|
Name |
Accession |
Description |
Interval |
E-value |
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
8-360 |
0e+00 |
|
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.
Pssm-ID: 239240 [Multi-domain] Cd Length: 353 Bit Score: 674.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHK 87
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 88 IVTQAVHEAGGKICMQILHAGRYAYSPKSVAPSAIQAPINPFKPRELDEEGIEKQIADFVNCSSLAQVAGYDGVEIMGSE 167
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 168 GYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWDEIVLLAKAIEKAGATI 247
Cdd:cd02930 161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 248 INTGIGWHEARIPTIATKVPRAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMVSMARPFLADPDFVNKAA 327
Cdd:cd02930 241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 1837635526 328 EGRADEINTCIGCNQACLDHTFGGKLTSCLVNP 360
Cdd:cd02930 321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
3-364 |
7.39e-172 |
|
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: 495.07 E-value: 7.39e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 3 ATYPHLLAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTP 80
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 81 EEAEKHKIVTQAVHEAGGKICMQILHAGRYAYSPKS-----VAPSAIQAPINPFKPRELDEEGIEKQIADFVNCSSLAQV 155
Cdd:COG1902 81 EQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPggwppVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 156 AGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWDEIVL 235
Cdd:COG1902 161 AGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 236 LAKAIEKAGATIINTGIGWHEARiPTIATKVPRAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMVSMARP 315
Cdd:COG1902 241 LAKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1837635526 316 FLADPDFVNKAAEGRADEINTCIGCNQaCLDHTFGGklTSCLVNPRACH 364
Cdd:COG1902 320 LLADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
9-329 |
1.37e-120 |
|
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: 362.27 E-value: 1.37e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 9 LAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKH 86
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMAT-EDGTptDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 87 KIVTQAVHEAGGKICMQILHAGRYAYSP----KSVAPSAIQAPINPFKPRELDEEGIEKQIADFVNCSSLAQVAGYDGVE 162
Cdd:cd02803 80 RKLTEAVHAHGAKIFAQLAHAGRQAQPNltggPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 163 IMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWDEIVLLAKAIEK 242
Cdd:cd02803 160 IHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 243 AGATIINTGIGWHEARIPTIA-TKVPRAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMVSMARPFLADPD 321
Cdd:cd02803 240 AGVDALHVSGGSYESPPPIIPpPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPD 319
|
....*...
gi 1837635526 322 FVNKAAEG 329
Cdd:cd02803 320 LPNKAREG 327
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
8-333 |
1.22e-99 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 309.00 E-value: 1.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMhTGLEEKPQGF---ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 84
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 85 KHKIVTQAVHEAGGKICMQILHAGRYAYS-----PKSVAPS---AIQAPINP-FKPR-ELDEEGIEKQIADFVNCSSLAQ 154
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREAPMeyrpdLEVDGPSdpfALGAQEFEiASPRyEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 155 VAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWDEIv 234
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 235 llAKAIEKAGATIINTGIGWHEARIpTIATKVPRAAFTKVT------AKLRGEIGIPLVTTNRINTPEVAEQVLAEGDAD 308
Cdd:pfam00724 240 --AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTrqqhntLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
|
330 340
....*....|....*....|....*
gi 1837635526 309 MVSMARPFLADPDFVNKAAEGRADE 333
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
8-341 |
6.46e-86 |
|
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: 273.33 E-value: 6.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHK 87
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 88 IVTQAVHEAGGKICMQILHAGRYAYSPKS----VAPSAIQAPINPFKPRELDEEGIEKQIADFVNCSSLAQVAGYDGVEI 163
Cdd:cd04734 81 RLAEAVHAHGAVIMIQLTHLGRRGDGDGSwlppLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 164 MGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWDEIVLLAKAIEKA 243
Cdd:cd04734 161 QAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 244 GAT-IINTGIG------WHEARIPTIAtkVPRAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMVSMARPF 316
Cdd:cd04734 241 GLIdYVNVSAGsyytllGLAHVVPSMG--MPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAH 318
|
330 340
....*....|....*....|....*
gi 1837635526 317 LADPDFVNKAAEGRADEINTCIGCN 341
Cdd:cd04734 319 IADPHLVAKAREGREDDIRPCIGCN 343
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
8-328 |
9.15e-73 |
|
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: 238.55 E-value: 9.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEE 82
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMcqysaEDGV---ATDWHLV--HYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 83 AEKHKIVTQAVHEAGGKICMQILHAGRYA--YSP---------------KSVAPSAIQAPINPFKPRELDEEGIEKQIAD 145
Cdd:cd02932 76 IEALKRIVDFIHSQGAKIGIQLAHAGRKAstAPPwegggpllppggggwQVVAPSAIPFDEGWPTPRELTREEIAEVVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 146 FVNCSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVE 225
Cdd:cd02932 156 FVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 226 GGSTWDEIVLLAKAIEKAGATIINTGIG--WHEARIPT-IATKVPRAaftkvtAKLRGEIGIPLVTTNRINTPEVAEQVL 302
Cdd:cd02932 236 GGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIPVgPGYQVPFA------ERIRQEAGIPVIAVGLITDPEQAEAIL 309
|
330 340
....*....|....*....|....*.
gi 1837635526 303 AEGDADMVSMARPFLADPDFVNKAAE 328
Cdd:cd02932 310 ESGRADLVALGRELLRNPYWPLHAAA 335
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
7-329 |
5.44e-67 |
|
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: 223.12 E-value: 5.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 7 HLLAPLDLGFTTLRNRTLMGSM---HTGLEEKPQgfERMAAYFAERArgGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA 83
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrsRADPDGVPT--DLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 84 EKHKIVTQAVHEAGGKICMQILHAGRYA---YSP---KSVAPSAIQAPINPFK---------PRELDEEGIEKQIADFVN 148
Cdd:cd02933 77 EGWKKVTDAVHAKGGKIFLQLWHVGRVShpsLLPggaPPVAPSAIAAEGKVFTpagkvpyptPRALTTEEIPGIVADFRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 149 CSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIyRLSMLDLVEGGS 228
Cdd:cd02933 157 AARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADRVGI-RLSPFGTFNDMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 229 TWDEIVL---LAKAIEKAgatiintGIGW-H--EARIPTIATKVPRAAFtkvtAKLRGEIGIPLVTTNRInTPEVAEQVL 302
Cdd:cd02933 236 DSDPEATfsyLAKELNKR-------GLAYlHlvEPRVAGNPEDQPPDFL----DFLRKAFKGPLIAAGGY-DAESAEAAL 303
|
330 340
....*....|....*....|....*..
