
2-316 |
2.84e-70 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 231.57 E-value: 2.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 2 LEQKLQLPHTELRNRLVMGSM--HTGLEEGWHNRKRLRAFYEARAKGGTGLIITGGYSPNIRGKLSPFASTFNSFYDVIK 79
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPMtrLRSLDDGTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 80 HKAYTDAVHQHGGKICLQLLHAGRYAY-----HPFNQAPSSIQA------PINPYKpKEMSLGSIKKTIKDFANSAKLAE 148
Cdd:pfam00724 82 WRKLTEAVHKNGSKAGVQLWHLGREAPmeyrpDLEVDGPSDPFAlgaqefEIASPR-YEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 149 KAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVK 228
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAETA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 229 QQALALEQAGVDifnTGIGWHEARVpTIASMVPAGAF------KEASKRLKETVSVPVIAVNRINTPEIANGILEAGESD 302
Cdd:pfam00724 241 QFIYLLAELGVR---LPDGWHLAYI-HAIEPRPRGAGpvrtrqQHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
|
330
....*....|....
gi 2249646788 303 LISMARPLLADPEF 316
Cdd:pfam00724 317 LVAMGRPFLADPDL 330
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
80-316 |
7.99e-70 |
|
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: 230.07 E-value: 7.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 80 HKAYTDAVHQHGGKICLQLLHAGRYA--YHPFNQ---------------APSSIQAPINPYKPKEMSLGSIKKTIKDFAN 142
Cdd:cd02932 79 LKRIVDFIHSQGAKIGIQLAHAGRKAstAPPWEGggpllppggggwqvvAPSAIPFDEGWPTPRELTREEIAEVVDAFVA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 143 SAKLAEKAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGS 222
Cdd:cd02932 159 AARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGW 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 223 TPDEVKQQALALEQAGVDIFN--TGiGWHEARVPTIA--SMVPagafkeASKRLKETVSVPVIAVNRINTPEIANGILEA 298
Cdd:cd02932 239 DLEDSVELAKALKELGVDLIDvsSG-GNSPAQKIPVGpgYQVP------FAERIRQEAGIPVIAVGLITDPEQAEAILES 311
|
250
....*....|....*...
gi 2249646788 299 GESDLISMARPLLADPEF 316
Cdd:cd02932 312 GRADLVALGRELLRNPYW 329
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
12-354 |
1.69e-62 |
|
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: 212.37 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 12 ELRNRLVMGSMHT-GL--EEGWHNrKRLRAFYEARAKGGTGLIITGGysPNIRGKLSPFA------STFNSFYDVIKHKA 82
Cdd:cd02931 11 EIKNRFAMAPMGPlGLadNDGAFN-QRGIDYYVERAKGGTGLIITGV--TMVDNEIEQFPmpslpcPTYNPTAFIRTAKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 83 YTDAVHQHGGKICLQLLHA-GRYAYHPFNQ-----APSSIQAPINPYKP-KEMSLGSIKKTIKDFANSAKLAEKAGYDGV 155
Cdd:cd02931 88 MTERVHAYGTKIFLQLTAGfGRVCIPGFLGedkpvAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIAKEAGFDGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 156 EIMG-SEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIP---NGSTPDEVKQQ- 230
Cdd:cd02931 168 EIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSVKSYIKdlrQGALPGEEFQEk 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 231 ----------ALALEQAGVDIFNTGIG----WHEARVPTIASmvpAGAFKEASKRLKETVSVPVIAVNRINTPEIANGIL 296
Cdd:cd02931 248 grdleeglkaAKILEEAGYDALDVDAGsydaWYWNHPPMYQK---KGMYLPYCKALKEVVDVPVIMAGRMEDPELASEAI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2249646788 297 EAGESDLISMARPLLADPEFFNKYVNNKSEQINICIGCNQGCLDHVFKNKRATCLVNP 354
Cdd:cd02931 325 NEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
2-329 |
4.50e-56 |
|
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: 193.97 E-value: 4.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 2 LEQKLQLPH-TELRNRLVMGSM--HTGLEEGwHNRKRLRAFYEARAKGGTGLIITGGY-SPNIRGKLSPFASTFNSFYDV 77
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVMAPMttYSSNPDG-TITDDELAYYQRRAGGVGMVITGATYvSPSGIGFEGGFSADDDSDIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 78 IKhkAYTDAVHQHGGKICLQLLHAGRYAYHPFNQ-----APSSIQAPINP-YKPKEMSLGSIKKTIKDFANSAKLAEKAG 151
Cdd:cd04735 80 LR--KLAQAIKSKGAKAILQIFHAGRMANPALVPggdvvSPSAIAAFRPGaHTPRELTHEEIEDIIDAFGEATRRAIEAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 152 YDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQK----FIIVFRLSVMDLIPNGSTPDEV 227
Cdd:cd04735 158 FDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHadkdFILGYRFSPEEPEEPGIRMEDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 228 KQQALALEQAGVDIFNTGIGWHearvpTIASMVPAGAFKEASKRLKETVS--VPVIAVNRINTPEIANGILEAGeSDLIS 305
Cdd:cd04735 238 LALVDKLADKGLDYLHISLWDF-----DRKSRRGRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETG-ADLVA 311
|
330 340
....*....|....*....|....
gi 2249646788 306 MARPLLADPEFFNKYVNNKSEQIN 329
Cdd:cd04735 312 IGRGLLVDPDWVEKIKEGREDEIN 335
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
81-320 |
2.37e-54 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240084 [Multi-domain] Cd Length: 338 Bit Score: 188.95 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGGKICLQLLHAGRYAYHPFNQAPSSIQAPINPY-------KPKEMSLGSIKKTIKDFANSAKLAEKAGYD 153
Cdd:cd04733 85 REWAAAAKANGALIWAQLNHPGRQSPAGLNQNPVAPSVALDPGglgklfgKPRAMTEEEIEDVIDRFAHAARLAQEAGFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 154 GVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVKQQALA 233
Cdd:cd04733 165 GVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEEDALEVVEA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 234 LEQAGVDIFNTGIGWHEArvPTIASMVPAGA------FKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLISMA 307
Cdd:cd04733 245 LEEAGVDLVELSGGTYES--PAMAGAKKESTiareayFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASGAVDGIGLA 322
|
250
....*....|...
