|
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 ... |
10-362 |
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: 671.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSMHTGLEELDDGIDRLAAFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 90 IVTQAVHEAGGKICMQILHAGRYAYSPKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSE 169
Cdd:cd02930 81 LITDAVHAEGGKIALQILHAGRYAYHPLCVAPSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVEIMGSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 170 GYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAGATL 249
Cdd:cd02930 161 GYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVALAKALEAAGADI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 250 INTGIGWHEARIPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPDFVNKAA 329
Cdd:cd02930 241 LNTGIGWHEARVPTIATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGDADMVSMARPFLADPDFVAKAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 15598288 330 AGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02930 321 AGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
6-366 |
2.15e-170 |
|
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: 491.22 E-value: 2.15e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 6 PYPHLLAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPE 83
Cdd:COG1902 3 KMPKLFSPLTLGGLTLKNRIVMAPMTRGRAD-EDGVptDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 84 EAEKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ-----VAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVA 158
Cdd:COG1902 82 QIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPggwppVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 159 GYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLL 238
Cdd:COG1902 162 GFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 239 AKAVEKAGATLINTGIGWHEARiPTIATKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPF 318
Cdd:COG1902 242 AKALEEAGVDYLHVSSGGYEPD-AMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVALGRPL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15598288 319 LADPDFVNKAAAGHAERINTCIGCNQaCLDHTFGGklTSCLVNPRACH 366
Cdd:COG1902 321 LADPDLPNKAAAGRGDEIRPCIGCNQ-CLPTFYGG--ASCYVDPRLGR 365
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
11-331 |
1.04e-119 |
|
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: 360.35 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 11 LAPLDLGFTTLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKH 88
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMAT-EDGTptDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 89 RIVTQAVHEAGGKICMQILHAGRYAYSP----KQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVE 164
Cdd:cd02803 80 RKLTEAVHAHGAKIFAQLAHAGRQAQPNltggPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 165 IMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEK 244
Cdd:cd02803 160 IHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 245 AGATLINTGIGWHEARIPTIA-TKVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADPD 323
Cdd:cd02803 240 AGVDALHVSGGSYESPPPIIPpPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLVALGRALLADPD 319
|
....*...
gi 15598288 324 FVNKAAAG 331
Cdd:cd02803 320 LPNKAREG 327
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
10-331 |
1.14e-97 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 303.99 E-value: 1.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMhTGLEEKPQGF---ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 86
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPM-TRLRSLDDGTkatGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 87 KHRIVTQAVHEAGGKICMQILHAGRYA---YSPKQVAPSAIQAPINPFKP-------KELDEEGIEKQIADFVNCASLAQ 156
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREApmeYRPDLEVDGPSDPFALGAQEfeiasprYEMSKEEIKQHIQDFVDAAKRAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 157 VAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIv 236
Cdd:pfam00724 161 EAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAET- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 237 llAKAVEKAGATLINTGIGWHEARIpTIATKVPRAAFTKVT------AKLRGEVGIPLITTNRINTPEVAEKVLAEGDAD 310
Cdd:pfam00724 240 --AQFIYLLAELGVRLPDGWHLAYI-HAIEPRPRGAGPVRTrqqhntLFVKGVWKGPLITVGRIDDPSVAAEIVSKGRAD 316
|
330 340
....*....|....*....|.
gi 15598288 311 MVSMARPFLADPDFVNKAAAG 331
Cdd:pfam00724 317 LVAMGRPFLADPDLPFKAKKG 337
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
10-343 |
5.47e-85 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.