gi 1837635526 303 AEGDADMVSMARPFLADPDFVNKAAEG 329
Cdd:cd02933 304 ADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
8-360 |
4.20e-64 |
|
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: 216.99 E-value: 4.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMHT-GLEEKPQGF-ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYsGAAKLSTPEEAEK 85
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFnQRGIDYYVERAKGGTGLIITGVTMVDNEIEQF-PMPSLPCPTYNPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 86 H-----KIVTQAVHEAGGKICMQILHA-GRYA---YSP--KSVAPSAIQAPINPFKP-RELDEEGIEKQIADFVNCSSLA 153
Cdd:cd02931 80 AfirtaKEMTERVHAYGTKIFLQLTAGfGRVCipgFLGedKPVAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 154 QVAGYDGVEIMG-SEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLS----MLDL----- 223
Cdd:cd02931 160 KEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksyIKDLrqgal 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 224 -----VEGGSTWDEIVLLAKAIEKAGATIINTGIG----WHEARIPTIATKvprAAFTKVTAKLRGEIGIPLVTTNRINT 294
Cdd:cd02931 240 pgeefQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQKK---GMYLPYCKALKEVVDVPVIMAGRMED 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1837635526 295 PEVAEQVLAEGDADMVSMARPFLADPDFVNKAAEGRADEINTCIGCNQACLDHTFGGKLTSCLVNP 360
Cdd:cd02931 317 PELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
18-338 |
1.74e-61 |
|
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: 208.99 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 18 TLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERArGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHKIVTQAVHE 95
Cdd:cd04735 12 TLKNRFVMAPMTTYSSN-PDGTitDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 96 AGGKICMQILHAGRYAYS-----PKSVAPSAIQAPiNPFK--PRELDEEGIEKQIADFVNCSSLAQVAGYDGVEIMGSEG 168
Cdd:cd04735 90 KGAKAILQIFHAGRMANPalvpgGDVVSPSAIAAF-RPGAhtPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 169 YFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVG----PNFIIIYRLSMLDLVEGGSTWDEIVLLAKAIEKAG 244
Cdd:cd04735 169 YLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDkhadKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 245 ATIINTGIGWHEARIPTIATKVPRAAfTKVTAKLRGEigIPLVTTNRINTPEVAEQVLAEGdADMVSMARPFLADPDFVN 324
Cdd:cd04735 249 LDYLHISLWDFDRKSRRGRDDNQTIM-ELVKERIAGR--LPLIAVGSINTPDDALEALETG-ADLVAIGRGLLVDPDWVE 324
|
330
....*....|....
gi 1837635526 325 KAAEGRADEINTCI 338
Cdd:cd04735 325 KIKEGREDEINLEI 338
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
8-325 |
1.35e-59 |
|
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: 203.59 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGF-TTLRNRTLMGSMHTGLEEKPQ--GFERMAAYfaER-ARGGVGLMVTGGI-----GPNEEGGVYSGAakLS 78
Cdd:cd04733 1 LGQPLTLPNgATLPNRLAKAAMSERLADGRGlpTPELIRLY--RRwAEGGIGLIITGNVmvdprHLEEPGIIGNVV--LE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 79 TPEEAEKHKIVTQAVHEAGGKICMQILHAGRYAY---SPKSVAPSAIQAPINPF----KPRELDEEGIEKQIADFVNCSS 151
Cdd:cd04733 77 SGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPaglNQNPVAPSVALDPGGLGklfgKPRAMTEEEIEDVIDRFAHAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 152 LAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSTWD 231
Cdd:cd04733 157 LAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 232 EIVLLAKAIEKAGATIINTGIGWHEAriPTIATKVP-----RAA-FTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEG 305
Cdd:cd04733 237 DALEVVEALEEAGVDLVELSGGTYES--PAMAGAKKestiaREAyFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASG 314
|
330 340
....*....|....*....|
gi 1837635526 306 DADMVSMARPFLADPDFVNK 325
Cdd:cd04733 315 AVDGIGLARPLALEPDLPNK 334
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
8-334 |
6.54e-51 |
|
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: 180.59 E-value: 6.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMhtGLEEKPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA-E 84
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPM--TRSFSPGGVpgQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVPRFHGEDAlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 85 KHKIVTQAVHEAGGKICMQILHAG--RYAYSP-----KSVAPSAIQAPINPFKpRELDEEGIEKQIADFVNCSSLAQVAG 157
Cdd:cd04747 79 GWKKVVDEVHAAGGKIAPQLWHVGamRKLGTPpfpdvPPLSPSGLVGPGKPVG-REMTEADIDDVIAAFARAAADARRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 158 YDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGS----TWDEI 233
Cdd:cd04747 158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTArladTPDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 234 VLLAKAIEKAGATIIN----------------TGIGWheAR----IPTIAT------KVPRAAFTkvtaklrgeiGIPLV 287
Cdd:cd04747 238 EALLAPLVDAGVDIFHcstrrfwepefegselNLAGW--TKkltgLPTITVgsvgldGDFIGAFA----------GDEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1837635526 288 TTNRINtpEVAEQvLAEGDADMVSMARPFLADPDFVNKAAEGRADEI 334
Cdd:cd04747 306 SPASLD--RLLER-LERGEFDLVAVGRALLSDPAWVAKVREGRLDEL 349
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
6-328 |
8.18e-44 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 168.58 E-value: 8.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 6 PHLLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTP 80
Cdd:PRK08255 397 PPMFTPFRLRGLTLKNRVVVSPMamysaVDGV---PGDFHLV--HLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYND 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 81 EEAEKHKIVTQAVH-EAGGKICMQILHAGRYAySPK----------------SVAPSAIQAPINPFKPRELDEEGIEKQI 143
Cdd:PRK08255 472 EQEAAWKRIVDFVHaNSDAKIGIQLGHSGRKG-STRlgwegidepleegnwpLISASPLPYLPGSQVPREMTRADMDRVR 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 144 ADFVNCSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDL 223
Cdd:PRK08255 551 DDFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDW 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 224 VEGGSTWDEIVLLAKAIEKAGATIIN--TGIGWHEARiPTIAtkvpRAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQV 301
Cdd:PRK08255 631 VEGGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYG----RMYQTPFADRIRNEAGIATIAVGAISEADHVNSI 705
|
330 340
....*....|....*....|....*...
