|
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 ... |
6-362 |
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: 538.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHVGLEGLENGLEKLTTFYQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDDSERWA 85
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 86 YLTHAIHKVGGAIALQLFHAGRYAYKDtigqSPVAPSPLKSPINPDTPRALAHEDIEQTIMDFATGALRAKKAGFDAVEI 165
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHP----LCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 166 MGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEVETLQWAQAMEEA 245
Cdd:cd02930 157 MGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 246 GADVLNVGIGWHESQVPTISMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMARPFLADPTLM 325
Cdd:cd02930 237 GADILNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFV 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 2273838322 326 TKAKAGRFTEINTCIACNQACLDHVFEGKTATCLVNP 362
Cdd:cd02930 317 AKAAAGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-366 |
9.83e-155 |
|
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: 450.00 E-value: 9.83e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 1 MNCKALFQPLQIGSLTLKNRVVMGSMHVGLEGlENGL--EKLTTFYQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDD 78
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 79 DDSERWAYLTHAIHKVGGAIALQLFHAGRYAYKD-TIGQSPVAPSPLKSPINPDTPRALAHEDIEQTIMDFATGALRAKK 157
Cdd:COG1902 81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDlPGGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 158 AGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEVETLQ 237
Cdd:COG1902 161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 238 WAQAMEEAGADVLNVGIGWHESQvPTISMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMARP 317
Cdd:COG1902 241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2273838322 318 FLADPTLMTKAKAGRFTEINTCIACNQaCLDHVFegKTATCLVNPEAGR 366
Cdd:COG1902 320 LLADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFY--GGASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
7-331 |
1.36e-131 |
|
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: 389.62 E-value: 1.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 7 FQPLQIGSLTLKNRVVMGSMHVGLEGLENGL-EKLTTFYQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDDSERWA 85
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMATEDGTPtDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 86 YLTHAIHKVGGAIALQLFHAGRYAYKDTIGQSPVAPSPLKSPINPDTPRALAHEDIEQTIMDFATGALRAKKAGFDAVEI 165
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQAQPNLTGGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 166 MGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEVETLQWAQAMEEA 245
Cdd:cd02803 161 HGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 246 GADVLNVGIGWHESQVPTI-SMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMARPFLADPTL 324
Cdd:cd02803 241 GVDALHVSGGSYESPPPIIpPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPDL 320
|
....*..
gi 2273838322 325 MTKAKAG 331
Cdd:cd02803 321 PNKAREG 327
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
6-343 |
4.25e-92 |
|
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: 288.36 E-value: 4.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHVGLEglENGL--EKLTTFYQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDDSER 83
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYA--EDGLpsERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 84 WAYLTHAIHKVGGAIALQLFHAGRYAYKDTIGQSPVAPSPLKSPINPDTPRALAHEDIEQTIMDFATGALRAKKAGFDAV 163
Cdd:cd04734 79 FRRLAEAVHAHGAVIMIQLTHLGRRGDGDGSWLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 164 EIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEVETLQWAQAME 243
Cdd:cd04734 159 ELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 244 EAGA-DVLNVGIG------WHESQVPtiSMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMAR 316
Cdd:cd04734 239 AEGLiDYVNVSAGsyytllGLAHVVP--SMGMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTR 316
|
330 340
....*....|....*....|....*..
gi 2273838322 317 PFLADPTLMTKAKAGRFTEINTCIACN 343
Cdd:cd04734 317 AHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
6-335 |
1.96e-90 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 283.96 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMhVGLEGLENGL---EKLTTFYQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDDSE 82
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 83 RWAYLTHAIHKVGGAIALQLFHAGRYAYKDTIGQ----SPVAPSPLKSPINP-DTPR-ALAHEDIEQTIMDFATGALRAK 156
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREAPMEYRPDlevdGPSDPFALGAQEFEiASPRyEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 157 KAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEVETL 236
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAETA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 237 QWAQAMEEAGADvlnVGIGWHESQVpTISMKVPRMHFLPV------AEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQ 310
Cdd:pfam00724 241 QFIYLLAELGVR---LPDGWHLAYI-HAIEPRPRGAGPVRtrqqhnTLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
|
330 340
....*....|....*....|....*
gi 2273838322 311 LISMARPFLADPTLMTKAKAGRFTE 335
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
6-322 |
1.63e-84 |
|
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: 268.59 E-value: 1.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSM--HVGLEGLenglekLTTF----YQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDD 79
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMcqYSAEDGV------ATDWhlvhYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 80 DSERWAYLTHAIHKVGGAIALQLFHAGRYA-------------YKDTIGQSPVAPSPLKSPINPDTPRALAHEDIEQTIM 146
Cdd:cd02932 75 QIEALKRIVDFIHSQGAKIGIQLAHAGRKAstappwegggpllPPGGGGWQVVAPSAIPFDEGWPTPRELTREEIAEVVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 147 DFATGALRAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLI 226
Cdd:cd02932 155 AFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 227 EGSTTEVETLQWAQAMEEAGADVLNVGIGW-HESQVPtismKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIE 305
Cdd:cd02932 235 EGGWDLEDSVELAKALKELGVDLIDVSSGGnSPAQKI----PVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILE 310
|
330
....*....|....*..
gi 2273838322 306 KGKVQLISMARPFLADP 322
Cdd:cd02932 311 SGRADLVALGRELLRNP 327
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
6-340 |
4.98e-75 |
|
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: 244.04 E-value: 4.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGS-LTLKNRVVMGSM-HVGleGLENGleKLTT----FYQKRAsHDVGLIVTGGAAVNAVGSGGPDFMTIYDDD 79
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVMAPMtTYS--SNPDG--TITDdelaYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 80 DSERWAYLTHAIHKvGGAIA-LQLFHAGRYA-YKDTIGQSPVAPSPLKSPINPD-TPRALAHEDIEQTIMDFATGALRAK 156
Cdd:cd04735 76 DIPGLRKLAQAIKS-KGAKAiLQIFHAGRMAnPALVPGGDVVSPSAIAAFRPGAhTPRELTHEEIEDIIDAFGEATRRAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 157 KAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYP----IFFRMSGLDLIEGSTTE 232
Cdd:cd04735 155 EAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHADkdfiLGYRFSPEEPEEPGIRM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 233 VETLQWAQAMEEAGADVLNVGIGWHESQVPTISMKVPrmhflPVAEKIAEAVS--IPVVASNRINDPRDAAFIIEKGkVQ 310
Cdd:cd04735 235 EDTLALVDKLADKGLDYLHISLWDFDRKSRRGRDDNQ-----TIMELVKERIAgrLPLIAVGSINTPDDALEALETG-AD 308
|
330 340 350
....*....|....*....|....*....|
gi 2273838322 311 LISMARPFLADPTLMTKAKAGRFTEINTCI 340
Cdd:cd04735 309 LVAIGRGLLVDPDWVEKIKEGREDEINLEI 338
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
6-362 |
8.59e-70 |
|
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.