gi 2249646788 308 RPLLADPEFFNKY 320
Cdd:cd04733 323 RPLALEPDLPNKL 335
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
11-316 |
9.27e-49 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 173.73 E-value: 9.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 11 TELRNRLVMGSM-------HTGLEEGWHnrkrlRAFYEARAKGGTGLIITGGYSPNIRGKLSPFASTFNSFYDVIKHKAY 83
Cdd:PRK13523 12 VTLKNRIVMSPMcmyssenKDGKVTNFH-----LIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIEGLHKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 84 TDAVHQHGGKICLQLLHAGRYAYHPFNQ-APSSIQAPINPYKPKEMSLGSIKKTIKDFANSAKLAEKAGYDGVEIMGSEG 162
Cdd:PRK13523 87 VTFIHDHGAKAAIQLAHAGRKAELEGDIvAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEIHGAHG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 163 YLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRaKVSQKFIIVfRLSVMDLIPNGSTPDEVKQQALALEQAGVDIF 242
Cdd:PRK13523 167 YLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVK-EVWDGPLFV-RISASDYHPGGLTVQDYVQYAKWMKEQGVDLI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2249646788 243 NTGIGwheARVPTIASMVPAGAFKEASKrLKETVSVPVIAVNRINTPEIANGILEAGESDLISMARPLLADPEF 316
Cdd:PRK13523 245 DVSSG---AVVPARIDVYPGYQVPFAEH-IREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNPYF 314
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
6-314 |
6.81e-47 |
|
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: 168.81 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 6 LQLPHTELRNRLVMGSMhTgleegwhnrkRLRA------------FYEARAkggtgliitgGY----------SPNIRGk 63
Cdd:cd02933 6 LKLGNLTLKNRIVMAPL-T----------RSRAdpdgvptdlmaeYYAQRA----------SAgliiteatqiSPQGQG- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 64 lspFAST---FNSfydviKH----KAYTDAVHQHGGKICLQLLHAGRYAyHPFNQ-------APSSIQAPINPYK----- 124
Cdd:cd02933 64 ---YPNTpgiYTD-----EQvegwKKVTDAVHAKGGKIFLQLWHVGRVS-HPSLLpggappvAPSAIAAEGKVFTpagkv 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 125 ----PKEMSLGSIKKTIKDFANSAKLAEKAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRA 200
Cdd:cd02933 135 pyptPRALTTEEIPGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 201 KVSQKFIIVfRLSvmdliP----NGSTPDEVKQQALALeqagVDIFNT-GIGW-H--EARVPTIASMVPAGAFKEASKRL 272
Cdd:cd02933 215 AIGADRVGI-RLS-----PfgtfNDMGDSDPEATFSYL----AKELNKrGLAYlHlvEPRVAGNPEDQPPDFLDFLRKAF 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2249646788 273 KetvsVPVIAVNRInTPEIANGILEAGESDLISMARPLLADP 314
Cdd:cd02933 285 K----GPLIAAGGY-DAESAEAALADGKADLVAFGRPFIANP 321
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
81-319 |
2.33e-46 |
|
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: 167.88 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGGKICLQLLHAG---RYAYHPFNQA----PSSIQAPINPyKPKEMSLGSIKKTIKDFANSAKLAEKAGYD 153
Cdd:cd04747 81 KKVVDEVHAAGGKIAPQLWHVGamrKLGTPPFPDVpplsPSGLVGPGKP-VGREMTEADIDDVIAAFARAAADARRLGFD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 154 GVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLS---VMD----LIPNgstPDE 226
Cdd:cd04747 160 GIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSqwkQQDytarLADT---PDE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 227 VKQQALALEQAGVDIFN----------------TGIGWheAR----VPTIA--SMVPAGAFkeaskrLKETVSVPVIAVN 284
Cdd:cd04747 237 LEALLAPLVDAGVDIFHcstrrfwepefegselNLAGW--TKkltgLPTITvgSVGLDGDF------IGAFAGDEGASPA 308
|
250 260 270
....*....|....*....|....*....|....*
gi 2249646788 285 RIntpEIANGILEAGESDLISMARPLLADPEFFNK 319
Cdd:cd04747 309 SL---DRLLERLERGEFDLVAVGRALLSDPAWVAK 340
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
76-335 |
2.07e-43 |
|
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: 160.21 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 76 DVIKHKAYTDAVHQHGGKICLQLLHAGRYAYHPFNQ----APSSIQ---APINPYKPKEMSLGSIKKTIKDFANSAKLAE 148
Cdd:cd02929 81 DIRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESRetplGPSQLPsefPTGGPVQAREMDKDDIKRVRRWYVDAALRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 149 KAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIPNGSTPDEVK 228
Cdd:cd02929 161 DAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIGPGGIESEGE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 229 QQALaLEQAG--VDIFNTGIG-WHEARVPtiASMVPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGILEAGESDLIS 305
Cdd:cd02929 241 GVEF-VEMLDelPDLWDVNVGdWANDGED--SRFYPEGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVVKSGILDLIG 317
|
250 260 270
....*....|....*....|....*....|
gi 2249646788 306 MARPLLADPEFFNKYVNNKSEQINICIGCN 335
Cdd:cd02929 318 AARPSIADPFLPKKIREGRIDDIRECIGCN 347
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
81-314 |
3.93e-40 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 157.02 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGG-KICLQLLHAGRYAY---------HPFNQ------APSSIqapinPYK-----PKEMSLGSIKKTIKD 139
Cdd:PRK08255 478 KRIVDFVHANSDaKIGIQLGHSGRKGStrlgwegidEPLEEgnwpliSASPL-----PYLpgsqvPREMTRADMDRVRDD 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 140 FANSAKLAEKAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVMDLIP 219
Cdd:PRK08255 553 FVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 220 NGSTPDEVKQQALALEQAGVDIFN--TGIGWHEARvPTIASM--VPagaFkeaSKRLKETVSVPVIAVNRINTPEIANGI 295
Cdd:PRK08255 633 GGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYGRMyqTP---F---ADRIRNEAGIATIAVGAISEADHVNSI 705
|
250
....*....|....*....
gi 2249646788 296 LEAGESDLISMARPLLADP 314
Cdd:PRK08255 706 IAAGRADLCALARPHLADP 724
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
81-315 |
1.26e-28 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 117.90 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGGKICLQLLHAGRYAY---HPFNQAP---SSIQAP--------------INPYKPKEMSLGSIKKTIKDF 140
Cdd:PRK10605 82 KKITAGVHAEGGHIAVQLWHTGRISHaslQPGGQAPvapSAINAGtrtslrdengqairVETSTPRALELEEIPGIVNDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 141 ANSAKLAEKAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVSQKF--IIVFRLSVMDLI 218
Cdd:PRK10605 162 RQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRigIRISPLGTFNNV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 219 PNGstPDEVKQQALALEQAGvdifNTGIGWHEARVPTIASMVP-AGAFKEAskrLKETVSVPVIAVNRInTPEIANGILE 297
Cdd:PRK10605 242 DNG--PNEEADALYLIEQLG----KRGIAYLHMSEPDWAGGEPySDAFREK---VRARFHGVIIGAGAY-TAEKAETLIG 311
|
250
....*....|....*...