gi 1837635526 302 LAEGDADMVSMARPFLADPDF-VNKAAE 328
Cdd:PRK08255 706 IAAGRADLCALARPHLADPAWtLHEAAE 733
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
8-334 |
2.09e-43 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 159.48 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFER---MAAYFAeRARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 84
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTnfhLIHYGT-RAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 85 KHKIVTQAVHEAGGKICMQILHAGRYAYSP-KSVAPSAIQAPINPFKPRELDEEGIEKQIADFVNCSSLAQVAGYDGVEI 163
Cdd:PRK13523 82 GLHKLVTFIHDHGAKAAIQLAHAGRKAELEgDIVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 164 MGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREA-VGPNFIiiyRLSMLDLVEGGSTWDEIVLLAKAIEK 242
Cdd:PRK13523 162 HGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVwDGPLFV---RISASDYHPGGLTVQDYVQYAKWMKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 243 AGATIINTGIG-WHEARIPTI-ATKVPRAaftkvtAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMVSMARPFLADP 320
Cdd:PRK13523 239 QGVDLIDVSSGaVVPARIDVYpGYQVPFA------EHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNP 312
|
330
....*....|....
gi 1837635526 321 DFVNKAAEGRADEI 334
Cdd:PRK13523 313 YFPRIAAKELGFEI 326
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
1-365 |
4.94e-42 |
|
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: 156.36 E-value: 4.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 1 MTATYPHLLAPLDLGFTTLRNR-------TLMGSMHTGLeekpqgferMAAYFAERARGGVGLMVTG--GIGPNEEGGVY 71
Cdd:cd02929 1 RDPRHDILFEPIKIGPVTARNRfyqvphcNGMGYRKPSA---------QAAMRGIKAEGGWGVVNTEqcSIHPSSDDTPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 72 SgAAKLSTPEEAEKHKIVTQAVHEAGGKICMQILHAGRYAYSPKS----VAPSAIQ---APINPFKPRELDEEGIEKQIA 144
Cdd:cd02929 72 I-SARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESretpLGPSQLPsefPTGGPVQAREMDKDDIKRVRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 145 DFVNCSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLV 224
Cdd:cd02929 151 WYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 225 --EGGSTWDEIVllaKAIEKAGATI----INTG--IGWHE-ARIPTIATKVPRAAFTK-VTAKlrgeigiPLVTTNRINT 294
Cdd:cd02929 231 gpGGIESEGEGV---EFVEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEPYIKFVKqVTSK-------PVVGVGRFTS 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1837635526 295 PEVAEQVLAEGDADMVSMARPFLADPDFVNKAAEGRADEINTCIGCNqACLDHTFGGKLTSCLVNPRACHE 365
Cdd:cd02929 301 PDKMVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
8-325 |
3.10e-38 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 145.64 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 8 LLAPLDLGFTTLRNRTLM-----------GSMHTGLeekpqgferMAAYFAERArgGVGLMVTGG--IGPNEEGgvYSGA 74
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMapltrlrsiepGDIPTPL---------MAEYYRQRA--SAGLIISEAtqISAQAKG--YAGA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 75 AKLSTPEEAEKHKIVTQAVHEAGGKICMQILHAGRYAYSP------KSVAPSAIQAP--------------INPFKPREL 134
Cdd:PRK10605 70 PGLHSPEQIAAWKKITAGVHAEGGHIAVQLWHTGRISHASlqpggqAPVAPSAINAGtrtslrdengqairVETSTPRAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 135 DEEGIEKQIADFVNCSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFII 214
Cdd:PRK10605 150 ELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRIG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 215 IyRLSML---DLVEGGSTWDEIVL-LAKAIEKagatiinTGIGWHEARIPTIATKVP-RAAFTKvtaKLRGEIGIPLVTT 289
Cdd:PRK10605 230 I-RISPLgtfNNVDNGPNEEADALyLIEQLGK-------RGIAYLHMSEPDWAGGEPySDAFRE---KVRARFHGVIIGA 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 1837635526 290 NRInTPEVAEQVLAEGDADMVSMARPFLADPDFVNK 325
Cdd:PRK10605 299 GAY-TAEKAETLIGKGLIDAVAFGRDYIANPDLVAR 333
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
6-323 |
6.63e-31 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 124.97 E-value: 6.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 6 PHLLAPLDLGFTTLRNRTLMGSMHT--GLEEKPQgfERMAAYFAERARGGvGLMVTGG--IGPNEEG-----GVYSGaak 76
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRcrALNGIPN--AALAEYYAQRSTPG-GFLISEGtlISPTAPGfphvpGIYSD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 77 lstpEEAEKHKIVTQAVHEAGGKICMQILHAGR---YAYSPKSVAP-SAIQAPIN---------------PfKPRELDEE 137
Cdd:PLN02411 84 ----EQVEAWKKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISerwrilmpdgsygkyP-KPRALETS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 138 GIEKQIADFVNCSSLAQVAGYDGVEIMGSEGYFINQFLAAHTNHRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 217
Cdd:PLN02411 159 EIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADRVGVRV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 218 LSMLDLVEGGSTwDEIVLLAKAIEKAGATIINTGigwheARIPTIATKVPRAAFTKVTAKLR---GEIGIPLVTTNRIN- 293
Cdd:PLN02411 239 SPAIDHLDATDS-DPLNLGLAVVERLNKLQLQNG-----SKLAYLHVTQPRYTAYGQTESGRhgsEEEEAQLMRTLRRAy 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1837635526 294 ----------TPEVAEQVLAEGDADMVSMARPFLADPDFV 323
Cdd:PLN02411 313 qgtfmcsggfTRELGMQAVQQGDADLVSYGRLFISNPDLV 352
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
377-508 |
3.64e-20 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 93.71 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG-------QFNVAKRVPGKEEfyetlryfkRKVETTGVDLRLNT 449
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllrygipEFRLPKDIVDREV---------ERLLKLGVEIRTNT 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1837635526 450 RV----SVDDLvKGGFDEIILATGI-VPRTPAIPGIENAKV---ISYLDAI-----LERKPVGRTAAVIGAG 508
Cdd:PRK11749 212 EVgrdiTLDEL-RAGYDAVFIGTGAgLPRFLGIPGENLGGVysaVDFLTRVnqavaDYDLPVGKRVVVIGGG 282
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
377-677 |
5.35e-20 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 94.17 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG--QFNV-AKRVPgkeefYETLRYFKRKVETTGVDLRLNTRVSV 453
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRYGIpAYRLP-----REVLDAEIQRILDLGVEVRLGVRVGE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 454 D---DLVKGGFDEIILATGI-VPRTPAIPGIENAKVIS---YLDAI--LERKPVGRTAAVIGAGGIGFDVSEYITHAGES 524
Cdd:PRK12771 213 DitlEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVLDavdFLRAVgeGEPPFLGKRVVVIGGGNTAMDAARTARRLGAE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 525 TSL--------DRHAFWQEwgIDENLEarggiAGIQAHPHAAARQVfllqrkkskVGDGLGkttgwihRTGLKNKQVQMl 596
Cdd:PRK12771 293 EVTivyrrtreDMPAHDEE--IEEALR-----EGVEINWLRTPVEI---------EGDENG-------ATGLRVITVEK- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 597 nsveylKVDNDGLHISIAGGEPQVLPVDTVVVCAGQD----PLRELH-----DGLVAAGQSV-------HLIGGADVAAE 660
Cdd:PRK12771 349 ------MELDEDGRPSPVTGEEETLEADLVVLAIGQDidsaGLESVPgvevgRGVVQVDPNFmmtgrpgVFAGGDMVPGP 422
|
330
....*....|....*..