Pssm-ID: 239241 [Multi-domain] Cd Length: 382 Bit Score: 231.63 E-value: 8.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHV-GLEGLENGL-EKLTTFYQKRASHDVGLIVTGGAAVnavgsggpdfmtiydDDDSER 83
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFnQRGIDYYVERAKGGTGLIITGVTMV---------------DNEIEQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 84 WAY-------------------LTHAIHKVGGAIALQLFHA-GRYAYKDTIGQS-PVAPSPLKSPINPD-TPRALAHEDI 141
Cdd:cd02931 66 FPMpslpcptynptafirtakeMTERVHAYGTKIFLQLTAGfGRVCIPGFLGEDkPVAPSPIPNRWLPEiTCRELTTEEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 142 EQTIMDFATGALRAKKAGFDAVEIMG-SEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRM 220
Cdd:cd02931 146 ETFVGKFGESAVIAKEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 221 S--------------GLDLIEGSTTEVETLQWAQAMEEAGADVLNVGIG----WHESQVPtisMKVPRMHFLPVAEKIAE 282
Cdd:cd02931 226 SvksyikdlrqgalpGEEFQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPP---MYQKKGMYLPYCKALKE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 283 AVSIPVVASNRINDPRDAAFIIEKGKVQLISMARPFLADPTLMTKAKAGRFTEINTCIACNQACLDHVFEGKTATCLVNP 362
Cdd:cd02931 303 VVDVPVIMAGRMEDPELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
6-322 |
1.40e-65 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 218.80 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHVGLEGLENGleKLTTF----YQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDDS 81
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDG--KVTNFhlihYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 82 ERWAYLTHAIHKVGGAIALQLFHAGRYAYKDTigqSPVAPSPLKSPINPDTPRALAHEDIEQTIMDFATGALRAKKAGFD 161
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAGRKAELEG---DIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 162 AVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREkVGDHyPIFFRMSGLDLIEGSTTEVETLQWAQA 241
Cdd:PRK13523 158 VIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKE-VWDG-PLFVRISASDYHPGGLTVQDYVQYAKW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 242 MEEAGADVLNVGIGwheSQVPTiSMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMARPFLAD 321
Cdd:PRK13523 236 MKEQGVDLIDVSSG---AVVPA-RIDVYPGYQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRN 311
|
.
gi 2273838322 322 P 322
Cdd:PRK13523 312 P 312
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
5-331 |
7.67e-65 |
|
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: 216.96 E-value: 7.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 5 ALFQPLQIGSLTLKNRVVMGSM---HVGLEGLENGLekLTTFYQKRAShdVGLIVTGGAAVNAVGSGGPDFMTIYDDDDS 81
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrsRADPDGVPTDL--MAEYYAQRAS--AGLIITEATQISPQGQGYPNTPGIYTDEQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 82 ERWAYLTHAIHKVGGAIALQLFHAGRYAYKDTI--GQSPVAPSPL---------KSPINPDTPRALAHEDIEQTIMDFAT 150
Cdd:cd02933 77 EGWKKVTDAVHAKGGKIFLQLWHVGRVSHPSLLpgGAPPVAPSAIaaegkvftpAGKVPYPTPRALTTEEIPGIVADFRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 151 GALRAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAV-----REKVGdhypifFRMS---G 222
Cdd:cd02933 157 AARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVaeaigADRVG------IRLSpfgT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 223 LDLIEGSTTEVETLQWAQAMEEAGADVLNV----GIGWHESQVPTISMKVpRMHFlpvaekiaeavSIPVVASNRInDPR 298
Cdd:cd02933 231 FNDMGDSDPEATFSYLAKELNKRGLAYLHLveprVAGNPEDQPPDFLDFL-RKAF-----------KGPLIAAGGY-DAE 297
|
330 340 350
....*....|....*....|....*....|...
gi 2273838322 299 DAAFIIEKGKVQLISMARPFLADPTLMTKAKAG 331
Cdd:cd02933 298 SAEAALADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
6-336 |
1.74e-61 |
|
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: 208.71 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHVGLEglENGL--EKLTTFYQKRASHDVGLIVTGGAAVNAVGSGG-PDFMTIYDDDDSE 82
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFS--PGGVpgQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGdPNVPRFHGEDALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 83 RWAYLTHAIHKVGGAIALQLFHAG---RYAYKDTIGQSPVAPSPLKSPiNPDTPRALAHEDIEQTIMDFATGALRAKKAG 159
Cdd:cd04747 79 GWKKVVDEVHAAGGKIAPQLWHVGamrKLGTPPFPDVPPLSPSGLVGP-GKPVGREMTEADIDDVIAAFARAAADARRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 160 FDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMS---GLD---LIEGSTTEV 233
Cdd:cd04747 158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSqwkQQDytaRLADTPDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 234 ETlqWAQAMEEAGADVLnvgigwHESQvptismkvpRMHFLPV-----------AEKIAEAVSIPV---------VASNR 293
Cdd:cd04747 238 EA--LLAPLVDAGVDIF------HCST---------RRFWEPEfegselnlagwTKKLTGLPTITVgsvgldgdfIGAFA 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2273838322 294 INDPRDAAFI------IEKGKVQLISMARPFLADPTLMTKAKAGRFTEI 336
Cdd:cd04747 301 GDEGASPASLdrllerLERGEFDLVAVGRALLSDPAWVAKVREGRLDEL 349
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
6-324 |
2.15e-61 |
|
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: 207.82 E-value: 2.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQI-GSLTLKNRVVMGSMHvglEGLENGL----EKLTTFYQKRASHDVGLIVTGGAAVNA---VGSGGPDFMTIYD 77
Cdd:cd04733 1 LGQPLTLpNGATLPNRLAKAAMS---ERLADGRglptPELIRLYRRWAEGGIGLIITGNVMVDPrhlEEPGIIGNVVLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 78 DDDSERWAYLTHAIHKVGGAIALQLFHAGRYAYKDtIGQSPVAPSPLKSPINPD----TPRALAHEDIEQTIMDFATGAL 153
Cdd:cd04733 78 GEDLEAFREWAAAAKANGALIWAQLNHPGRQSPAG-LNQNPVAPSVALDPGGLGklfgKPRAMTEEEIEDVIDRFAHAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 154 RAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIEGSTTEV 233
Cdd:cd04733 157 LAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 234 ETLQWAQAMEEAGADVLNVGIGWHESQVptisMKVPRMH--------FLPVAEKIAEAVSIPVVASNRIndpRDAAFI-- 303
Cdd:cd04733 237 DALEVVEALEEAGVDLVELSGGTYESPA----MAGAKKEstiareayFLEFAEKIRKVTKTPLMVTGGF---RTRAAMeq 309
|
330 340
....*....|....*....|..