gi 2249646788 298 AGESDLISMARPLLADPE 315
Cdd:PRK10605 312 KGLIDAVAFGRDYIANPD 329
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
81-202 |
1.24e-23 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 103.40 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 81 KAYTDAVHQHGGKICLQLLHAGR---YAYHPFNQAP-SSIQAPINPY--------------KPKEMSLGSIKKTIKDFAN 142
Cdd:PLN02411 90 KKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISERwrilmpdgsygkypKPRALETSEIPEVVEHYRQ 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 143 SAKLAEKAGYDGVEIMGSEGYLINEFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKV 202
Cdd:PLN02411 170 AALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAI 229
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
373-653 |
7.58e-20 |
|
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: 92.51 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGqfnLAM-QVPgkeDF---NHTLNYFTNELKRLNVDLQLGTEFTDN 448
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG---LLRyGIP---EFrlpKDVLDREIELIEALGVEFRTNVEVGKD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 449 M-----LNQYDDVVFATGV-RPREAKIECSDGKRV-FAYD---EVIRGE-----VELGDKIAILGAGGIGFD-------- 505
Cdd:COG0493 198 ItldelLEEFDAVFLATGAgKPRDLGIPGEDLKGVhSAMDfltAVNLGEapdtiLAVGKRVVVIGGGNTAMDcartalrl 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 506 -----MVAFLSEHKGQTIEQFKTQWGIEcEAAPEKDNRQIYmlkrsagRF-GSELGKTTgwihrqvakqhGVKqIAECQY 579
Cdd:COG0493 278 gaesvTIVYRRTREEMPASKEEVEEALE-EGVEFLFLVAPV-------EIiGDENGRVT-----------GLE-CVRMEL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 580 LSFDKQGLK--ITVKGEEQILDVDTVIACIGQVSNTETF-------------------DNQTENAKVHVIG----GAKLA 634
Cdd:COG0493 338 GEPDESGRRrpVPIEGSEFTLPADLVILAIGQTPDPSGLeeelgleldkrgtivvdeeTYQTSLPGVFAGGdavrGPSLV 417
|
330
....*....|....*....
gi 2249646788 635 AaidakRAIFEALQVARKI 653
Cdd:COG0493 418 V-----WAIAEGRKAARAI 431
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
373-618 |
1.19e-19 |
|
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: 90.07 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQM-GGQFNLAMQVPGKEDFNHTLNYF-------TNELKRL--NVDLQLG 442
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWadlykrkEEVVKKLnnGIEVLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 443 TE----------FTDNMLN-------QYDDVVFATGVRPR-----EAKIECSDGKRVFAYDEVIRgEVELGDKIAILGAG 500
Cdd:pfam07992 83 TEvvsidpgakkVVLEELVdgdgetiTYDRLVIATGARPRlppipGVELNVGFLVRTLDSAEALR-LKLLPKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 501 GIGFDMVAFLSEHKGQ-TIeqfktqwgieceaapekdnrqIYMLKRSAGRFGSELGKttgWIHRqVAKQHGVKQIAECQY 579
Cdd:pfam07992 162 YIGVELAAALAKLGKEvTL---------------------IEALDRLLRAFDEEISA---ALEK-ALEKNGVEVRLGTSV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2249646788 580 LSFDKQGLKITVK-GEEQILDVDTVIACIGQVSNTETFDN 618
Cdd:pfam07992 217 KEIIGDGDGVEVIlKDGTEIDADLVVVAIGRRPNTELLEA 256
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
366-621 |
3.99e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 71.75 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 366 KAPSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG-------QFNLAMQVPGKEdfnhtlnyfTNELKRLNVD 438
Cdd:PRK11749 136 APKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllrygipEFRLPKDIVDRE---------VERLLKLGVE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 439 LQLGTE----FT-DNMLNQYDDVVFATGV-RPREAKIECSDGKRVF-AYDEVIR-------GEVELGDKIAILGAGGIGF 504
Cdd:PRK11749 207 IRTNTEvgrdITlDELRAGYDAVFIGTGAgLPRFLGIPGENLGGVYsAVDFLTRvnqavadYDLPVGKRVVVIGGGNTAM 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 505 DMVaflsehkGQTIEQfktqwGIEceaapekdnrQIYMLKR------SAGRFGSELGKTTG----WIHRQVA---KQHGV 571
Cdd:PRK11749 287 DAA-------RTAKRL-----GAE----------SVTIVYRrgreemPASEEEVEHAKEEGvefeWLAAPVEilgDEGRV 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2249646788 572 KQIaECQY---LSFDKQGL-KITVKGEEQILDVDTVIACIGQVSNTETFDNQTE 621
Cdd:PRK11749 345 TGV-EFVRmelGEPDASGRrRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPG 397
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
373-619 |
4.46e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 70.53 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQmGGQFNLAMQV---PGkedFNHTL------NYFTNELKRLNVDLQLGT 443
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP-GGQLATTKEIenyPG---FPEGIsgpelaERLREQAERFGAEILLEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 444 ----EFTDNML-------NQY--DDVVFATGVRPREAKIECSD---GKRVFaYDEVIRGEVELGDKIAILGAGGIGFDMV 507
Cdd:COG0492 79 vtsvDKDDGPFrvttddgTEYeaKAVIIATGAGPRKLGLPGEEefeGRGVS-YCATCDGFFFRGKDVVVVGGGDSALEEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 508 AFLSEHKgqtieqfktqwgieceaapekdnRQIYMLKRsagrfGSELGKTTGWIHRqVAKQHGVKQIAECQYLSFDKQG- 586
Cdd:COG0492 158 LYLTKFA-----------------------SKVTLIHR-----RDELRASKILVER-LRANPKIEVLWNTEVTEIEGDGr 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 2249646788 587 -----LKITVKGEEQILDVDTVIACIGQVSNTETFDNQ 619
Cdd:COG0492 209 vegvtLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGL 246
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
365-610 |
7.04e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 70.40 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 365 EKAPSSRL-VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQfnLAMQVPG----KED---------------FNHT 424
Cdd:PRK12770 12 EKPPPTGKkVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGL--MLFGIPEfripIERvregvkeleeagvvfHTRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 425 LNYFTNELKRLNVDlQLGTEFTD--NMLNQYDDVVFATGV-RPREAKIECSDGKRVFA---------------YDEVIRG 486
Cdd:PRK12770 90 KVCCGEPLHEEEGD-EFVERIVSleELVKKYDAVLIATGTwKSRKLGIPGEDLPGVYSaleylfriraaklgyLPWEKVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 487 EVElGDKIAILGAGGIGFDmVAFLSEHKGQtieqfktqwgieceaapEKdnrqIYMLKRS------AGRFGSELGKTTG- 559
Cdd:PRK12770 169 PVE-GKKVVVVGAGLTAVD-AALEAVLLGA-----------------EK----VYLAYRRtineapAGKYEIERLIARGv 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 560 -WIHR----QVAKQHGVK--QIAECQYLSFDKQGLKITVK--GEEQILDVDTVIACIGQV 610
Cdd:PRK12770 226 eFLELvtpvRIIGEGRVEgvELAKMRLGEPDESGRPRPVPipGSEFVLEADTVVFAIGEI 285
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
339-473 |
4.53e-12 |
|
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: 67.53 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 339 LDHVFKNKratclvNPQAAFELDYSLEKAPSSRLVlVVGAGPAGLAASCYLAAKGHKVTLIERKEQMggqfnlaMQVPGK 418
Cdd:COG0446 100 LPGVFTLR------TLDDADALREALKEFKGKRAV-VIGGGPIGLELAEALRKRGLKVTLVERAPRL-------LGVLDP 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2249646788 419 EdfnhTLNYFTNELKRLNVDLQLGTE-------------FTDNMLNQYDDVVFATGVRP-----REAKIECSD 473
Cdd:COG0446 166 E----MAALLEEELREHGVELRLGETvvaidgddkvavtLTDGEEIPADLVVVAPGVRPntelaKDAGLALGE 234
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
395-614 |
7.55e-12 |
|
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: 66.76 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 395 KVTLIERKEQMGGQ-FNLAMQVPGKEDFNHTLNYFTNE-LKRLNVDLQLGTE------------FTDNMLNQYDDVVFAT 460
Cdd:COG0446 7 EITVIEKGPHHSYQpCGLPYYVGGGIKDPEDLLVRTPEsFERKGIDVRTGTEvtaidpeaktvtLRDGETLSYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 461 GVRPREAKIECSDGKRVF---AYDEV--IRGEVEL--GDKIAILGAGGIGFDMVAFLSEHKGQ-TIeqfktqwgieceaa 532
Cdd:COG0446 87 GARPRPPPIPGLDLPGVFtlrTLDDAdaLREALKEfkGKRAVVIGGGPIGLELAEALRKRGLKvTL-------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 533 pekdnrqIYMLKRSAGRFGSELGKttgWIHRQVaKQHGVKQIAECQYLSFD-KQGLKITVKGEEQIlDVDTVIACIGQVS 611
Cdd:COG0446 153 -------VERAPRLLGVLDPEMAA---LLEEEL-REHGVELRLGETVVAIDgDDKVAVTLTDGEEI-PADLVVVAPGVRP 220
|
...