gi 1837635526 661 LDAKRAINQGSRLAAEI 677
Cdd:PRK12771 423 RTVTTAIGHGKKAARNI 439
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
377-634 |
5.71e-20 |
|
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: 90.84 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEI-GGQFNVAKRVPGKEEFYETLRYF-------KRKVETTGVDLRLN 448
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWadlykrkEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 449 TRVSVDDLVKG-----------------GFDEIILATGIVPRTPAIPGIE--NAKVISYLDA--ILERKPVGRTAAVIGA 507
Cdd:pfam07992 81 LGTEVVSIDPGakkvvleelvdgdgetiTYDRLVIATGARPRLPPIPGVElnVGFLVRTLDSaeALRLKLLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 508 GGIGFDVSEYITHAGESTSLdrhafwqewgidenLEARGgiagiqahphaaarqvFLLQRKKSKVGDGLGKTtgwihrtg 587
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTL--------------IEALD----------------RLLRAFDEEISAALEKA-------- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1837635526 588 LKNKQVQMLNSVEYLKVDNDGLHISIAGGEPQVLPVDTVVVCAGQDP 634
Cdd:pfam07992 203 LEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRP 249
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
377-514 |
2.42e-19 |
|
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: 90.96 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGqfnvakrvpgkeefyeTLRY----FK----------RKVETTG 442
Cdd:COG0493 122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG----------------LLRYgipeFRlpkdvldreiELIEALG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 443 VDLRLNTRV----SVDDLvKGGFDEIILATGI-VPRTPAIPGIENAKVIS---YL------DAILERKPVGRTAAVIGAG 508
Cdd:COG0493 186 VEFRTNVEVgkdiTLDEL-LEEFDAVFLATGAgKPRDLGIPGEDLKGVHSamdFLtavnlgEAPDTILAVGKRVVVIGGG 264
|
....*.
gi 1837635526 509 GIGFDV 514
Cdd:COG0493 265 NTAMDC 270
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
377-479 |
3.58e-16 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 81.75 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGqfnvakrvpgkeefyeTLRY----FK-------RKVET---TG 442
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG----------------LLRYgipdFKlekevidRRIELmeaEG 207
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1837635526 443 VDLRLNTRV----SVDDLVKgGFDEIILATGI-VPRTPAIPG 479
Cdd:PRK12810 208 IEFRTNVEVgkdiTAEELLA-EYDAVFLGTGAyKPRDLGIPG 248
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
378-524 |
4.11e-15 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 76.70 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGaGEIGGQFNVAKRV---PGKEEF---YETLRYFKRKVETTGVDLRLNTRV 451
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEIenyPGFPEGisgPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 452 SVdDLVKGGF------------DEIILATGIVPRTPAIPGIENAKV--ISY---LDAILERkpvGRTAAVIGAGGIGFDV 514
Cdd:COG0492 81 SV-DKDDGPFrvttddgteyeaKAVIIATGAGPRKLGLPGEEEFEGrgVSYcatCDGFFFR---GKDVVVVGGGDSALEE 156
|
170
....*....|
gi 1837635526 515 SEYITHAGES 524
Cdd:COG0492 157 ALYLTKFASK 166
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
377-515 |
2.03e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 76.73 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFNVAkrVPGKEEFYETLRYFKRKVETTGVDLRLNTRVSVD-- 454
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDip 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1837635526 455 -DLVKGGFDEIILATGI-VPRTPAIPGIENAKVISYLDAILE----------RKPVGRTAAVIGAGGIGFDVS 515
Cdd:PRK13984 362 lEELREKHDAVFLSTGFtLGRSTRIPGTDHPDVIQALPLLREirdylrgegpKPKIPRSLVVIGGGNVAMDIA 434
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
377-513 |
1.88e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 73.62 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG-------QFNVAKRVPGKEefYETLRYFKRKVETtgvDLRLNT 449
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGvlkygipEFRLPKKIVDVE--IENLKKLGVKFET---DVIVGK 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1837635526 450 RVSVDDLVKGGFDEIILATGI-VPRTPAIPGiENAKVISYLDAILER------------KPV--GRTAAVIGAGGIGFD 513
Cdd:PRK12778 507 TITIEELEEEGFKGIFIASGAgLPNFMNIPG-ENSNGVMSSNEYLTRvnlmdaaspdsdTPIkfGKKVAVVGGGNTAMD 584
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
377-516 |
2.06e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 71.94 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ--FNVAK-RVPgkeefYETLRYFKRKVETTGVDLRLNTRV-- 451
Cdd:PRK12770 19 KKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLmlFGIPEfRIP-----IERVREGVKELEEAGVVFHTRTKVcc 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 452 -----------------SVDDLVKgGFDEIILATGI-VPRTPAIPGIENAKVISYLDAIL------------ERKP--VG 499
Cdd:PRK12770 94 geplheeegdefverivSLEELVK-KYDAVLIATGTwKSRKLGIPGEDLPGVYSALEYLFriraaklgylpwEKVPpvEG 172
|
170
....*....|....*..