gi 2273838322 304 -IEKGKVQLISMARPFLADPTL 324
Cdd:cd04733 310 aLASGAVDGIGLARPLALEPDL 331
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
6-367 |
5.33e-53 |
|
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: 186.02 E-value: 5.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVV-------MGSMHVGLEGLENGLeklttfyqkRASHDVGLIVTGGAAVNAVGSGGP-DFMTIYD 77
Cdd:cd02929 8 LFEPIKIGPVTARNRFYqvphcngMGYRKPSAQAAMRGI---------KAEGGWGVVNTEQCSIHPSSDDTPrISARLWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 78 DDDSERWAYLTHAIHKVGGAIALQLFHAGRYAYKDTIGQSPVAPSPLKS---PINPDTPRALAHEDIEQTIMDFATGALR 154
Cdd:cd02929 79 DGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESRETPLGPSQLPSefpTGGPVQAREMDKDDIKRVRRWYVDAALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 155 AKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLI--EGSTTE 232
Cdd:cd02929 159 ARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIgpGGIESE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 233 VETLQWAQAMEEAgADVLNVGIG-WHESQVPtiSMKVPRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEKGKVQL 311
Cdd:cd02929 239 GEGVEFVEMLDEL-PDLWDVNVGdWANDGED--SRFYPEGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEVVKSGILDL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2273838322 312 ISMARPFLADPTLMTKAKAGRFTEINTCIACNqACLDHVFEGKTATCLVNPEAGRE 367
Cdd:cd02929 316 IGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
5-331 |
7.06e-50 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 185.53 E-value: 7.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 5 ALFQPLQIGSLTLKNRVVMGSMhvGLEGLENGLekLTTF----YQKRASHDVGLIVTGGAAVNAVGSGGPDFMTIYDDDD 80
Cdd:PRK08255 398 PMFTPFRLRGLTLKNRVVVSPM--AMYSAVDGV--PGDFhlvhLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQ 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 81 SERWAYLTHAIHKVGGA-IALQLFHAGRYAYK----DTI------GQSP-VAPSPLK-SPINpDTPRALAHEDIEQTIMD 147
Cdd:PRK08255 474 EAAWKRIVDFVHANSDAkIGIQLGHSGRKGSTrlgwEGIdepleeGNWPlISASPLPyLPGS-QVPREMTRADMDRVRDD 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 148 FATGALRAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYPIFFRMSGLDLIE 227
Cdd:PRK08255 553 FVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVE 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 228 GSTTEVETLQWAQAMEEAGADVLNVGIGwhesQVPTISMKV-PRMHFLPVAEKIAEAVSIPVVASNRINDPRDAAFIIEK 306
Cdd:PRK08255 633 GGNTPDDAVEIARAFKAAGADLIDVSSG----QVSKDEKPVyGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAA 708
|
330 340
....*....|....*....|....*..
gi 2273838322 307 GKVQLISMARPFLADP--TLMTKAKAG 331
Cdd:PRK08255 709 GRADLCALARPHLADPawTLHEAAEIG 735
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
6-206 |
2.17e-40 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 151.42 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMhVGLEGLENG---LEKLTTFYQKRAShdVGLIVTGGAAVNAVGSGGPDFMTIYDDDDSE 82
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMAPL-TRLRSIEPGdipTPLMAEYYRQRAS--AGLIISEATQISAQAKGYAGAPGLHSPEQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 83 RWAYLTHAIHKVGGAIALQLFHAGRYAYKDTI--GQSPVAPSPLKSP--------------INPDTPRALAHEDIEQTIM 146
Cdd:PRK10605 80 AWKKITAGVHAEGGHIAVQLWHTGRISHASLQpgGQAPVAPSAINAGtrtslrdengqairVETSTPRALELEEIPGIVN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 147 DFATGALRAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAV 206
Cdd:PRK10605 160 DFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAG 219
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
6-221 |
1.02e-34 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 136.14 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 6 LFQPLQIGSLTLKNRVVMGSMHV--GLEGLENglEKLTTFYQKRASHDvGLIVTGGAAVNAVGSGGPDFMTIYDDDDSER 83
Cdd:PLN02411 12 LFSPYKMGRFDLSHRVVLAPMTRcrALNGIPN--AALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 84 WAYLTHAIHKVGGAIALQLFHAGRYAYKDtigQSPVAPSPLKS---PIN-------PD-------TPRALAHEDIEQTIM 146
Cdd:PLN02411 89 WKKVVDAVHAKGSIIFCQLWHVGRASHQV---YQPGGAAPISStnkPISerwrilmPDgsygkypKPRALETSEIPEVVE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273838322 147 DFATGALRAKKAGFDAVEIMGSEGYLINQFVSPVTNKRTDQWGGSLKNRLAFPTKIVTAVREKVGDHYpIFFRMS 221
Cdd:PLN02411 166 HYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVRVS 239
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
379-601 |
1.16e-21 |
|
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: 95.85 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYI-GGQLNFAKLIPGKQEFNETLRY-------YKTQLDQL--NVELH 448
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLwadlykrKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 449 LNTHVDSSSP------LLN---------EADDIIIAAGIMPRKPHIKGIDAHSIPSYRDL-----FEERIVPNhHVTIIG 508
Cdd:pfam07992 81 LGTEVVSIDPgakkvvLEElvdgdgetiTYDRLVIATGARPRLPPIPGVELNVGFLVRTLdsaeaLRLKLLPK-RVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 509 GGGIACDLALFLKEKGVEtITLLQRSTKFAKGTGKTTRWATLMELKQADINMIGGISSYDDITDDSITFTIGNKQRTLSH 588
Cdd:pfam07992 160 GGYIGVELAAALAKLGKE-VTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDA 238
|
250
....*....|...
gi 2273838322 589 TMIVLAAGQLPND 601
Cdd:pfam07992 239 DLVVVAIGRRPNT 251
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
378-534 |
3.50e-16 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 80.96 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 378 PKRLLIIGAGPAGLETARVAAKRGHH---VILADEK----------PYIGGQLNFAKLIPGKQEFnetlryyktqLDQLN 444
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDgeiTVIGAEPhppynrpplsKVLAGETDEEDLLLRPADF----------YEENG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 445 VELHLNTHV------------DSSSPLlnEADDIIIAAGIMPRKPHIKGIDAHSIPSYRDL-----FEERIVPNHHVTII 507
Cdd:COG1251 71 IDLRLGTRVtaidraartvtlADGETL--PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLddadaLRAALAPGKRVVVI 148
|
170 180
....*....|....*....|....*..