gi 2249646788 612 NTE 614
Cdd:COG0446 221 NTE 223
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
367-617 |
1.55e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 64.13 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 367 APSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGqfnlaMQVPGKEDFNHTLNYFTNELKR---LNVDLQLGT 443
Cdd:PRK12771 134 PDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG-----MMRYGIPAYRLPREVLDAEIQRildLGVEVRLGV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 444 EFTDNML-----NQYDDVVFATGV-RPREAKIECSDGKRVFAYDEVIR----GE-VELGDKIAILGAGGIGFDmVAFLSE 512
Cdd:PRK12771 209 RVGEDITleqleGEFDAVFVAIGAqLGKRLPIPGEDAAGVLDAVDFLRavgeGEpPFLGKRVVVIGGGNTAMD-AARTAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 513 HKG---------QTIEQFkTQWGIECEAApEKDNRQIYMLKRSAGRFGSELGKTTGWihrqvakqhgvkqIAECQYLSFD 583
Cdd:PRK12771 288 RLGaeevtivyrRTREDM-PAHDEEIEEA-LREGVEINWLRTPVEIEGDENGATGLR-------------VITVEKMELD 352
|
250 260 270
....*....|....*....|....*....|....
gi 2249646788 584 KQGLKITVKGEEQILDVDTVIACIGQVSNTETFD 617
Cdd:PRK12771 353 EDGRPSPVTGEEETLEADLVVLAIGQDIDSAGLE 386
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
373-627 |
1.64e-10 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 63.57 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIErKEQMGG---------------------------QFNLAMQVPG-------- 417
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGGtclnvgcipskallhaaevahearhaaEFGISAGAPSvdwaalma 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 418 -KEDFNHTLNYFTNE-LKRLNVDLQLGT-EFTDNmlNQ----------YDDVVFATGVRPREAKIECSDGKRVFAYDEVI 484
Cdd:COG1249 85 rKDKVVDRLRGGVEElLKKNGVDVIRGRaRFVDP--HTvevtggetltADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 485 RGEvELGDKIAILGAGGIGfdmvaflsehkgqtieqfktqwgieCEAApekdnrQIYmlkrsaGRFGSE----------L 554
Cdd:COG1249 163 ELE-ELPKSLVVIGGGYIG-------------------------LEFA------QIF------ARLGSEvtlvergdrlL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 555 GKTTGWIHRQVAKQ---HGVKQIAECQYLSFDKQGLKITV----KGEEQILDVDTVIACIGQVSNTETFDnqTENAKVHV 627
Cdd:COG1249 205 PGEDPEISEALEKAlekEGIDILTGAKVTSVEKTGDGVTVtledGGGEEAVEADKVLVATGRRPNTDGLG--LEAAGVEL 282
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
357-653 |
2.16e-10 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 63.26 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 357 AFELDYSLEKAPSSRL---VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG-------QFNLAMQVPGKEdfnhtLN 426
Cdd:PRK12810 127 AFEEGWVKPDPPVKRTgkkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipDFKLEKEVIDRR-----IE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 427 YFTNE--LKRLNVdlQLGTEFT-DNMLNQYDDVVFATGV-RPREAKIECSDGKRV-FAYD-----------EVIRGEVEL 490
Cdd:PRK12810 202 LMEAEgiEFRTNV--EVGKDITaEELLAEYDAVFLGTGAyKPRDLGIPGRDLDGVhFAMDfliqntrrvlgDETEPFISA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 491 GDK-IAILGAGGIGFDMV--AFL----------------SEHKGQTIE-----QFKTQWGIEcEAAPEKDNRQiymlkrs 546
Cdd:PRK12810 280 KGKhVVVIGGGDTGMDCVgtAIRqgaksvtqrdimpmppSRRNKNNPWpywpmKLEVSNAHE-EGVEREFNVQ------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 547 AGRFGSELGKTTGwihrqvakqhgvkqiAECQYLSFDKQGLKItVKGEEQILDVDTVIACIGQVSNTETF--------DN 618
Cdd:PRK12810 352 TKEFEGENGKVTG---------------VKVVRTELGEGDFEP-VEGSEFVLPADLVLLAMGFTGPEAGLlaqfgvelDE 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2249646788 619 -----------QTENAKVHVIGgaklaaaiDAKR-------AIFEALQVARKI 653
Cdd:PRK12810 416 rgrvaapdnayQTSNPKVFAAG--------DMRRgqslvvwAIAEGRQAARAI 460
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
373-407 |
2.57e-10 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 63.33 E-value: 2.57e-10
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
136-308 |
3.32e-09 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 57.21 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 136 TIKDFANSAKLAEKAGYDGVEIMGSEGYlinefmanhtnkrtdnyggslenRMRLAVEIVKAVRAKVSQkFIIVFRLSVM 215
Cdd:cd04722 69 AAAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAVPD-VKVVVKLSPT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 216 DLIPNGstpdevkqqalALEQAGVDIFNTGIGWhearvPTIASMVPAGAFKEASKRLKETVSVPVIAVNRINTPEIANGI 295
Cdd:cd04722 125 GELAAA-----------AAEEAGVDEVGLGNGG-----GGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEA 188
|
170
....*....|...