gi 1837635526 500 RTAAVIGAGGIGFDVSE 516
Cdd:PRK12770 173 KKVVVVGAGLTAVDAAL 189
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
377-511 |
2.58e-13 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 72.10 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGH--EVTLFDGAGE-----------IGGQFNVAKRVPGKEEFYETLryfkrkvettGV 443
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPdgEITVIGAEPHppynrpplskvLAGETDEEDLLLRPADFYEEN----------GI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 444 DLRLNTRV-SVD------DLVKG---GFDEIILATGIVPRTPAIPGIENAKVISY-----LDAILERKPVGRTAAVIGAG 508
Cdd:COG1251 72 DLRLGTRVtAIDraartvTLADGetlPYDKLVLATGSRPRVPPIPGADLPGVFTLrtlddADALRAALAPGKRVVVIGGG 151
|
...
gi 1837635526 509 GIG 511
Cdd:COG1251 152 LIG 154
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
401-634 |
7.51e-13 |
|
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: 69.84 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 401 EVTLFDGAGEIGGQ-----FNVAKRVPGKEE-FYETLRYFKRKvettGVDLRLNTRV-SVDD-----LVKGG----FDEI 464
Cdd:COG0446 7 EITVIEKGPHHSYQpcglpYYVGGGIKDPEDlLVRTPESFERK----GIDVRTGTEVtAIDPeaktvTLRDGetlsYDKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 465 ILATGIVPRTPAIPGIENAKV-----ISYLDAILE--RKPVGRTAAVIGAGGIGFDVSEYITHAGESTSLdrhafwqewg 537
Cdd:COG0446 83 VLATGARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTL---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 538 idenlearggiagIQAHPHaaarqvfLLQRKKSKVGDGLGKTtgwihrtgLKNKQVQMLNSVEYLKVD-NDGLHISIAGG 616
Cdd:COG0446 153 -------------VERAPR-------LLGVLDPEMAALLEEE--------LREHGVELRLGETVVAIDgDDKVAVTLTDG 204
|
250
....*....|....*...
gi 1837635526 617 EpqVLPVDTVVVCAGQDP 634
Cdd:COG0446 205 E--EIPADLVVVAPGVRP 220
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
377-513 |
7.01e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 68.12 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG-------QFNVAKRVPGKEEFyetlryfkRKVETTGVDLRLNT 449
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlvygipEFRLPKETVVKKEI--------ENIKKLGVKIETNV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 450 ----RVSVDDLVK-GGFDEIILATGI-VPRTPAIPGiENAKVISYLDAILER-------KP-------VGRTAAVIGAGG 509
Cdd:PRK12831 213 vvgkTVTIDELLEeEGFDAVFIGSGAgLPKFMGIPG-ENLNGVFSANEFLTRvnlmkayKPeydtpikVGKKVAVVGGGN 291
|
....
gi 1837635526 510 IGFD 513
Cdd:PRK12831 292 VAMD 295
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
372-574 |
4.27e-11 |
|
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: 65.27 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 372 PTTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG----------QFNVAKRV--------PGKEEFY----E 429
Cdd:COG2072 2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglRLDTPSHLyslpffpnWSDDPDFptgdE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 430 TLRYFKRKVETTGV--DLRLNTRV-SVD-DLVKGGF------------DEIILATGI--VPRTPAIPGIENAKVISYL-- 489
Cdd:COG2072 82 ILAYLEAYADKFGLrrPIRFGTEVtSARwDEADGRWtvttddgetltaRFVVVATGPlsRPKIPDIPGLEDFAGEQLHsa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 490 ----DAILERKPVgrtaAVIGAGGIGFDVSEYITHAGEST---------SLDRHAFWQEWGidenleaRGGIAGIQAHPH 556
Cdd:COG2072 162 dwrnPVDLAGKRV----LVVGTGASAVQIAPELARVAAHVtvfqrtppwVLPRPNYDPERG-------RPANYLGLEAPP 230
|
250 260
....*....|....*....|.
gi 1837635526 557 AAARQV---FLLQRKKSKVGD 574
Cdd:COG2072 231 ALNRRDaraWLRRLLRAQVKD 251
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
377-513 |
1.27e-10 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 64.75 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG--QFNVAK-RVPGK--EEFYETLRyfkrkveTTGVDLRLNTR- 450
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGmmRYGIPRfRLPESviDADIAPLR-------AMGAEFRFNTVf 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1837635526 451 ---VSVDDLvKGGFDEIILATGI-VPRTPAIPGIENAKVISYLD-----AILERKPVGRTAAVIGAGGIGFD 513
Cdd:PRK12814 267 grdITLEEL-QKEFDAVLLAVGAqKASKMGIPGEELPGVISGIDflrnvALGTALHPGKKVVVIGGGNTAID 337
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
379-511 |
2.15e-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: 63.18 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDgAGEIGG------------------QFNVAKRVP------GKEEF-YETLRY 433
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGGtclnvgcipskallhaaeVAHEARHAAefgisaGAPSVdWAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 434 FKRKV------------ETTGVDL-----RL--NTRVSVDDLVKGGFDEIILATGIVPRTPAIPGIENAKVISYlDAILE 494
Cdd:COG1249 85 RKDKVvdrlrggveellKKNGVDVirgraRFvdPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTS-DEALE 163
|
170
....*....|....*..
gi 1837635526 495 RKPVGRTAAVIGAGGIG 511
Cdd:COG1249 164 LEELPKSLVVIGGGYIG 180
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
378-413 |
3.40e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 59.52 E-value: 3.40e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
143-314 |
4.58e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 53.74 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 143 IADFVNCSSLAQVAGYDGVEIMGSEGYfinqflaahtnhrtdrwggsyenRMRLPVEIVRRVREAVgPNFIIIYRLSMLD 222
Cdd:cd04722 70 AAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAV-PDVKVVVKLSPTG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 223 lveggstwdeiVLLAKAIEKAGATIINTGIGWHEARIPTIATKVPRaaftkVTAKLRGEIGIPLVTTNRINTPEVAEQVL 302
Cdd:cd04722 126 -----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADL-----LLILAKRGSKVPVIAGGGINDPEDAAEAL 189
|
170
....*....|..
gi 1837635526 303 AEGdADMVSMAR 314
Cdd:cd04722 190 ALG-ADGVIVGS 200
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
361-472 |
4.96e-08 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 56.02 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 361 RACHETELNYIPTTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFN-VAKRVPGKEEFYETLRYFKRKVE 439
Cdd:COG1148 125 KAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAqLHKTFPGLDCPQCILEPLIAEVE 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1837635526 440 TT-GVDLRLNTRV-SVD--------DLVKGGFDE-------IILATGIVP 472
Cdd:COG1148 205 ANpNITVYTGAEVeEVSgyvgnftvTIKKGPREEieievgaIVLATGFKP 254
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
377-413 |
8.30e-08 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 55.22 E-value: 8.30e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
377-413 |
1.00e-07 |
|
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: 1.00e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
370-474 |
1.22e-07 |
|
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: 54.05 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 370 YIPTTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFNvakrvpgkeefYETLRYFKRKVETTGVDLRLNT 449
Cdd:COG0446 118 ALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLD-----------PEMAALLEEELREHGVELRLGE 186
|
90 100 110
....*....|....*....|....*....|....*.