Pssm-ID: 240085 [Multi-domain] Cd Length: 343 Bit Score: 271.02 E-value: 5.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHR 89
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 90 IVTQAVHEAGGKICMQILHAGR---YAYS-PKQVAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEI 165
Cdd:cd04734 81 RLAEAVHAHGAVIMIQLTHLGRrgdGDGSwLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 166 MGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKA 245
Cdd:cd04734 161 QAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 246 GAT-LINTGIG------WHEARIPTIAtkVPRAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPF 318
Cdd:cd04734 241 GLIdYVNVSAGsyytllGLAHVVPSMG--MPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAAGHADMVGMTRAH 318
|
330 340
....*....|....*....|....*
gi 15598288 319 LADPDFVNKAAAGHAERINTCIGCN 343
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 ... |
10-330 |
1.99e-74 |
|
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: 242.78 E-value: 1.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEE 84
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMcqysaEDGV---ATDWHLV--HYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 85 AEKHRIVTQAVHEAGGKICMQILHAGRYA--YSPKQ---------------VAPSAIQAPINPFKPKELDEEGIEKQIAD 147
Cdd:cd02932 76 IEALKRIVDFIHSQGAKIGIQLAHAGRKAstAPPWEgggpllppggggwqvVAPSAIPFDEGWPTPRELTREEIAEVVDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 148 FVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVE 227
Cdd:cd02932 156 FVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 228 GGSSWDEIVLLAKAVEKAGATLINTGIG--WHEARIPT-IATKVPRAaftkvtAKLRGEVGIPLITTNRINTPEVAEKVL 304
Cdd:cd02932 236 GGWDLEDSVELAKALKELGVDLIDVSSGgnSPAQKIPVgPGYQVPFA------ERIRQEAGIPVIAVGLITDPEQAEAIL 309
|
330 340
....*....|....*....|....*.
gi 15598288 305 AEGDADMVSMARPFLADPDFVNKAAA 330
Cdd:cd02932 310 ESGRADLVALGRELLRNPYWPLHAAA 335
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
9-331 |
7.64e-66 |
|
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: 220.42 E-value: 7.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 9 HLLAPLDLGFTTLRNRTLMGSM---HTGLEEKPQgfERMAAYFAERArgGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA 85
Cdd:cd02933 1 KLFSPLKLGNLTLKNRIVMAPLtrsRADPDGVPT--DLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 86 EKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ------VAPSAIQAPINPFK---------PKELDEEGIEKQIADFVN 150
Cdd:cd02933 77 EGWKKVTDAVHAKGGKIFLQLWHVGRVSHPSLLpggappVAPSAIAAEGKVFTpagkvpyptPRALTTEEIPGIVADFRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 151 CASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIyRLSMLDLVEGGS 230
Cdd:cd02933 157 AARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADRVGI-RLSPFGTFNDMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 231 SWDEIVL---LAKAVEKAG-ATLintgigwH--EARIPTIATKVPRAAFTKVTAKLRGevgiPLITTNRInTPEVAEKVL 304
Cdd:cd02933 236 DSDPEATfsyLAKELNKRGlAYL-------HlvEPRVAGNPEDQPPDFLDFLRKAFKG----PLIAAGGY-DAESAEAAL 303
|
330 340
....*....|....*....|....*..
gi 15598288 305 AEGDADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd02933 304 ADGKADLVAFGRPFIANPDLVERLKNG 330
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
10-362 |
6.05e-62 |
|
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.
Pssm-ID: 239241 [Multi-domain] Cd Length: 382 Bit Score: 211.21 E-value: 6.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMHT-GLEEKPQGF-ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYsGAAKLSTPEEAEK 87
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMGPlGLADNDGAFnQRGIDYYVERAKGGTGLIITGVTMVDNEIEQF-PMPSLPCPTYNPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 88 H-----RIVTQAVHEAGGKICMQILHA-GRYA---YSP--KQVAPSAIQAPINPFKP-KELDEEGIEKQIADFVNCASLA 155
Cdd:cd02931 80 AfirtaKEMTERVHAYGTKIFLQLTAGfGRVCipgFLGedKPVAPSPIPNRWLPEITcRELTTEEVETFVGKFGESAVIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 156 QVAGYDGVEIMG-SEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLS----MLDL----- 225
Cdd:cd02931 160 KEAGFDGVEIHAvHEGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvksyIKDLrqgal 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 226 -----VEGGSSWDEIVLLAKAVEKAGATLINTGIG----WHEARIPTIATKvprAAFTKVTAKLRGEVGIPLITTNRINT 296
Cdd:cd02931 240 pgeefQEKGRDLEEGLKAAKILEEAGYDALDVDAGsydaWYWNHPPMYQKK---GMYLPYCKALKEVVDVPVIMAGRMED 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598288 297 PEVAEKVLAEGDADMVSMARPFLADPDFVNKAAAGHAERINTCIGCNQACLDHTFGGKLTSCLVNP 362
Cdd:cd02931 317 PELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAVNP 382
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
10-331 |
6.85e-60 |
|
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: 204.36 E-value: 6.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGF-TTLRNRTLMGSMHTGLEEKPQ--GFERMAAYfaER-ARGGVGLMVTGGI-----GPNEEGGVYSGAakLS 80
Cdd:cd04733 1 LGQPLTLPNgATLPNRLAKAAMSERLADGRGlpTPELIRLY--RRwAEGGIGLIITGNVmvdprHLEEPGIIGNVV--LE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 81 TPEEAEKHRIVTQAVHEAGGKICMQILHAGRYAY---SPKQVAPSAIQAPINPF----KPKELDEEGIEKQIADFVNCAS 153
Cdd:cd04733 77 SGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPaglNQNPVAPSVALDPGGLGklfgKPRAMTEEEIEDVIDRFAHAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 154 LAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGSSWD 233
Cdd:cd04733 157 LAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 234 EIVLLAKAVEKAGATLINTGIGWHEAriPTIATKVP-----RAA-FTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEG 307
Cdd:cd04733 237 DALEVVEALEEAGVDLVELSGGTYES--PAMAGAKKestiaREAyFLEFAEKIRKVTKTPLMVTGGFRTRAAMEQALASG 314
|
330 340
....*....|....*....|....
gi 15598288 308 DADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd04733 315 AVDGIGLARPLALEPDLPNKLLAG 338
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
20-340 |
1.08e-58 |
|
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: 201.67 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 20 TLRNRTLMGSMHTGLEEkPQGF--ERMAAYFAERArGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAEKHRIVTQAVHE 97
Cdd:cd04735 12 TLKNRFVMAPMTTYSSN-PDGTitDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 98 AGGKICMQILHAGRYAYS-----PKQVAPSAIQAPiNPFK--PKELDEEGIEKQIADFVNCASLAQVAGYDGVEIMGSEG 170
Cdd:cd04735 90 KGAKAILQIFHAGRMANPalvpgGDVVSPSAIAAF-RPGAhtPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 171 YFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVG----PNFIIIYRLSMLDLVEGGSSWDEIVLLAKAVEKAG 246
Cdd:cd04735 169 YLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDkhadKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADKG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 247 ATLINTGIGWHEARIPTIATKVPRAAfTKVTAKLRGEvgIPLITTNRINTPEVAEKVLAEGdADMVSMARPFLADPDFVN 326
Cdd:cd04735 249 LDYLHISLWDFDRKSRRGRDDNQTIM-ELVKERIAGR--LPLIAVGSINTPDDALEALETG-ADLVAIGRGLLVDPDWVE 324
|
330
....*....|....