gi 2249646788 296 LEAGeSDLISMAR 308
Cdd:cd04722 189 LALG-ADGVIVGS 200
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
365-461 |
8.86e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.59 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 365 EKAPSS-RLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG-------QFNLAMQVPGKEdfnhtlnyfTNELKRLN 436
Cdd:PRK12814 187 ERAPKSgKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGmmrygipRFRLPESVIDAD---------IAPLRAMG 257
|
90 100 110
....*....|....*....|....*....|
gi 2249646788 437 VDLQLGTEF-----TDNMLNQYDDVVFATG 461
Cdd:PRK12814 258 AEFRFNTVFgrditLEELQKEFDAVLLAVG 287
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
373-614 |
2.18e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 56.69 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGH--KVTLIERkEQmGGQFN---LAMQVPGKEDFNHTLNYFTNELKRLNVDLQLGTE--- 444
Cdd:COG1251 4 IVIIGAGMAGVRAAEELRKLDPdgEITVIGA-EP-HPPYNrppLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRvta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 445 --------FTDN--MLNqYDDVVFATGVRPREAKIECSDGKRVFAY----D-EVIRGEVELGDKIAILGAGGIGFDMVAF 509
Cdd:COG1251 82 idraartvTLADgeTLP-YDKLVLATGSRPRVPPIPGADLPGVFTLrtldDaDALRAALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 510 LSEHkgqtieqfktqwGIE---CEAAPekdnrqiYMLKRSAGRFGSELgkttgwIHRQVAkQHGVK-----QIAEcqyLS 581
Cdd:COG1251 161 LRKR------------GLEvtvVERAP-------RLLPRQLDEEAGAL------LQRLLE-ALGVEvrlgtGVTE---IE 211
|
250 260 270
....*....|....*....|....*....|....
gi 2249646788 582 FDKQGLKITVK-GEEqiLDVDTVIACIGQVSNTE 614
Cdd:COG1251 212 GDDRVTGVRLAdGEE--LPADLVVVAIGVRPNTE 243
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
357-612 |
2.66e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 56.56 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 357 AFELDYSLEKAPSSRL--VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG-------QFNLAmqvpgKEDfnhTLNY 427
Cdd:PRK12831 125 ARENGIDLSETEEKKGkkVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlvygipEFRLP-----KET---VVKK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 428 FTNELKRLNVDLQL----GTEFT-DNMLNQ--YDDVVFATGV-RPREAKIECSDGKRVF-------------AYDEVIRG 486
Cdd:PRK12831 197 EIENIKKLGVKIETnvvvGKTVTiDELLEEegFDAVFIGSGAgLPKFMGIPGENLNGVFsanefltrvnlmkAYKPEYDT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 487 EVELGDKIAILGAGGIGFDmvaflsehkgqtieqfktqwgieceAApekdnrqiymlkRSAGRFGSELgkttgWI----- 561
Cdd:PRK12831 277 PIKVGKKVAVVGGGNVAMD-------------------------AA------------RTALRLGAEV-----HIvyrrs 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 562 -------HRQV--AKQHGVK------------------QIAECQYLSF---DKQGLK--ITVKGEEQILDVDTVIACIGQ 609
Cdd:PRK12831 315 eeelparVEEVhhAKEEGVIfdlltnpveilgdengwvKGMKCIKMELgepDASGRRrpVEIEGSEFVLEVDTVIMSLGT 394
|
...
gi 2249646788 610 VSN 612
Cdd:PRK12831 395 SPN 397
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
375-408 |
3.51e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 50.61 E-value: 3.51e-08
10 20 30
....*....|....*....|....*....|....
gi 2249646788 375 VVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQ 408
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
373-407 |
8.81e-08 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 54.86 E-value: 8.81e-08
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG3349 6 VVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
373-404 |
1.10e-07 |
|
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: 54.17 E-value: 1.10e-07
10 20 30
....*....|....*....|....*....|..
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQ 404
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAPP 37
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
373-407 |
1.20e-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: 54.45 E-value: 1.20e-07
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
365-420 |
1.41e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 54.48 E-value: 1.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2249646788 365 EKAPSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQFN-LAMQVPGKED 420
Cdd:COG1148 135 IKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPGLDC 191
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
373-444 |
2.13e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 48.74 E-value: 2.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQFNLAMQvpgkedfnhtlNYFTNELKRLNVDLQLGTE 444
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIA-----------KILQEKLEKNGIEFLLNTT 62
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
373-407 |
4.29e-07 |
|
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: 52.56 E-value: 4.29e-07
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
373-407 |
6.14e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 52.20 E-value: 6.14e-07
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
138-320 |
6.69e-07 |
|
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: 50.96 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 138 KDFANSAKLAEKAGYDGVEI-MG--SEgylinefMANHTNkrtdnYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSV 214
Cdd:cd02801 67 ETLAEAAKIVEELGADGIDLnMGcpSP-------KVTKGG-----AGAALLKDPELVAEIVRAVREAVPIPVTVKIRLGW 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 215 mdlipngSTPDEVKQQALALEQAGVDIFntgigwhearvpTI----ASMVPAG-AFKEASKRLKETVSVPVIAVNRINTP 289
Cdd:cd02801 135 -------DDEEETLELAKALEDAGASAL------------TVhgrtREQRYSGpADWDYIAEIKEAVSIPVIANGDIFSL 195
|
170 180 190
....*....|....*....|....*....|.
gi 2249646788 290 EIANGILEAGESDLISMARPLLADPEFFNKY 320
Cdd:cd02801 196 EDALRCLEQTGVDGVMIGRGALGNPWLFREI 226
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
373-407 |
1.18e-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: 51.51 E-value: 1.18e-06
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
373-503 |
1.25e-06 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 51.31 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG---------------------QFN---LAMQVPGKEDF------- 421
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGgcthtgtipskalreavlrliGFNqnpLYSSYRVKLRItfadlla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 422 --NHTLN----YFTNELKRLNVDLQLGT-EFTD-NMLN-----------QYDDVVFATGVRP-REAKIECsDGKRVFAYD 481
Cdd:PRK05249 88 raDHVINkqveVRRGQYERNRVDLIQGRaRFVDpHTVEvecpdgevetlTADKIVIATGSRPyRPPDVDF-DHPRIYDSD 166
|
170 180
....*....|....*....|....*
gi 2249646788 482 EVIrgevELGD---KIAILGAGGIG 503
Cdd:PRK05249 167 SIL----SLDHlprSLIIYGAGVIG 187
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
360-506 |
1.38e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 51.31 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 360 LDYSLEKAPSSrlVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQFNLAM---QVPgKEDFNHTLNYFTNELKRLN 436
Cdd:PRK13984 275 LDDEPEKKNKK--VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIpsyRLP-DEALDKDIAFIEALGVKIH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 437 VDLQLGTEFTDNMLNQYDDVVF-ATGVR-PREAKIECSDGKRVF-AYD------EVIRGE---VELGDKIAILGAGGIGF 504
Cdd:PRK13984 352 LNTRVGKDIPLEELREKHDAVFlSTGFTlGRSTRIPGTDHPDVIqALPllreirDYLRGEgpkPKIPRSLVVIGGGNVAM 431
|
..