gi 2273838322 508 GGGGIACDLALFLKEKGVETiTLLQRS 534
Cdd:COG1251 149 GGGLIGLEAAAALRKRGLEV-TVVERA 174
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
381-537 |
6.60e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.01 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILAdEKPYIGGQLNFAKLI---PGKQEF---NETLRYYKTQLDQLNVELHLNT--- 451
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVI-EGGEPGGQLATTKEIenyPGFPEGisgPELAERLREQAERFGAEILLEEvts 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 452 --------HVDSSSPLLNEADDIIIAAGIMPRKPHIKGIDA---HSIpSY---RDLFEeriVPNHHVTIIGGGGIACDLA 517
Cdd:COG0492 82 vdkddgpfRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEfegRGV-SYcatCDGFF---FRGKDVVVVGGGDSALEEA 157
|
170 180
....*....|....*....|
gi 2273838322 518 LFLKEKGVEtITLLQRSTKF 537
Cdd:COG0492 158 LYLTKFASK-VTLIHRRDEL 176
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
374-536 |
1.12e-15 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 78.88 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 374 PASKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGKQEFNETLRYYKTQLDQLNVELHLNTHV 453
Cdd:PRK12770 14 PPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFG--IPEFRIPIERVREGVKELEEAGVVFHTRTKV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 454 DSSSP------------------LLNEADDIIIAAGI-MPRKPHIKGIDA----------HSIPSYR-DLFEERIVPN-- 501
Cdd:PRK12770 92 CCGEPlheeegdefverivsleeLVKKYDAVLIATGTwKSRKLGIPGEDLpgvysaleylFRIRAAKlGYLPWEKVPPve 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2273838322 502 -HHVTIIGGGGIACDLALFLKEKGVETITLLQRSTK 536
Cdd:PRK12770 172 gKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTI 207
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
381-600 |
5.94e-15 |
|
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: 77.43 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILAdEKPYIGG------------------------------------QLNFAKLIP 424
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALV-EKGRLGGtclnvgcipskallhaaevahearhaaefgisagapSVDWAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 425 GKQEFNETLR-YYKTQLDQLNVELH------LNTH---VDSSSPLlnEADDIIIAAGIMPRKPHIKGIDAHSIPSYRDLF 494
Cdd:COG1249 85 RKDKVVDRLRgGVEELLKKNGVDVIrgrarfVDPHtveVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 495 EERIVPNhHVTIIGGGGIACDLALFLKEKGVEtITLLQRSTKFAKGTGKTTRwATLME-LKQADINMIGGiSSYDDITDD 573
Cdd:COG1249 163 ELEELPK-SLVVIGGGYIGLEFAQIFARLGSE-VTLVERGDRLLPGEDPEIS-EALEKaLEKEGIDILTG-AKVTSVEKT 238
|
250 260 270
....*....|....*....|....*....|.
gi 2273838322 574 S----ITFTIGNKQRTLSHTMIVLAAGQLPN 600
Cdd:COG1249 239 GdgvtVTLEDGGGEEAVEADKVLVATGRRPN 269
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
381-600 |
5.70e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 68.26 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKpYIGG-------------------------------------QLNFAKLI 423
Cdd:PRK06116 7 LIVIGGGSGGIASANRAAMYGAKVALIEAK-RLGGtcvnvgcvpkklmwygaqiaeafhdyapgygfdvtenKFDWAKLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 424 PGKQEFNETLR-YYKTQLDQLNVELHlNTH---VDSSSPLLNE----ADDIIIAAGIMPRKPHIKGIDaHSIPSyRDLFE 495
Cdd:PRK06116 86 ANRDAYIDRLHgSYRNGLENNGVDLI-EGFarfVDAHTVEVNGerytADHILIATGGRPSIPDIPGAE-YGITS-DGFFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 496 ERIVPNHhVTIIGGGGIACDLALFLKEKGVETiTLLQRSTKFAKGTGKTTRWATLMELKQADINMIGG--ISSYDDITDD 573
Cdd:PRK06116 163 LEELPKR-VAVVGAGYIAVEFAGVLNGLGSET-HLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNavPKAVEKNADG 240
|
250 260
....*....|....*....|....*..
gi 2273838322 574 SITFTIGNkQRTLSHTMIVLAAGQLPN 600
Cdd:PRK06116 241 SLTLTLED-GETLTVDCLIWAIGREPN 266
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
379-536 |
8.27e-12 |
|
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: 67.47 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPgkqEF---NETLRYYKTQLDQLNVELHLNTHVDS 455
Cdd:COG0493 122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRYG--IP---EFrlpKDVLDREIELIEALGVEFRTNVEVGK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 456 SSP---LLNEADDIIIAAGIM-PRKPHIKGIDAHSI--------PSYRDLFEERIVP-NHHVTIIGGGGIACDLALFLKE 522
Cdd:COG0493 197 DITldeLLEEFDAVFLATGAGkPRDLGIPGEDLKGVhsamdfltAVNLGEAPDTILAvGKRVVVIGGGNTAMDCARTALR 276
|
170
....*....|....
gi 2273838322 523 KGVETITLLQRSTK 536
Cdd:COG0493 277 LGAESVTIVYRRTR 290
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
365-536 |
3.78e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 62.59 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 365 GRETELQMTPASKP--KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGkqefnetLRYYKTQLDQ 442
Cdd:PRK12771 122 AIANGWKFPAPAPDtgKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYG--IPA-------YRLPREVLDA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 443 -------LNVELHLNTHVD---SSSPLLNEADDIIIAAGI-MPRKPHIKGIDAHSIPS----YRDLFEERIVPNH-HVTI 506
Cdd:PRK12771 193 eiqrildLGVEVRLGVRVGediTLEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVLDavdfLRAVGEGEPPFLGkRVVV 272
|
170 180 190
....*....|....*....|....*....|
gi 2273838322 507 IGGGGIACDLALFLKEKGVETITLLQRSTK 536
Cdd:PRK12771 273 IGGGNTAMDAARTARRLGAEEVTIVYRRTR 302
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
366-536 |
5.09e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 62.12 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 366 RETELQMTPASKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPgkqEF---NETLRYYKTQLDQ 442
Cdd:PRK11749 128 TGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLRYG--IP---EFrlpKDIVDREVERLLK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 443 LNVELHLNTHVD---SSSPLLNEADDIIIAAGI-MPRKPHIKGIDAHSI-------------PSYRDLFEERivpnhHVT 505
Cdd:PRK11749 203 LGVEIRTNTEVGrdiTLDELRAGYDAVFIGTGAgLPRFLGIPGENLGGVysavdfltrvnqaVADYDLPVGK-----RVV 277
|
170 180 190
....*....|....*....|....*....|.