gi 1837635526 450 RV-SVDD-------LVKGG---FDEIILATGIVPRT 474
Cdd:COG0446 187 TVvAIDGddkvavtLTDGEeipADLVVVAPGVRPNT 222
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
377-412 |
1.75e-07 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 54.12 E-value: 1.75e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIG 412
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
377-413 |
2.54e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 53.70 E-value: 2.54e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
380-469 |
2.70e-07 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 53.52 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 380 AVVGAGPAGLSAATVAAERGHEVTLFDGAGEIG--------GQFNV---------AKRVPGKEEF----------YETLR 432
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVGrkilisggGRCNFtnseplpefLNYYGGNPHFlksalsrftpEDLIA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1837635526 433 YFKR-----KVETTG------------------------VDLRLNTRVSVDDLVKGGF------------DEIILATG 469
Cdd:COG2081 81 FFEGlgietKEESSGrvfpdsskasdilrallaelreagVEIRLRTRVTGIEKEDGGFgvetpdgetvraDAVVLATG 158
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
377-413 |
3.73e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 52.57 E-value: 3.73e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
378-513 |
7.47e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 52.64 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG-------QFNVAKRVPGKEefYETLRYFKRKVETTGVdlrLNTR 450
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGvlqygipSFRLPRDIIDRE--VQRLVDIGVKIETNKV---IGKT 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 451 VSVDDLVKG-GFDEIILATGI-VPRTPAIPGIENAKVIS-----------------YLDAILErkpVGRTAAVIGAGGIG 511
Cdd:PRK12775 507 FTVPQLMNDkGFDAVFLGVGAgAPTFLGIPGEFAGQVYSanefltrvnlmggdkfpFLDTPIS---LGKSVVVIGAGNTA 583
|
..
gi 1837635526 512 FD 513
Cdd:PRK12775 584 MD 585
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
381-414 |
8.05e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 46.76 E-value: 8.05e-07
10 20 30
....*....|....*....|....*....|....
gi 1837635526 381 VVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ 414
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
367-485 |
1.84e-06 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 50.86 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 367 ELNYIPtthvKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFN--VAKRVpgkeefyetLRYFKRKvettGVD 444
Cdd:COG1249 163 ELEELP----KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDpeISEAL---------EKALEKE----GID 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1837635526 445 LRLNTRV---------------SVDDLVKGGFDEIILATGIVPRTPAIpGIENAKV 485
Cdd:COG1249 226 ILTGAKVtsvektgdgvtvtleDGGGEEAVEADKVLVATGRRPNTDGL-GLEAAGV 280
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
379-511 |
2.04e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 50.56 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDGaGEIGGqfNVAKR--VPGK-----EEFYETLRYFKR---KVETTGVDLRL- 447
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGG--TCLNVgcIPSKaliaaAEAFHEAKHAEEfgiHADGPKIDFKKv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 448 --NTRVSVDDLVKG---------------G------------------FDEIILATGivPRTPAIPGIENA--KVISYLD 490
Cdd:PRK06292 83 maRVRRERDRFVGGvveglekkpkidkikGtarfvdpntvevngerieAKNIVIATG--SRVPPIPGVWLIlgDRLLTSD 160
|
170 180
....*....|....*....|.
gi 1837635526 491 AILERKPVGRTAAVIGAGGIG 511
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIG 181
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
378-451 |
2.76e-06 |
|
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: 45.66 E-value: 2.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFNVakrvpgkeefyETLRYFKRKVETTGVDLRLNTRV 451
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDP-----------EIAKILQEKLEKNGIEFLLNTTV 63
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
375-474 |
3.04e-06 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 50.14 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 375 HVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGA--------GEIGGQFnvakrvpgkeefyetlryFKRKVETTGVDLR 446
Cdd:COG1251 141 PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAprllprqlDEEAGAL------------------LQRLLEALGVEVR 202
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1837635526 447 LNTRVS---VDDLVKG-----G----FDEIILATGIVPRT 474
Cdd:COG1251 203 LGTGVTeieGDDRVTGvrladGeelpADLVVVAIGVRPNT 242
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
373-562 |
3.08e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 50.30 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 373 TTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG--------QFNV-----AKRVPGK--------EEFYETL 431
Cdd:COG1231 4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGrvwtlrfgDDGLyaelgAMRIPPShtnllalaRELGLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 432 RYFKRKVETTGVDLRlNTRVSVDDLV--KGGFDEII------LATGIVPRTPAIPGIENAKVISYLDAILERKPVGRTAA 503
Cdd:COG1231 84 EPFPNENGNALLYLG-GKRVRAGEIAadLRGVAELLakllraLAAALDPWAHPAAELDRESLAEWLRRNGASPSARRLLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1837635526 504 VIGAGGIGFDVSEYITHAgestsLDRHAFWQEWGiDENLEARGGIAGIqahPHAAARQV 562
Cdd:COG1231 163 LLGAGEYGADPDELSLLD-----LLRYAASAGGG-AQQFRIVGGMDQL---PRALAAEL 212
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
373-469 |
4.42e-06 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 50.02 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 373 TTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFNVAkrVPGKEEFYETLRYFKRKVETTGVDLRLNTRVS 452
Cdd:PRK12809 307 VPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG--IPPFKLDKTVLSQRREIFTAMGIDFHLNCEIG 384
|
90 100
....*....|....*....|.
gi 1837635526 453 VD----DLVKgGFDEIILATG 469
Cdd:PRK12809 385 RDitfsDLTS-EYDAVFIGVG 404
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
379-516 |
5.66e-06 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 49.34 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFdGAGEIGGQ-FNV-----------------AKRVP-----------------G 423
Cdd:TIGR02053 3 LVIIGSGAAAFAAAIKAAELGASVAMV-ERGPLGGTcVNVgcvpskmllraaevahyARKPPfgglaatvavdfgelleG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 424 KEEFYETLRYFKRK--VETTGVDLRLNTRVSVDD---LVKGG-----FDEIILATGIVPRTPAIPGIENAKVISYLDAiL 493
Cdd:TIGR02053 82 KREVVEELRHEKYEdvLSSYGVDYLRGRARFKDPktvKVDLGrevrgAKRFLIATGARPAIPPIPGLKEAGYLTSEEA-L 160
|
170 180
....*....|....*....|...