gi 2249646788 505 DM 506
Cdd:PRK13984 432 DI 433
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
373-511 |
1.46e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 51.08 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIE------------RKEQMGGQFNL-AMQVPGKEDfnHTLNYftneLKRLNVDL 439
Cdd:COG1231 10 VVIVGAGLAGLAAARELRKAGLDVTVLEardrvggrvwtlRFGDDGLYAELgAMRIPPSHT--NLLAL----ARELGLPL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2249646788 440 QlgtEFTDNMlnqYDDVVFATGVRPREAKIECSDGKRVFAYDEVIRgevELGDKIAILGAGGIGFDMVAFLS 511
Cdd:COG1231 84 E---PFPNEN---GNALLYLGGKRVRAGEIAADLRGVAELLAKLLR---ALAAALDPWAHPAAELDRESLAE 146
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
373-408 |
1.74e-06 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 50.95 E-value: 1.74e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER--KEQMGGQ 408
Cdd:COG3573 8 VIVVGAGLAGLVAAAELADAGRRVLLLDQepEANLGGQ 45
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
373-501 |
1.97e-06 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 50.74 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEqmggqfnlamqvpgKEDFNHTLnyftNELKRLNVDLQLGtEFTDNMLNQ 452
Cdd:PRK14106 8 VLVVGAGVSGLALAKFLKKLGAKVILTDEKE--------------EDQLKEAL----EELGELGIELVLG-EYPEEFLEG 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2249646788 453 YDDVVFATGVRPREAKIECSDGKRVfaydEVIrGEVEL------GDKIAILGAGG 501
Cdd:PRK14106 69 VDLVVVSPGVPLDSPPVVQAHKKGI----EVI-GEVELayrfskAPIVAITGTNG 118
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
364-474 |
2.26e-06 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 50.53 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 364 LEKAPSSRLVLVVGAGPAGL--AAScyLAAKGHKVTLIERKEQMggqfnLAMQVP---GKedfnhtlnYFTNELKRLNVD 438
Cdd:COG1251 136 RAALAPGKRVVVIGGGLIGLeaAAA--LRKRGLEVTVVERAPRL-----LPRQLDeeaGA--------LLQRLLEALGVE 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2249646788 439 LQLGT--------------EFTDNMLNQYDDVVFATGVRP-----REAKIECSDG 474
Cdd:COG1251 201 VRLGTgvteiegddrvtgvRLADGEELPADLVVVAIGVRPntelaRAAGLAVDRG 255
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
374-406 |
2.27e-06 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 50.43 E-value: 2.27e-06
10 20 30
....*....|....*....|....*....|...
gi 2249646788 374 LVVGAGPAGLAASCYLAAKGHKVTLIERKEQMG 406
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
373-503 |
2.93e-06 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 50.14 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIErKEQMGG---------------------------QFNLAMQvPGKEDFNHTL 425
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVE-KEKLGGtclnrgcipskallhaaeradearhseDFGIKAE-NVGIDFKKVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 426 NY-----------FTNELKRLNVD-------------LQLGTEFTDNMLnQYDDVVFATGVRPREAK-IEcSDGKRVFAY 480
Cdd:PRK06416 85 EWkngvvnrltggVEGLLKKNKVDiirgeaklvdpntVRVMTEDGEQTY-TAKNIILATGSRPRELPgIE-IDGRVIWTS 162
|
170 180
....*....|....*....|...
gi 2249646788 481 DEVIRGEvELGDKIAILGAGGIG 503
Cdd:PRK06416 163 DEALNLD-EVPKSLVVIGGGYIG 184
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
373-401 |
1.22e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 47.98 E-value: 1.22e-05
10 20
....*....|....*....|....*....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER 401
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLER 33
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
378-406 |
1.25e-05 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 47.27 E-value: 1.25e-05
10 20
....*....|....*....|....*....
gi 2249646788 378 AGPAGLAASCYLAAKGHKVTLIERKEQMG 406
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
373-407 |
2.48e-05 |
|
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: 47.01 E-value: 2.48e-05
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:pfam01266 2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
373-408 |
3.17e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.90 E-value: 3.17e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQ 408
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
373-403 |
7.22e-05 |
|
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: 45.00 E-value: 7.22e-05
10 20 30
....*....|....*....|....*....|.
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKE 403
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKS 33
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
373-408 |
8.71e-05 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 45.53 E-value: 8.71e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIerKEQMGGQ 408
Cdd:PRK15317 214 VLVVGGGPAGAAAAIYAARKGIRTGIV--AERFGGQ 247
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
373-407 |
1.07e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 45.50 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PRK12843 19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
373-405 |
1.12e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 45.28 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|...
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQM 405
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
373-407 |
1.14e-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: 45.21 E-value: 1.14e-04
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
373-525 |
1.35e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.88 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQF------------------NLAMQVPGKEDF-NHTLNYFTNE-- 431
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKIlisgggrcnvtnlseepdNFLSRYPGNPKFlKSALSRFTPWdf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 432 ---LKRLNVDLQLGTE---FTDNM---------LNQYDD--VVFATGVRPREAKIECSDGKRVFAYDEVIRGE---VELG 491
Cdd:pfam03486 83 iafFESLGVPLKEEDHgrlFPDSDkasdivdalLNELKElgVKIRLRTRVLSVEKDDDGRFRVKTGGEELEADslvLATG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2249646788 492 DK-IAILGAGGIGFDmvafLSEHKGQTIE-------QFKTQW 525
Cdd:pfam03486 163 GLsWPKTGSTGFGYP----LAEQFGHTIIplrpalvPFTIDE 200
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
373-407 |
1.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.88 E-value: 1.44e-04
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PRK07208 7 VVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
373-401 |
1.92e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 44.16 E-value: 1.92e-04
10 20
....*....|....*....|....*....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER 401
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
373-408 |
2.03e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 2.03e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERK-EQ-MGGQ 408
Cdd:PRK12834 7 VIVVGAGLAGLVAAAELADAGKRVLLLDQEnEAnLGGQ 44
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
373-511 |
2.11e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.40 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIErKEQMGG---------------------------QFNLAMQVP---GKEDFN 422
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIE-KGPLGGtclnvgcipskaliaaaeafheakhaeEFGIHADGPkidFKKVMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 423 H---TLNYFTN-----ELKRLNVDLQLGT-EFTDN---MLN----QYDDVVFATGVR-PREAKIECSDGKRVFAYDEVIR 485
Cdd:PRK06292 85 RvrrERDRFVGgvvegLEKKPKIDKIKGTaRFVDPntvEVNgeriEAKNIVIATGSRvPPIPGVWLILGDRLLTSDDAFE 164
|
170 180
....*....|....*....|....*.
gi 2249646788 486 GEvELGDKIAILGAGGIGFDMVAFLS 511
Cdd:PRK06292 165 LD-KLPKSLAVIGGGVIGLELGQALS 189
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
433-619 |
2.44e-04 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 43.88 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 433 KRLNV-DLQLGTEFTDNmlnqYDDVVFATGVRPREAKIECSDGKRVFAYDEVIRGEV--ELGDK-----IAILGAGGIGF 504
Cdd:PRK09564 87 KTITVkNLKTGSIFNDT----YDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLAlkELLKDeeiknIVIIGAGFIGL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 505 DMVaflsehkgqtiEQFKTQwgieceaapEKDNRQIYMLKRSAGR-FGSELGKttgwIHRQVAKQHGVKQIAECQYLSFD 583
Cdd:PRK09564 163 EAV-----------EAAKHL---------GKNVRIIQLEDRILPDsFDKEITD----VMEEELRENGVELHLNEFVKSLI 218
|
170 180 190
....*....|....*....|....*....|....*....