gi 2273838322 506 IIGGGGIACDLALFLKEKGVETITLLQRSTK 536
Cdd:PRK11749 278 VIGGGNTAMDAARTAKRLGAESVTIVYRRGR 308
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
378-611 |
1.34e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 60.53 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 378 PKRLLIIGAGPAGLETARVAAKR---GHHVILADEKPYiggqLNFAKLIP----GKQEFNETLRYYKTQLDQLNVELHLN 450
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPY----HLFQPLLPevaaGTLSPDDIAIPLRELLRRAGVRFIQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 451 T-----------HVDSSSPLlnEADDIIIAAGIMPRKPHIKGIDAHSIP------------SYRDLFEERIVPNH-HVTI 506
Cdd:COG1252 77 EvtgidpeartvTLADGRTL--SYDYLVIATGSVTNFFGIPGLAEHALPlktledalalreRLLAAFERAERRRLlTIVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 507 IGGGG----IACDLALFLKEKGVE--------TITLLQRSTKFAKGTGKTTRWATLMELKQADINMIGGiSSYDDITDDS 574
Cdd:COG1252 155 VGGGPtgveLAGELAELLRKLLRYpgidpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTG-TRVTEVDADG 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 2273838322 575 ITFTIGnkqRTLSHTMIVLAAGQLPNDgvFMQKSSLE 611
Cdd:COG1252 234 VTLEDG---EEIPADTVIWAAGVKAPP--LLADLGLP 265
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
430-600 |
2.30e-09 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 59.16 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 430 NETLRYYKTQLDQLNVELHLNTHVDSSSPLLN-----------EADDIIIAAGIM--PRKPHIKGIDAHS--IPSYRDLF 494
Cdd:pfam13738 75 NEYAEYLRRVADHFELPINLFEEVTSVKKEDDgfvvttskgtyQARYVIIATGEFdfPNKLGVPELPKHYsyVKDFHPYA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 495 EERivpnhhVTIIGGGGIACDLALFLKEKGVEtITLLQRSTKFAKGTGKTTRW------ATLMEL-KQADINMIGGiSSY 567
Cdd:pfam13738 155 GQK------VVVIGGYNSAVDAALELVRKGAR-VTVLYRGSEWEDRDSDPSYSlspdtlNRLEELvKNGKIKAHFN-AEV 226
|
170 180 190
....*....|....*....|....*....|....*
gi 2273838322 568 DDITDDSITFTIG--NKQRTLSHTMIVLAAGQLPN 600
Cdd:pfam13738 227 KEITEVDVSYKVHteDGRKVTSNDDPILATGYHPD 261
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
339-536 |
7.33e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.97 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 339 CIA-CNQACLDHVFEGKTATC-LVNPEAGRETEL--QMTPASKP---KRLLIIGAGPAGLETARVAAKRGHHVILADEKP 411
Cdd:PRK12814 147 CPApCEEACRRHGVDEPVSICaLKRYAADRDMESaeRYIPERAPksgKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 412 YIGGQLNFAklIPGKQEFNETLRYYKTQLDQLNVELHLNTHVD---SSSPLLNEADDIIIAAGI-MPRKPHIKGIDAHSI 487
Cdd:PRK12814 227 QAGGMMRYG--IPRFRLPESVIDADIAPLRAMGAEFRFNTVFGrdiTLEELQKEFDAVLLAVGAqKASKMGIPGEELPGV 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2273838322 488 PSYRDLFE-----ERIVPNHHVTIIGGGGIACDLALFLKEKGVETITLLQRSTK 536
Cdd:PRK12814 305 ISGIDFLRnvalgTALHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTR 358
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
136-307 |
1.86e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 54.90 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 136 LAHEDIEQTIMdfaTGALRAKKAGFDAVEIMGSEGYLInqfvspvtnkrtdqwggslknrlAFPTKIVTAVREKVGDHyP 215
Cdd:cd04722 64 LAINDAAAAVD---IAAAAARAAGADGVEIHGAVGYLA-----------------------REDLELIRELREAVPDV-K 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 216 IFFRMSGLDLIEgsttevetlqwAQAMEEAGADVLNVGIGWhesqvPTISMKVPRMHFLPVAEKIAEAVSIPVVASNRIN 295
Cdd:cd04722 117 VVVKLSPTGELA-----------AAAAEEAGVDEVGLGNGG-----GGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180
|
170
....*....|..
gi 2273838322 296 DPRDAAFIIEKG 307
Cdd:cd04722 181 DPEDAAEALALG 192
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
404-600 |
2.58e-08 |
|
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: 55.97 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 404 VILADEKPYIGGQLN-FAKLIPG-KQEFNETLRYYKTQLDQLNVELHLNT------------HVDSSSPLlnEADDIIIA 469
Cdd:COG0446 8 ITVIEKGPHHSYQPCgLPYYVGGgIKDPEDLLVRTPESFERKGIDVRTGTevtaidpeaktvTLRDGETL--SYDKLVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 470 AGIMPRKPHIKGIDAHSIPSYRDL-----FEERI--VPNHHVTIIGGGGIACDLALFLKEKGVEtITLLQRSTK-FAKGT 541
Cdd:COG0446 86 TGARPRPPPIPGLDLPGVFTLRTLddadaLREALkeFKGKRAVVIGGGPIGLELAEALRKRGLK-VTLVERAPRlLGVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273838322 542 GKTTRWAtLMELKQADINMIGG--ISSYDDITDDSITFTIGnkqRTLSHTMIVLAAGQLPN 600
Cdd:COG0446 165 PEMAALL-EEELREHGVELRLGetVVAIDGDDKVAVTLTDG---EEIPADLVVVAPGVRPN 221
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
379-457 |
3.08e-08 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 56.79 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLN-FAKLIPGK---QEFNETLryYKTQLDQLNVELHLNTHVD 454
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPGLdcpQCILEPL--IAEVEANPNITVYTGAEVE 218
|
...
gi 2273838322 455 SSS 457
Cdd:COG1148 219 EVS 221
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
381-541 |
3.54e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 56.34 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYiGG------------------------------------QLNFAKLIP 424
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPL-GGtclnvgcipskaliaaaeafheakhaeefgihadgpKIDFKKVMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 425 GKQEfnETLRYYKTQLDQL--NVELHL---------NTHVDSSSPLLnEADDIIIAAGimPRKPHIKG---IDAHSIPSY 490
Cdd:PRK06292 85 RVRR--ERDRFVGGVVEGLekKPKIDKikgtarfvdPNTVEVNGERI-EAKNIVIATG--SRVPPIPGvwlILGDRLLTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2273838322 491 RDLFEERIVPNHhVTIIGGGGIACDLALFLKEKGVETiTLLQRSTKFAKGT 541
Cdd:PRK06292 160 DDAFELDKLPKS-LAVIGGGVIGLELGQALSRLGVKV-TVFERGDRILPLE 208
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
379-510 |
3.85e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 56.33 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGkqefnetlryYKT----------QLDQLNVELH 448
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRYG--IPD----------FKLekevidrrieLMEAEGIEFR 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273838322 449 LNTHVD---SSSPLLNEADDIIIAAGIM-PRKPHIKGIDA---HS-----IPSYRDLFEERIVP-----NHHVTIIGGG 510
Cdd:PRK12810 212 TNVEVGkdiTAEELLAEYDAVFLGTGAYkPRDLGIPGRDLdgvHFamdflIQNTRRVLGDETEPfisakGKHVVVIGGG 290
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
370-517 |
6.72e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 55.54 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 370 LQMTPASKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGKQEFNETLRYYKTQLDQLNVELHL 449
Cdd:PRK13984 275 LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 450 NTHVDSSSPL--LNEADDII-IAAGI-MPRKPHIKGIDAHSIPSYRDLFEE-----------RIVPNHHVtIIGGGGIAC 514
Cdd:PRK13984 353 NTRVGKDIPLeeLREKHDAVfLSTGFtLGRSTRIPGTDHPDVIQALPLLREirdylrgegpkPKIPRSLV-VIGGGNVAM 431
|
...