gi 1837635526 494 ERKPVGRTAAVIGAGGIGFDVSE 516
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQ 183
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
377-527 |
1.10e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 48.50 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAA--ERGHEVTLFD-------GAGE----IGGQF----NVAKRVPgkEEFYETLRYFKRKVE 439
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKrlNKELEITVYEktdivsfGACGlpyfVGGFFddpnTMIARTP--EEFIKSGIDVKTEHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 440 TTGVDlRLNTRVSVDDLVKG-----GFDEIILATGIVPRTPAIPGIeNAKVISYL----DAI----LERKPVGRTAAVIG 506
Cdd:PRK09564 79 VVKVD-AKNKTITVKNLKTGsifndTYDKLMIATGARPIIPPIKNI-NLENVYTLksmeDGLalkeLLKDEEIKNIVIIG 156
|
170 180
....*....|....*....|.
gi 1837635526 507 AGGIGFDVSEYITHAGESTSL 527
Cdd:PRK09564 157 AGFIGLEAVEAAKHLGKNVRI 177
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
377-413 |
1.91e-05 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 47.42 E-value: 1.91e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERgHEVTLFDGAGEIGG 413
Cdd:COG2907 4 MRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
374-413 |
2.37e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.19 E-value: 2.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1837635526 374 THVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:PRK07208 2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
377-454 |
2.63e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 47.43 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG-------QFNVAKRVPGKeefyetlryfKRKVETT-GVDLRLN 448
Cdd:PRK12769 328 KRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGlltfgipAFKLDKSLLAR----------RREIFSAmGIEFELN 397
|
....*.
gi 1837635526 449 TRVSVD 454
Cdd:PRK12769 398 CEVGKD 403
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
367-485 |
3.62e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 46.71 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 367 ELNYIPtthvKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQF-----NVAKRVPGKEeFYetlryFKRKVETT 441
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEdpevsKQAQKILSKE-FK-----IKLGAKVT 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1837635526 442 GVDLRLNTRVSVDDlvKGG------FDEIILATGIVPRTPAIpGIENAKV 485
Cdd:PRK06292 234 SVEKSGDEKVEELE--KGGktetieADYVLVATGRRPNTDGL-GLENTGI 280
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
378-414 |
3.90e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 46.72 E-value: 3.90e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ 414
Cdd:PLN02487 77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGK 113
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
381-511 |
5.39e-05 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 46.29 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 381 VVGAGPAGLSAATVAAERGHEVTLFDgAGEIGGQ-FNVAKrVPGKE-----EFYETLRY--------------------F 434
Cdd:PRK06416 9 VIGAGPGGYVAAIRAAQLGLKVAIVE-KEKLGGTcLNRGC-IPSKAllhaaERADEARHsedfgikaenvgidfkkvqeW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 435 KRKVETT------------GVDL-----RL--NTRVSVDDLVKGG---FDEIILATGIVPRTpaIPGIE-NAKVISYLDA 491
Cdd:PRK06416 87 KNGVVNRltggvegllkknKVDIirgeaKLvdPNTVRVMTEDGEQtytAKNIILATGSRPRE--LPGIEiDGRVIWTSDE 164
|
170 180
....*....|....*....|
gi 1837635526 492 ILERKPVGRTAAVIGAGGIG 511
Cdd:PRK06416 165 ALNLDEVPKSLVVIGGGYIG 184
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
377-474 |
6.67e-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: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQFN--VAKRVpgkeefyetLRYFKRKvettGVDLRLNTRV--- 451
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDeeISAAL---------EKALEKN----GVEVRLGTSVkei 219
|
90 100 110
....*....|....*....|....*....|..
gi 1837635526 452 ---SVDDLVKGG------FDEIILATGIVPRT 474
Cdd:pfam07992 220 igdGDGVEVILKdgteidADLVVVAIGRRPNT 251
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
378-445 |
8.70e-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: 45.08 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIG--------GQFNVAKRVPGKEEFY----ETLRYFKRKVETTGVDL 445
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSELArlalEALDLWEELEEELGIDC 80
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
378-445 |
1.24e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 44.90 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDgAGEIG--------GQFNVAKRVPGKEEFY----ETLRYFKRKVETTGVDL 445
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGsgasgrnaGQLRPGLAALADRALVrlarEALDLWRELAAELGIDC 82
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
461-531 |
1.50e-04 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 45.20 E-value: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1837635526 461 FDEIILATGIVPRTPAIPGIENAKVISY-----LDAILERKPVGRTAAVIGAGGIGFDVSEYITHAGESTSLDRHA 531
Cdd:TIGR02374 97 YDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHA 172
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
378-412 |
2.34e-04 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 43.77 E-value: 2.34e-04
10 20 30
....*....|....*....|....*....|....*
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIG 412
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
377-414 |
2.84e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 44.47 E-value: 2.84e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ 414
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
373-482 |
3.45e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 43.58 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 373 TTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIggqfnvakrVPGKEEFYETLRyfKRKVETTGVDLRLNTRVS 452
Cdd:PRK07251 154 ETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI---------LPREEPSVAALA--KQYMEEDGITFLLNAHTT 222
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1837635526 453 V-----DDLV------KGGFDEIILATGIVPRTPAIpGIEN 482
Cdd:PRK07251 223 EvkndgDQVLvvtedeTYRFDALLYATGRKPNTEPL-GLEN 262
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
384-412 |
3.77e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 43.03 E-value: 3.77e-04
10 20
....*....|....*....|....*....
gi 1837635526 384 AGPAGLSAATVAAERGHEVTLFDGAGEIG 412
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
379-414 |
3.81e-04 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 43.43 E-value: 3.81e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ 414
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
379-414 |
5.99e-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: 5.99e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGQ 414
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
381-511 |
6.89e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 42.50 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 381 VVGAGPAGLSAATVAAERGHEVTLFdGAGEIGGQ------------------FNVAKR-------VPGKEEF-YETLRYF 434
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALI-ERGLLGGTcvntgcvptktliasaraAHLARRaaeygvsVGGPVSVdFKAVMAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 435 KRKV-------------ETTGVDLRLNT-------RVSVDDlVKGGFDEIILATGIVPRTPAIPGIENakvISYL--DAI 492
Cdd:PRK06370 89 KRRIrarsrhgseqwlrGLEGVDVFRGHarfespnTVRVGG-ETLRAKRIFINTGARAAIPPIPGLDE---VGYLtnETI 164
|
170
....*....|....*....
gi 1837635526 493 LERKPVGRTAAVIGAGGIG 511
Cdd:PRK06370 165 FSLDELPEHLVIIGGGYIG 183
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
376-413 |
8.41e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 42.54 E-value: 8.41e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1837635526 376 VKKIAVVGAGPAGLSAATVAAERGHEVTLFDGAGeIGG 413
Cdd:PRK07845 1 MTRIVIIGGGPGGYEAALVAAQLGADVTVIERDG-LGG 37
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
378-411 |
9.28e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 41.98 E-value: 9.28e-04
10 20 30
....*....|....*....|....*....|....