gi 2249646788 584 -KQGLK--ITVKGEeqiLDVDTVIACIGQVSNTETFDNQ 619
Cdd:PRK09564 219 gEDKVEgvVTDKGE---YEADVVIVATGVKPNTEFLEDT 254
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
373-490 |
2.80e-04 |
|
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: 43.92 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMggqfnlamqvPGKEDfnhtlnyftnELKRLNVDLQLGtEFTDNMLNQ 452
Cdd:COG0771 7 VLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAP----------ELAAA----------ELEAPGVEVVLG-EHPEELLDG 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2249646788 453 YDDVVFATGVRP--------REAKIecsdgkrvfaydEVIrGEVEL 490
Cdd:COG0771 66 ADLVVKSPGIPPdhpllkaaRAAGI------------PVI-GEIEL 98
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
362-404 |
3.54e-04 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 43.68 E-value: 3.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2249646788 362 YSLEKAPSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQ 404
Cdd:PRK01747 252 FARPGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEA 294
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
369-407 |
3.63e-04 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 43.31 E-value: 3.63e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2249646788 369 SSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
375-407 |
3.81e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 43.27 E-value: 3.81e-04
10 20 30
....*....|....*....|....*....|...
gi 2249646788 375 VVGAGPAGLAASCYLAAKGHKVTLIERKeQMGG 407
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERG-LLGG 41
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
373-407 |
3.90e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.94 E-value: 3.90e-04
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:COG3380 6 IAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
373-406 |
4.72e-04 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 43.10 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMG 406
Cdd:PRK08163 7 VLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
373-407 |
5.33e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 42.07 E-value: 5.33e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2249646788 373 VLVVGAGPAGLAASCYLA-AKGHKVTLIERKEQMGG 407
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAkNRGLKVAIIERSVSPGG 55
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
373-408 |
5.81e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 43.32 E-value: 5.81e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQ 408
Cdd:PLN02976 696 IIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
373-402 |
6.58e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 42.58 E-value: 6.58e-04
10 20 30
....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERK 402
Cdd:PRK07494 10 IAVIGGGPAGLAAAIALARAGASVALVAPE 39
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
373-432 |
7.01e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 42.79 E-value: 7.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQFNLA---MQVPG---------KEDFNHTLNYFTNEL 432
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWSggwMWIPRnplarragiVEDIEQPRTYLRHEL 86
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
136-299 |
7.61e-04 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 41.16 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 136 TIKDFANSAKLAEKAGYDGVEIMGsegylinefmanhtnkrtdNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVfrlsVM 215
Cdd:cd00945 63 TTEVKVAEVEEAIDLGADEIDVVI-------------------NIGSLKEGDWEEVLEEIAAVVEAADGGLPLK----VI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 216 DLIPNGSTPDEVKQQALALEQAGVDIFNTGIGWHearvptiasmvPAGAFKEASKRLKETVS--VPVIAVNRINTPEIAN 293
Cdd:cd00945 120 LETRGLKTADEIAKAARIAAEAGADFIKTSTGFG-----------GGGATVEDVKLMKEAVGgrVGVKAAGGIKTLEDAL 188
|
....*.
gi 2249646788 294 GILEAG 299
Cdd:cd00945 189 AAIEAG 194
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
373-401 |
7.99e-04 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 42.41 E-value: 7.99e-04
10 20
....*....|....*....|....*....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER 401
Cdd:COG2509 33 VVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
138-320 |
9.05e-04 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 41.93 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 138 KDFANSAKLAEKAGYDGVEI-MGSEgylinefmANHTNKRtdNYGGSLENRMRLAVEIVKAVRAKVSQKFIIVFRLSVmd 216
Cdd:pfam01207 66 ALLAEAAKLVEDRGADGIDInMGCP--------SKKVTRG--GGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGW-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 217 lipngstpDEVKQQAL----ALEQAGVDIFNTgigwHeARVPtiASMVPAGAFKEASKRLKETVSVPVIAVNRINTPEIA 292
Cdd:pfam01207 134 --------DDSHENAVeiakIVEDAGAQALTV----H-GRTR--AQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDA 198
|
170 180
....*....|....*....|....*...
gi 2249646788 293 NGILEAGESDLISMARPLLADPEFFNKY 320
Cdd:pfam01207 199 QRCLAYTGADGVMIGRGALGNPWLFAEQ 226
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
345-407 |
9.67e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 42.51 E-value: 9.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2249646788 345 NKRATCLVNPQAAfeldysLEKAPssrlVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PRK12779 291 NERFAGRISPWAA------AVKPP----IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGG 343
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
144-243 |
9.73e-04 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 41.29 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 144 AKLAEKAGYDGVEImgsegylineFMANHTNKRTDNYGGSLENRMRLAVEIVKAVRAKVsqkfiIVFRLSVMDLIPNGST 223
Cdd:cd03174 80 IERALEAGVDEVRI----------FDSASETHSRKNLNKSREEDLENAEEAIEAAKEAG-----LEVEGSLEDAFGCKTD 144
|
90 100
....*....|....*....|
gi 2249646788 224 PDEVKQQALALEQAGVDIFN 243
Cdd:cd03174 145 PEYVLEVAKALEEAGADEIS 164
|
|
| PRK06184 |
PRK06184 |
hypothetical protein; Provisional |
373-404 |
9.88e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235728 [Multi-domain] Cd Length: 502 Bit Score: 42.28 E-value: 9.88e-04
10 20 30
....*....|....*....|....*....|..
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQ 404
Cdd:PRK06184 6 VLIVGAGPTGLTLAIELARRGVSFRLIEKAPE 37
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
373-408 |
1.45e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 41.44 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2249646788 373 VLVVGAGPAGLAAScyLAAK--GHKVTLIERKEQMGGQ 408
Cdd:pfam12831 2 VVVVGGGPAGVAAA--IAAAraGAKVLLVERRGFLGGM 37
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
136-321 |
1.51e-03 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 41.00 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 136 TIKDFANSAKLAEKAGYDGVEImgsegylinefmaN----HTNKRTDNYGGSLEnrmrLAVEIVKAVRAKVSqKFIIVfR 211
Cdd:cd04740 100 TVEEFVEVAEKLADAGADAIEL-------------NiscpNVKGGGMAFGTDPE----AVAEIVKAVKKATD-VPVIV-K 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 212 LSvmdliPNGstpDEVKQQALALEQAGVDIF---NTGIGWH---EARVPtIASMVPAG----AFK----EASKRLKETVS 277
Cdd:cd04740 161 LT-----PNV---TDIVEIARAAEEAGADGLtliNTLKGMAidiETRKP-ILGNVTGGlsgpAIKpialRMVYQVYKAVE 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2249646788 278 VPVIAVNRINTPEIANGILEAGESdLISMARPLLADPEFFNKYV 321
Cdd:cd04740 232 IPIIGVGGIASGEDALEFLMAGAS-AVQVGTANFVDPEAFKEII 274
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
352-408 |
1.52e-03 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 41.75 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 352 VNPQAAFELDYSLEKA--PSSRL-VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQ 408
Cdd:PLN02612 72 VNFLEAAALSASFRSAprPAKPLkVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGK 131
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
367-400 |
1.53e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 41.39 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|....