gi 2273838322 515 DLA 517
Cdd:PRK13984 432 DIA 434
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
381-537 |
9.31e-08 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 54.17 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLeTARVAAKRGHHVILADEKPYIGGQLNFAKLI---PGkqeFNETLRYY------KTQLDQLNVEL---H 448
Cdd:TIGR01292 2 VIIIGAGPAGL-TAAIYAARANLKPLLIEGMEPGGQLTTTTEVenyPG---FPEGISGPelmekmKEQAVKFGAEIiyeE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 449 LNTHVDSSSPLL--------NEADDIIIAAGIMPRKPHI--------KGIDAHSI---PSYRdlfeerivpNHHVTIIGG 509
Cdd:TIGR01292 78 VIKVDKSDRPFKvytgdgkeYTAKAVIIATGASARKLGIpgedefwgRGVSYCATcdgPFFK---------NKEVAVVGG 148
|
170 180
....*....|....*....|....*...
gi 2273838322 510 GGIACDLALFLKEKGVeTITLLQRSTKF 537
Cdd:TIGR01292 149 GDSAIEEALYLTRIAK-KVTLVHRRDKF 175
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
366-533 |
1.32e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 54.75 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 366 RETELQMTPASKPK---RLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPgkqEF---NETLRYYKTQ 439
Cdd:PRK12778 416 RESGNISVPEVAEKngkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYG--IP---EFrlpKKIVDVEIEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 440 LDQLNVELHLNTHVD---SSSPLLNEA-DDIIIAAGI-MPRKPHIKGIDAHSIPS-------------YRDLFEERIVPN 501
Cdd:PRK12778 491 LKKLGVKFETDVIVGktiTIEELEEEGfKGIFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaASPDSDTPIKFG 570
|
170 180 190
....*....|....*....|....*....|..
gi 2273838322 502 HHVTIIGGGGIACDLALFLKEKGVETITLLQR 533
Cdd:PRK12778 571 KKVAVVGGGNTAMDSARTAKRLGAERVTIVYR 602
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
379-471 |
6.33e-07 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 52.44 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGKQEFNETLRYYKTQLDQLNVELHLNTHVD---S 455
Cdd:PRK12769 328 KRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFG--IPAFKLDKSLLARRREIFSAMGIEFELNCEVGkdiS 405
|
90
....*....|....*.
gi 2273838322 456 SSPLLNEADDIIIAAG 471
Cdd:PRK12769 406 LESLLEDYDAVFVGVG 421
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
371-515 |
7.80e-07 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 52.34 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 371 QMTPasKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAklIPGKQEFNETLRYYKTQLDQLNVELHLN 450
Cdd:PRK12809 305 KVVP--RSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG--IPPFKLDKTVLSQRREIFTAMGIDFHLN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 451 THVDSS---SPLLNEADDIIIAAGIMP-RKPHIKGIDA----HSIP----SYRDL--FEER------IVPNHHVTIIGGG 510
Cdd:PRK12809 381 CEIGRDitfSDLTSEYDAVFIGVGTYGmMRADLPHEDApgviQALPfltaHTRQLmgLPESeeypltDVEGKRVVVLGGG 460
|
....*
gi 2273838322 511 GIACD 515
Cdd:PRK12809 461 DTTMD 465
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
373-534 |
8.51e-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: 51.79 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 373 TPASKPKRLLIIGAGPAGLETARVAAKRGH-HVILaDEKPYIGG-------------------QLNFA------KLIPGK 426
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIdFVVL-EKADDVGGtwrdnrypglrldtpshlySLPFFpnwsddPDFPTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 427 QEFNETLRYYKTQLDqLNVELHLNTHV-----DSSSPLLN---------EADDIIIAAGI--MPRKPHIKGIDAHSIPS- 489
Cdd:COG2072 80 DEILAYLEAYADKFG-LRRPIRFGTEVtsarwDEADGRWTvttddgetlTARFVVVATGPlsRPKIPDIPGLEDFAGEQl 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2273838322 490 ----YRDLFEeriVPNHHVTIIGGGGIACDLALFLKEKGVETiTLLQRS 534
Cdd:COG2072 159 hsadWRNPVD---LAGKRVLVVGTGASAVQIAPELARVAAHV-TVFQRT 203
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
369-536 |
2.20e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 50.40 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 369 ELQMTPASKPKRLLIIGAGPAGLETARVAAKRGHHVIL--ADEKPyiGGQLNFAklIPgkqEF----NETLRYYKTQLDQ 442
Cdd:PRK12831 131 DLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEP--GGVLVYG--IP---EFrlpkETVVKKEIENIKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 443 LNVELHLNTHVDSS---SPLLNEA--DDIIIAAGI-MPRKPHIKGIDAHSIPS-------------YRDLFEERIVPNHH 503
Cdd:PRK12831 204 LGVKIETNVVVGKTvtiDELLEEEgfDAVFIGSGAgLPKFMGIPGENLNGVFSanefltrvnlmkaYKPEYDTPIKVGKK 283
|
170 180 190
....*....|....*....|....*....|...