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEI 411
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
379-479 |
1.09e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 42.51 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG--QFNVAK-RVPGK--EEFYETLRYFKRKVETTGVdlrLNTRVSV 453
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGvlRYGIPEfRLPNQliDDVVEKIKLLGGRFVKNFV---VGKTATL 385
|
90 100
....*....|....*....|....*..
gi 1837635526 454 DDLVKGGFDEIILATGI-VPRTPAIPG 479
Cdd:PRK12779 386 EDLKAAGFWKIFVGTGAgLPTFMNVPG 412
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
377-406 |
1.47e-03 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 41.44 E-value: 1.47e-03
10 20 30
....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVD 30
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
381-414 |
1.59e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 41.70 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1837635526 381 VVGAGPAGLSAATVAAERGHEVTLFD--GAGEIGGQ 414
Cdd:COG3573 10 VVGAGLAGLVAAAELADAGRRVLLLDqePEANLGGQ 45
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
185-310 |
1.86e-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: 41.06 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 185 RWGGSYENR--MRLPVEIVRRVREAVGPNFIIiyrlsmldLVEGGSTWD--EIVLLAKAIEKAgatiintGIGWHEARIP 260
Cdd:cd03316 161 KVGGPDSGGedLREDLARVRAVREAVGPDVDL--------MVDANGRWDlaEAIRLARALEEY-------DLFWFEEPVP 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1837635526 261 tiatkvprAAFTKVTAKLRGEIGIPLVTTNRINTPEVAEQVLAEGDADMV 310
Cdd:cd03316 226 --------PDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDII 267
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
377-406 |
2.41e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 40.78 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQVTVFD 31
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
378-472 |
2.52e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 40.89 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGH-------------EVTLFDGAGEIGGQFN--VAKRVpgkeefyetLRYFKRKvettG 442
Cdd:COG1252 151 TIVVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRILPGLGekLSEAA---------EKELEKR----G 217
|
90 100 110
....*....|....*....|....*....|....*...
gi 1837635526 443 VDLRLNTRV-SVDD---LVKGG----FDEIILATGIVP 472
Cdd:COG1252 218 VEVHTGTRVtEVDAdgvTLEDGeeipADTVIWAAGVKA 255
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
376-406 |
2.91e-03 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 40.09 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|.
gi 1837635526 376 VKKIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:COG1250 2 IKKVAVIGAGTMGAGIAAVFANAGYEVVLLD 32
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
379-414 |
3.23e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 40.65 E-value: 3.23e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDGAGE--IGGQ 414
Cdd:PRK12834 7 VIVVGAGLAGLVAAAELADAGKRVLLLDQENEanLGGQ 44
|
|
| sdhA |
PRK08641 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
377-405 |
3.43e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236319 [Multi-domain] Cd Length: 589 Bit Score: 40.73 E-value: 3.43e-03
10 20
....*....|....*....|....*....
gi 1837635526 377 KKIAVVGAGPAGLSAATVAAERGHEVTLF 405
Cdd:PRK08641 4 GKVIVVGGGLAGLMATIKAAEAGVHVDLF 32
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
379-562 |
5.16e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 40.13 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 379 IAVVGAGPAGLSAATVAAERGHEVTLFDgAGEIGGQ-FNVAKrVPGK--------------------------------- 424
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIE-RGTIGGTcVNVGC-VPSKimiraahiahlrrespfdggiaatvptidrsrl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837635526 425 ----EEFYETLRYFKRK--VETT-------GVDLRLNTRVSVDDLVKGG-----FDEIILATGIVPRTPAIPGIENAKVI 486
Cdd:PRK13748 179 laqqQARVDELRHAKYEgiLDGNpaitvlhGEARFKDDQTLIVRLNDGGervvaFDRCLIATGASPAVPPIPGLKETPYW 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1837635526 487 SYLDAiLERKPVGRTAAVIGAGGIGFDVSEYITHAG-ESTSLDRHA--FWQEWGIDENLEARGGIAGIQAHPHAAARQV 562
Cdd:PRK13748 259 TSTEA-LVSDTIPERLAVIGSSVVALELAQAFARLGsKVTILARSTlfFREDPAIGEAVTAAFRAEGIEVLEHTQASQV 336
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
378-406 |
5.95e-03 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 39.26 E-value: 5.95e-03
10 20
....*....|....*....|....*....
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWD 32
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
381-413 |
6.59e-03 |
|
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: 39.43 E-value: 6.59e-03
10 20 30
....*....|....*....|....*....|...
gi 1837635526 381 VVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:COG1053 8 VVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
378-443 |
6.69e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 39.76 E-value: 6.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGGqfNVAK----------RVPGKEEFYETLRYFKRKVETTGV 443
Cdd:PTZ00306 411 RVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG--NSAKatsgingwgtRAQAKQDVLDGGKFFERDTHLSGK 484
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
378-406 |
7.07e-03 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 37.90 E-value: 7.07e-03
10 20
....*....|....*....|....*....
gi 1837635526 378 KIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVD 29
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
369-413 |
7.37e-03 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 39.46 E-value: 7.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1837635526 369 NYIPTTHVkkiAVVGAGPAGLSAATVAAERGHEVTLFDGAGEIGG 413
Cdd:PLN02172 6 NPINSQHV---AVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
372-406 |
9.17e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 39.08 E-value: 9.17e-03
10 20 30
....*....|....*....|....*....|....*
gi 1837635526 372 PTTHVKKIAVVGAGPAGLSAATVAAERGHEVTLFD 406
Cdd:PRK08132 19 DDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLD 53
|
|
| |