gi 2249646788 367 APSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIE 400
Cdd:PRK08132 20 DPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLD 53
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
373-505 |
1.65e-03 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 41.85 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG-------QFNLAMQVPGKEdfnhtlnyfTNELKRLNVDLQ----L 441
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGvlqygipSFRLPRDIIDRE---------VQRLVDIGVKIEtnkvI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 442 GTEFT-DNMLNQ--YDDVVFATGV-RPREAKIECSDGKRVFAYDE------VIRGE--------VELGDKIAILGAGGIG 503
Cdd:PRK12775 504 GKTFTvPQLMNDkgFDAVFLGVGAgAPTFLGIPGEFAGQVYSANEfltrvnLMGGDkfpfldtpISLGKSVVVIGAGNTA 583
|
..
gi 2249646788 504 FD 505
Cdd:PRK12775 584 MD 585
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
373-401 |
2.17e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 40.77 E-value: 2.17e-03
10 20
....*....|....*....|....*....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER 401
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
373-403 |
2.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 41.13 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|.
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKE 403
Cdd:PRK06126 10 VLIVGGGPVGLALALDLGRRGVDSILVERKD 40
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
362-477 |
2.54e-03 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 40.84 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 362 YSLEKAPSSrlVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQFNlamqvpgkEDFNHTLnyfTNELKRLNVDLQL 441
Cdd:COG1249 162 LELEELPKS--LVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGED--------PEISEAL---EKALEKEGIDILT 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 442 GTEFT-----DNML------------NQYDDVVFATGVRPR-------EAKIECSDGKRV 477
Cdd:COG1249 229 GAKVTsvektGDGVtvtledgggeeaVEADKVLVATGRRPNtdglgleAAGVELDERGGI 288
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
368-408 |
2.70e-03 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 41.16 E-value: 2.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2249646788 368 PSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQ 408
Cdd:PLN03000 182 SSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGR 222
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
373-401 |
2.81e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 40.55 E-value: 2.81e-03
10 20
....*....|....*....|....*....
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIER 401
Cdd:PRK00711 3 VVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
193-299 |
4.85e-03 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 38.98 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 193 EIVKAVRAKVSQKfiivfrlsVMDLIpngSTPDEvkqqALALEQAGVDIFNTGI-GWhearvpTIASMVPAGAFKEASKR 271
Cdd:PRK01130 109 ELVKRIKEYPGQL--------LMADC---STLEE----GLAAQKLGFDFIGTTLsGY------TEETKKPEEPDFALLKE 167
|
90 100
....*....|....*....|....*...
gi 2249646788 272 LKETVSVPVIAVNRINTPEIANGILEAG 299
Cdd:PRK01130 168 LLKAVGCPVIAEGRINTPEQAKKALELG 195
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
368-478 |
5.29e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 40.12 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 368 PSSRLVLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGGQfnLAMQVPG----KEDFNHTLNYFTNELKRLNVDLQLGT 443
Cdd:PRK12769 325 KSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGL--LTFGIPAfkldKSLLARRREIFSAMGIEFELNCEVGK 402
|
90 100 110
....*....|....*....|....*....|....*..
gi 2249646788 444 EFT-DNMLNQYDDVVFATGV-RPREAKIECSDGKRVF 478
Cdd:PRK12769 403 DISlESLLEDYDAVFVGVGTyRSMKAGLPNEDAPGVY 439
|
|
| NanE |
COG3010 |
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]; |
270-299 |
6.73e-03 |
|
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 442247 Cd Length: 226 Bit Score: 38.55 E-value: 6.73e-03
10 20 30
....*....|....*....|....*....|
gi 2249646788 270 KRLKETVSVPVIAVNRINTPEIANGILEAG 299
Cdd:COG3010 170 KELVAALGVPVIAEGRIHTPEQAAAALELG 199
|
|
| PRK06475 |
PRK06475 |
FAD-binding protein; |
374-405 |
7.67e-03 |
|
FAD-binding protein;
Pssm-ID: 180582 [Multi-domain] Cd Length: 400 Bit Score: 39.04 E-value: 7.67e-03
10 20 30
....*....|....*....|....*....|..
gi 2249646788 374 LVVGAGPAGLAASCYLAAKGHKVTLIERKEQM 405
Cdd:PRK06475 6 LIAGAGVAGLSAALELAARGWAVTIIEKAQEL 37
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
193-299 |
7.81e-03 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 38.33 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 193 EIVKAVRAKVSQkfiivfrlSVMDLIpngSTPDEvkqqALALEQAGVDIFNTGI-GWHEARVptiasmVPAGAFKEASKR 271
Cdd:cd04729 113 ELIKRIHEEYNC--------LLMADI---STLEE----ALNAAKLGFDIIGTTLsGYTEETA------KTEDPDFELLKE 171
|
90 100
....*....|....*....|....*...
gi 2249646788 272 LKETVSVPVIAVNRINTPEIANGILEAG 299
Cdd:cd04729 172 LRKALGIPVIAEGRINSPEQAAKALELG 199
|
|
| PRK06252 |
PRK06252 |
methylcobalamin:coenzyme M methyltransferase; Validated |
195-261 |
8.63e-03 |
|
methylcobalamin:coenzyme M methyltransferase; Validated
Pssm-ID: 235753 Cd Length: 339 Bit Score: 38.71 E-value: 8.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2249646788 195 VKAVRAKVSQKFIIVFRLSVMDLIPNGsTPDEVKQQALALEQAGVDIFNTGIGwhearvptIASMVP 261
Cdd:PRK06252 265 VKTAKENVGDRAALIGNVSTSFTLLNG-TPEKVKAEAKKCLEDGVDILAPGCG--------IAPKTP 322
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
360-477 |
8.94e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 38.96 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2249646788 360 LDYSLEKAPSSRL--VLVVGAGPAG--LAASCYLAAKGH-----------KVTLIERKEQMGGQFNLAMQvpgkedfnht 424
Cdd:COG1252 137 LLAAFERAERRRLltIVVVGGGPTGveLAGELAELLRKLlrypgidpdkvRITLVEAGPRILPGLGEKLS---------- 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2249646788 425 lNYFTNELKRLNVDLQLGT---EFTDNMLN-------QYDDVVFATGVRP----REAKIECSDGKRV 477
Cdd:COG1252 207 -EAAEKELEKRGVEVHTGTrvtEVDADGVTledgeeiPADTVIWAAGVKAppllADLGLPTDRRGRV 272
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
373-407 |
9.94e-03 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 38.90 E-value: 9.94e-03
10 20 30
....*....|....*....|....*....|....*
gi 2249646788 373 VLVVGAGPAGLAASCYLAAKGHKVTLIERKEQMGG 407
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
|
|
| |