gi 2273838322 504 VTIIGGGGIACDLALFLKEKGVETITLLQRSTK 536
Cdd:PRK12831 284 VAVVGGGNVAMDAARTALRLGAEVHIVYRRSEE 316
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
377-455 |
2.36e-06 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 49.81 E-value: 2.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273838322 377 KPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIggqlnFAKLIPgkqEFNETLryyKTQLDQLNVELHLNTHVDS 455
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL-----LGVLDP---EMAALL---EEELREHGVELRLGETVVA 190
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
381-600 |
9.64e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 48.84 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILAdEKPYIGGQLNFAKLIPGKQEFN-----ETLR--------------------- 434
Cdd:PTZ00058 51 LIVIGGGSGGMAAARRAARNKAKVALV-EKDYLGGTCVNVGCVPKKIMFNaasihDILEnsrhygfdtqfsfnlpllver 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 435 ----------YYKTQLDQLNVEL------------HLNTHVDSSSPLLNEADD-----------------------IIIA 469
Cdd:PTZ00058 130 rdkyirrlndIYRQNLKKDNVEYfegkgsllsenqVLIKKVSQVDGEADESDDdevtivsagvsqlddgqviegknILIA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 470 AGIMPRKPHIKGIDaHSIPSyRDLFeeRIVPNHHVTIIGGGGIACDLALFLKEKGVETiTLLQRSTKFAKGTGKTTRWAT 549
Cdd:PTZ00058 210 VGNKPIFPDVKGKE-FTISS-DDFF--KIKEAKRIGIAGSGYIAVELINVVNRLGAES-YIFARGNRLLRKFDETIINEL 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2273838322 550 LMELKQADINMI--GGISSYDDITDDSITFTIGNKQRTLSHTMIVLAAGQLPN 600
Cdd:PTZ00058 285 ENDMKKNNINIIthANVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPN 337
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
378-417 |
1.98e-05 |
|
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: 47.52 E-value: 1.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2273838322 378 PKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQL 417
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
503-561 |
2.53e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 42.96 E-value: 2.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2273838322 503 HVTIIGGGGIACDLALFLKEKGVETiTLLQRSTKFAKGTGKTTRWATLMELKQADINMI 561
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKV-TVVERRDRLLPGFDPEIAKILQEKLEKNGIEFL 58
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
147-333 |
2.55e-05 |
|
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: 45.95 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 147 DFATGALRAKKAGFDAVEI-MGSegylinqfvsP---VTNKRtdqwGGS--LKN--RLAfptKIVTAVREKVGdhYPIF- 217
Cdd:cd02801 68 TLAEAAKIVEELGADGIDLnMGC----------PspkVTKGG----AGAalLKDpeLVA---EIVRAVREAVP--IPVTv 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 218 -FRMsgldlieGSTTEVETLQWAQAMEEAGADVLnvgigwhesqvpTISMKVPRMHFLPVA-----EKIAEAVSIPVVAS 291
Cdd:cd02801 129 kIRL-------GWDDEEETLELAKALEDAGASAL------------TVHGRTREQRYSGPAdwdyiAEIKEAVSIPVIAN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2273838322 292 NRINDPRDAAFIIEKGKVQLISMARPFLADPTLMTKAKAGRF 333
Cdd:cd02801 190 GDIFSLEDALRCLEQTGVDGVMIGRGALGNPWLFREIKELLE 231
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
380-415 |
3.81e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 46.42 E-value: 3.81e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2273838322 380 RLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
380-453 |
3.94e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 42.19 E-value: 3.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273838322 380 RLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNfaklipgkqefNETLRYYKTQLDQLNVELHLNTHV 453
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFD-----------PEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
377-484 |
5.96e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 45.39 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 377 KPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQlnfaklipgkqeFNETLR-YYKTQLDQLNVELHLNTHV-- 453
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA------------FDEEISaALEKALEKNGVEVRLGTSVke 218
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2273838322 454 -----DSSSPLLNE-----ADDIIIAAGimpRKPHIKGIDA 484
Cdd:pfam07992 219 iigdgDGVEVILKDgteidADLVVVAIG---RRPNTELLEA 256
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
379-465 |
6.73e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 45.65 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIG--------GQLN----------FAKLIPGKQEFNETLRYYKTQL 440
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRCNvtnlseepdnFLSRYPGNPKFLKSALSRFTPW 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2273838322 441 D------QLNVELHLNTH------VDSSSP----LLNEADD 465
Cdd:pfam03486 81 DfiaffeSLGVPLKEEDHgrlfpdSDKASDivdaLLNELKE 121
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
378-602 |
6.82e-05 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 45.73 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 378 PKRLLIIGAgpAGLETARVAAKRGHHVILADEKPyiggqlNFAKLIPGKQE------------FNET--LRYYKT--QLD 441
Cdd:TIGR01423 58 PKKLMVTGA--QYMDTLRESAGFGWEFDRSSVKA------NWKALIAAKNKavldinksyegmFADTegLTFFLGwgALE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 442 QLNVELhLNTHVDSSSPLLN--EADDIIIAAGIMPRKPHIKGIDaHSIPSYRDLFEERivPNHHVTIIGGGGIACDLA-L 518
Cdd:TIGR01423 130 DKNVVL-VRESADPKSAVKErlQAEHILLATGSWPQMLGIPGIE-HCISSNEAFYLDE--PPRRVLTVGGGFISVEFAgI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 519 FLKEKGV-ETITLLQRSTKFAKGTGKTTRWATLMELKQADINMIG--GISSYDDITDDS--ITFTIGnkqRTLSHTMIVL 593
Cdd:TIGR01423 206 FNAYKPRgGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTneNPAKVTLNADGSkhVTFESG---KTLDVDVVMM 282
|
....*....
gi 2273838322 594 AAGQLPNDG 602
Cdd:TIGR01423 283 AIGRVPRTQ 291
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
383-416 |
6.88e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 41.36 E-value: 6.88e-05
10 20 30
....*....|....*....|....*....|....
gi 2273838322 383 IIGAGPAGLETARVAAKRGHHVILADEKPYIGGQ 416
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
375-415 |
7.68e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 45.65 E-value: 7.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2273838322 375 ASKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:PRK07208 1 MTNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
375-475 |
9.34e-05 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 45.13 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 375 ASKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYI-GGQLnfaklipgkqefNETL-RYYKTQLDQLNVELHLNTH 452
Cdd:COG1251 139 LAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlPRQL------------DEEAgALLQRLLEALGVEVRLGTG 206
|
90 100 110
....*....|....*....|....*....|....*..
gi 2273838322 453 V--------------DSSSPLlnEADDIIIAAGIMPR 475
Cdd:COG1251 207 VteiegddrvtgvrlADGEEL--PADLVVVAIGVRPN 241
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
382-419 |
1.36e-04 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 44.66 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2273838322 382 LIIGAGPAGLETARVAAKRGHHVILADEKPYIG--------GQLNF 419
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGrkilisggGRCNF 46
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
382-419 |
2.87e-04 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 43.74 E-value: 2.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2273838322 382 LIIGAGPAGLETARVAAKRGHHVILADEKPYIG--------GQLNF 419
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGkkllisggGRCNL 46
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
368-482 |
3.51e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 43.58 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 368 TELQMTPAsKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIggqlnFAKLIPGKQEFNetlryyKTQLDQLNVEL 447
Cdd:PRK07251 148 TGIQSLET-LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI-----LPREEPSVAALA------KQYMEEDGITF 215
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2273838322 448 HLNTHVDSSSpllNEADDIIIAAG-----------IMPRKPHIKGI 482
Cdd:PRK07251 216 LLNAHTTEVK---NDGDQVLVVTEdetyrfdallyATGRKPNTEPL 258
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
381-414 |
5.16e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 42.31 E-value: 5.16e-04
10 20 30
....*....|....*....|....*....|....