gi 15598288 327 KAAAGHAERINTCI 340
Cdd:cd04735 325 KIKEGREDEINLEI 338
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
10-331 |
1.38e-48 |
|
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: 174.43 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMhtGLEEKPQGF--ERMAAYFAERARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEA-E 86
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPM--TRSFSPGGVpgQDVAAYYRRRAAGGVGLIITEGTAVDHPAASGDPNVPRFHGEDAlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 87 KHRIVTQAVHEAGGKICMQILHAG--RYAYSP-----KQVAPSAIQAPINPFKPkELDEEGIEKQIADFVNCASLAQVAG 159
Cdd:cd04747 79 GWKKVVDEVHAAGGKIAPQLWHVGamRKLGTPpfpdvPPLSPSGLVGPGKPVGR-EMTEADIDDVIAAFARAAADARRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 160 YDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLVEGGS----SWDEI 235
Cdd:cd04747 158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSQWKQQDYTArladTPDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 236 -VLLAKAVEkAGATLIN----------------TGIGWheAR----IPTIAT------KVPRAAFtkvtaklrgeVGIPL 288
Cdd:cd04747 238 eALLAPLVD-AGVDIFHcstrrfwepefegselNLAGW--TKkltgLPTITVgsvgldGDFIGAF----------AGDEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15598288 289 ITTNRIntpEVAEKVLAEGDADMVSMARPFLADPDFVNKAAAG 331
Cdd:cd04747 305 ASPASL---DRLLERLERGEFDLVAVGRALLSDPAWVAKVREG 344
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
2-330 |
8.42e-45 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 171.28 E-value: 8.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 2 TAAVPYPHLLAPLDLGFTTLRNRTLMGSM-----HTGLeekPQGFERMaaYFAERARGGVGLMVTGGIGPNEEGGVYSGA 76
Cdd:PRK08255 391 PVARPPPPMFTPFRLRGLTLKNRVVVSPMamysaVDGV---PGDFHLV--HLGARALGGAGLVMTEMTCVSPEGRITPGC 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 77 AKLSTPEEAEKHRIVTQAVH-EAGGKICMQILHAGRYAySPKQ----------------VAPSAIQAPINPFKPKELDEE 139
Cdd:PRK08255 466 PGLYNDEQEAAWKRIVDFVHaNSDAKIGIQLGHSGRKG-STRLgwegidepleegnwplISASPLPYLPGSQVPREMTRA 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 140 GIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 219
Cdd:PRK08255 545 DMDRVRDDFVAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVR 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 220 LSMLDLVEGGSSWDEIVLLAKAVEKAGATLIN--TGIGWHEARiPTIAtkvpRAAFTKVTAKLRGEVGIPLITTNRINTP 297
Cdd:PRK08255 625 ISAHDWVEGGNTPDDAVEIARAFKAAGADLIDvsSGQVSKDEK-PVYG----RMYQTPFADRIRNEAGIATIAVGAISEA 699
|
330 340 350
....*....|....*....|....*....|...
gi 15598288 298 EVAEKVLAEGDADMVSMARPFLADPDFVNKAAA 330
Cdd:PRK08255 700 DHVNSIIAAGRADLCALARPHLADPAWTLHEAA 732
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
10-329 |
1.49e-43 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 159.86 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLMGSMHTGLEEKPQGFER---MAAYFAeRARGGVGLMVTGGIGPNEEGGVYSGAAKLSTPEEAE 86
Cdd:PRK13523 3 LFSPYTIKDVTLKNRIVMSPMCMYSSENKDGKVTnfhLIHYGT-RAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 87 KHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ-VAPSAIQAPINPFKPKELDEEGIEKQIADFVNCASLAQVAGYDGVEI 165
Cdd:PRK13523 82 GLHKLVTFIHDHGAKAAIQLAHAGRKAELEGDiVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 166 MGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREA-VGPNFIiiyRLSMLDLVEGGSSWDEIVLLAKAVEK 244
Cdd:PRK13523 162 HGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVwDGPLFV---RISASDYHPGGLTVQDYVQYAKWMKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 245 AGATLINTGIG-WHEARIPTI-ATKVPRAaftkvtAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVSMARPFLADP 322
Cdd:PRK13523 239 QGVDLIDVSSGaVVPARIDVYpGYQVPFA------EHIREHANIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNP 312
|
....*..
gi 15598288 323 DFVNKAA 329
Cdd:PRK13523 313 YFPRIAA 319
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
6-367 |
2.11e-38 |
|
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: 146.35 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 6 PYPHLLAPLDLGFTTLRNR-------TLMGSMHTGLeekpqgferMAAYFAERARGGVGLMVTG--GIGPNEEGGVYSgA 76
Cdd:cd02929 4 RHDILFEPIKIGPVTARNRfyqvphcNGMGYRKPSA---------QAAMRGIKAEGGWGVVNTEqcSIHPSSDDTPRI-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 77 AKLSTPEEAEKHRIVTQAVHEAGGKICMQILHAGRYA--YSPKQV--APSAIQ---APINPFKPKELDEEGIEKQIADFV 149
Cdd:cd02929 74 ARLWDDGDIRNLAAMTDAVHKHGALAGIELWHGGAHApnRESRETplGPSQLPsefPTGGPVQAREMDKDDIKRVRRWYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 150 NCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYRLSMLDLV--E 227
Cdd:cd02929 154 DAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDELIgpG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 228 GGSSWDEIVllaKAVEKAGATL----INTG--IGWHE-ARIPTIATKVPRAAFTK-VTAKlrgevgiPLITTNRINTPEV 299
Cdd:cd02929 234 GIESEGEGV---EFVEMLDELPdlwdVNVGdwANDGEdSRFYPEGHQEPYIKFVKqVTSK-------PVVGVGRFTSPDK 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598288 300 AEKVLAEGDADMVSMARPFLADPDFVNKAAAGHAERINTCIGCNqACLDHTFGGKLTSCLVNPRACHE 367
Cdd:cd02929 304 MVEVVKSGILDLIGAARPSIADPFLPKKIREGRIDDIRECIGCN-ICISGDEGGVPMRCTQNPTAGEE 370
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
10-327 |
3.98e-38 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 145.25 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 10 LLAPLDLGFTTLRNRTLM-----------GSMHTGLeekpqgferMAAYFAERArgGVGLMVTGG--IGPNEEGgvYSGA 76
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMapltrlrsiepGDIPTPL---------MAEYYRQRA--SAGLIISEAtqISAQAKG--YAGA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 77 AKLSTPEEAEKHRIVTQAVHEAGGKICMQILHAGRYAYSPKQ------VAPSAIQAP--------------INPFKPKEL 136
Cdd:PRK10605 70 PGLHSPEQIAAWKKITAGVHAEGGHIAVQLWHTGRISHASLQpggqapVAPSAINAGtrtslrdengqairVETSTPRAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 137 DEEGIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFII 216
Cdd:PRK10605 150 ELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADRIG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 217 IyRLSML---DLVEGGSSWDEIVL-LAKAVEKagatlinTGIGWHEARIPTIATKVP-RAAFTKvtaKLRGEVGIPLITT 291
Cdd:PRK10605 230 I-RISPLgtfNNVDNGPNEEADALyLIEQLGK-------RGIAYLHMSEPDWAGGEPySDAFRE---KVRARFHGVIIGA 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 15598288 292 NRInTPEVAEKVLAEGDADMVSMARPFLADPDFVNK 327
Cdd:PRK10605 299 GAY-TAEKAETLIGKGLIDAVAFGRDYIANPDLVAR 333
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
8-325 |
9.76e-31 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 124.58 E-value: 9.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 8 PHLLAPLDLGFTTLRNRTLMGSMHT--GLEEKPQgfERMAAYFAERARGGvGLMVTGG--IGPNEEG-----GVYSGaak 78
Cdd:PLN02411 10 ETLFSPYKMGRFDLSHRVVLAPMTRcrALNGIPN--AALAEYYAQRSTPG-GFLISEGtlISPTAPGfphvpGIYSD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 79 lstpEEAEKHRIVTQAVHEAGGKICMQILHAGR---YAYSPKQVAP-SAIQAPIN---------------PfKPKELDEE 139
Cdd:PLN02411 84 ----EQVEAWKKVVDAVHAKGSIIFCQLWHVGRashQVYQPGGAAPiSSTNKPISerwrilmpdgsygkyP-KPRALETS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 140 GIEKQIADFVNCASLAQVAGYDGVEIMGSEGYFINQFLVQHTNQRTDRWGGSYENRMRLPVEIVRRVREAVGPNFIIIYR 219
Cdd:PLN02411 159 EIPEVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADRVGVRV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 220 LSMLDLVEGGSSwDEIVLLAKAVEKAGATLINTGigwheARIPTIATKVPRAAFTKVTAKLR---GEVGIPLITTNRIN- 295