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIG 414
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
381-417 |
6.65e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 42.60 E-value: 6.65e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQL 417
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
372-415 |
7.74e-04 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 42.54 E-value: 7.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2273838322 372 MTPASKP---KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:PLN02172 1 MAPAQNPinsQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
377-488 |
8.19e-04 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 42.27 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 377 KPKRLLIIGAGPAGLETARVAAKRGHHVILADEKpyiggqlnfaKLIPGKQEFNEtlryyktqLDQLNVELHLNTHVDSS 456
Cdd:PRK14106 4 KGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEK----------EEDQLKEALEE--------LGELGIELVLGEYPEEF 65
|
90 100 110
....*....|....*....|....*....|..
gi 2273838322 457 splLNEADDIIIAAGIMPRKPHIKGIDAHSIP 488
Cdd:PRK14106 66 ---LEGVDLVVVSPGVPLDSPPVVQAHKKGIE 94
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
381-415 |
9.08e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 42.37 E-value: 9.08e-04
10 20 30
....*....|....*....|....*....|....*
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:PRK12842 12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
381-540 |
1.26e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 41.73 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILAdEKPYIGG-------------------------------------QLNFAKLI 423
Cdd:PRK06370 8 AIVIGAGQAGPPLAARAAGLGMKVALI-ERGLLGGtcvntgcvptktliasaraahlarraaeygvsvggpvSVDFKAVM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 424 PGKQEFNETLRY-YKTQLDQL-NVELHL--------NThVDSSSPLLnEADDIIIAAGIMPRKPHIKGIDAHSIPSYRDL 493
Cdd:PRK06370 87 ARKRRIRARSRHgSEQWLRGLeGVDVFRgharfespNT-VRVGGETL-RAKRIFINTGARAAIPPIPGLDEVGYLTNETI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2273838322 494 FEERIVPNHHVtIIGGGGIACDLALFLKEKGVEtITLLQRSTKFAKG 540
Cdd:PRK06370 165 FSLDELPEHLV-IIGGGYIGLEFAQMFRRFGSE-VTVIERGPRLLPR 209
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
376-417 |
1.68e-03 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 41.37 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2273838322 376 SKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQL 417
Cdd:PLN02612 91 AKPLKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKV 132
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
375-412 |
1.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 41.19 E-value: 1.82e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2273838322 375 ASKPKRLLIIGA-GPAGLETARVAAKRGHHVILADEKPY 412
Cdd:PRK06849 1 MNTKKTVLITGArAPAALELARLFHNAGHTVILADSLKY 39
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
380-421 |
2.05e-03 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 40.64 E-value: 2.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2273838322 380 RLLIIGAGPAGLETARVAAKRGHHVILADEKPYiggQLNFAK 421
Cdd:cd08261 162 TVLVVGAGPIGLGVIQVAKARGARVIVVDIDDE---RLEFAR 200
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
144-312 |
2.18e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 40.67 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 144 TIMDFATGALRAKKAGFDAVEImgsegylinqfvspvtnkrtdQWGG--SLKNRLAFPTKIVTAVREKVGDHYPIFFRM- 220
Cdd:cd03316 139 SPEELAEEAKRAVAEGFTAVKL---------------------KVGGpdSGGEDLREDLARVRAVREAVGPDVDLMVDAn 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 221 SGLDLIEGsttevetLQWAQAMEEAgadvlnvGIGWHESQVPtismkvprMHFLPVAEKIAEAVSIPVVASNRINDPRDA 300
Cdd:cd03316 198 GRWDLAEA-------IRLARALEEY-------DLFWFEEPVP--------PDDLEGLARLRQATSVPIAAGENLYTRWEF 255
|
170
....*....|..
gi 2273838322 301 AFIIEKGKVQLI 312
Cdd:cd03316 256 RDLLEAGAVDII 267
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
372-415 |
2.37e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 40.67 E-value: 2.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2273838322 372 MTPASKPKRLLIIGAGPAGLETARVAAKRGHHVIL--ADEKpyIGG 415
Cdd:COG1231 1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVleARDR--VGG 44
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
378-415 |
2.58e-03 |
|
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: 40.61 E-value: 2.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2273838322 378 PKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
380-415 |
2.94e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 40.46 E-value: 2.94e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2273838322 380 RLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
381-420 |
2.96e-03 |
|
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: 40.35 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFA 420
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWS 41
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
386-414 |
4.40e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 39.57 E-value: 4.40e-03
10 20
....*....|....*....|....*....
gi 2273838322 386 AGPAGLETARVAAKRGHHVILADEKPYIG 414
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
379-416 |
5.27e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 40.24 E-value: 5.27e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2273838322 379 KRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQ 416
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
381-415 |
5.54e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 39.70 E-value: 5.54e-03
10 20 30
....*....|....*....|....*....|....*
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIGG 415
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
383-416 |
5.61e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 39.88 E-value: 5.61e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2273838322 383 IIGAGPAGLETARVAAKRGHHVILADEKP--YIGGQ 416
Cdd:PRK12834 9 VVGAGLAGLVAAAELADAGKRVLLLDQENeaNLGGQ 44
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
376-425 |
6.52e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 39.76 E-value: 6.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2273838322 376 SKPKRLLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGqlNFAKLIPG 425
Cdd:PTZ00306 407 SLPARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG--NSAKATSG 454
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
201-333 |
8.44e-03 |
|
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: 38.85 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 201 KIVTAVREKVGDHYPIFFRMsGLDLiegstTEVETLQWAQAMEEAGADVLnvgigwhesqvpTISMKVPRMHFLPVAE-- 278
Cdd:pfam01207 112 QIVKAVVKAVGIPVTVKIRI-GWDD-----SHENAVEIAKIVEDAGAQAL------------TVHGRTRAQNYEGTADwd 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273838322 279 ---KIAEAVSIPVVASNRINDPRDAAFIIEKGKVQLISMARPFLADPTL---MTKAKAGRF 333
Cdd:pfam01207 174 aikQVKQAVSIPVIANGDITDPEDAQRCLAYTGADGVMIGRGALGNPWLfaeQHTVKTGEF 234
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
380-409 |
8.67e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 39.07 E-value: 8.67e-03
10 20 30
....*....|....*....|....*....|
gi 2273838322 380 RLLIIGAGPAGLETARVAAKRGHHVILADE 409
Cdd:PRK07845 3 RIVIIGGGPGGYEAALVAAQLGADVTVIER 32
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
381-517 |
8.79e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 38.98 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 381 LLIIGAGPAGLETARVAAKRGHHVILADEKPYIGGQLNFAKLIPGKqefneTLRYYKTQLDQLNV-ELHLNTHV--DSSS 457
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSK-----ALREAVLRLIGFNQnPLYSSYRVklRITF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273838322 458 PLLNEADDIIIAAGIMPRK--------PHIKG----IDAHSI---------------------------PSYRDLFEERI 498
Cdd:PRK05249 83 ADLLARADHVINKQVEVRRgqyernrvDLIQGrarfVDPHTVevecpdgevetltadkiviatgsrpyrPPDVDFDHPRI 162
|
170 180 190
....*....|....*....|....*....|
gi 2273838322 499 -----------VPnHHVTIIGGGGIACDLA 517
Cdd:PRK05249 163 ydsdsilsldhLP-RSLIIYGAGVIGCEYA 191
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
382-416 |
9.36e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 39.01 E-value: 9.36e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2273838322 382 LIIGAGPAGLETARVAAKRGHHVILADEKP--YIGGQ 416
Cdd:COG3573 9 IVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGGQ 45
|
|
| |