Cdd:PLN02411 239 SPAIDHLDATDS-DPLNLGLAVVERLNKLQLQNG-----SKLAYLHVTQPRYTAYGQTESGRhgsEEEEAQLMRTLRRAy 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15598288 296 ----------TPEVAEKVLAEGDADMVSMARPFLADPDFV 325
Cdd:PLN02411 313 qgtfmcsggfTRELGMQAVQQGDADLVSYGRLFISNPDLV 352
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
399-644 |
3.44e-12 |
|
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: 67.73 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 399 ERGHRVSLFDAAGEI-GGQFNVAKRVPGKEEFHETLRYFRN---------KLESTGVELHLN----------RRVGVDDL 458
Cdd:pfam07992 21 QLGGKVTLIEDEGTCpYGGCVLSKALLGAAEAPEIASLWADlykrkeevvKKLNNGIEVLLGtevvsidpgaKKVVLEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 459 VAGG-----YDEIVLATGIVPRTPAIPGIEHP--KVISYLDA--ILERKPVGGKVAVIGAGGIGfdvsefithagpstsl 529
Cdd:pfam07992 101 VDGDgetitYDRLVIATGARPRLPPIPGVELNvgFLVRTLDSaeALRLKLLPKRVVVVGGGYIG---------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 530 ereafwkewgidtrLEARGGIAGIKAEVHPAARQVFLLQRKKSKVGDglgkttgWIHRAgLKNKQVQMVNAVEYLRIDDA 609
Cdd:pfam07992 165 --------------VELAAALAKLGKEVTLIEALDRLLRAFDEEISA-------ALEKA-LEKNGVEVRLGTSVKEIIGD 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 15598288 610 GLHIRVAEGEPQVLPVDTVIVCAGQDPLREL--QDGL 644
Cdd:pfam07992 223 GDGVEVILKDGTEIDADLVVVAIGRRPNTELleAAGL 259
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
403-636 |
9.49e-12 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 66.76 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 403 RVSLFDAAGEIGGQ-FNVAKRVPGKEEFHETLRYF-RNKLESTGVELHLNRRV-GVDD-----LVAGG----YDEIVLAT 470
Cdd:COG0446 7 EITVIEKGPHHSYQpCGLPYYVGGGIKDPEDLLVRtPESFERKGIDVRTGTEVtAIDPeaktvTLRDGetlsYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 471 GIVPRTPAIPGIEHPKV-----ISYLDAILE--RKPVGGKVAVIGAGGIGFDVSEFithagpstslereafWKEWGIDTR 543
Cdd:COG0446 87 GARPRPPPIPGLDLPGVftlrtLDDADALREalKEFKGKRAVVIGGGPIGLELAEA---------------LRKRGLKVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 544 LearggiagikaeVHPAARqvfLLQRKKSKVGDGLGKTtgwihragLKNKQVQMVNAVEYLRID-DAGLHIRVAEGEpqV 622
Cdd:COG0446 152 L------------VERAPR---LLGVLDPEMAALLEEE--------LREHGVELRLGETVVAIDgDDKVAVTLTDGE--E 206
|
250
....*....|....
gi 15598288 623 LPVDTVIVCAGQDP 636
Cdd:COG0446 207 IPADLVVVAPGVRP 220
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
425-633 |
2.32e-10 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 62.85 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 425 GKEEFHETLRYFRNKLESTGVELHLNRRV-GVDD-----LVAGG----YDEIVLATGIVPRTPAIPGIEHPKVISY---- 490
Cdd:COG1251 51 GETDEEDLLLRPADFYEENGIDLRLGTRVtAIDRaartvTLADGetlpYDKLVLATGSRPRVPPIPGADLPGVFTLrtld 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 491 -LDAILERKPVGGKVAVIGAGGIGfdvsefithagpstslereafwkewgidtrLEARGGIAGIKAEV---HPAARqvfL 566
Cdd:COG1251 131 dADALRAALAPGKRVVVIGGGLIG------------------------------LEAAAALRKRGLEVtvvERAPR---L 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598288 567 LQRKkskvgdgLGKTTGWIHRAGLKNKQVQMV--NAVEYLRIDDAGLHIRVAEGEpqVLPVDTVIVCAG 633
Cdd:COG1251 178 LPRQ-------LDEEAGALLQRLLEALGVEVRlgTGVTEIEGDDRVTGVRLADGE--ELPADLVVVAIG 237
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
377-648 |
1.08e-09 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 61.35 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 377 RPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEEfhetlryfrNKLESTGVELHL 449
Cdd:PRK11749 139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGllrygipEFRLPKDIVDREV---------ERLLKLGVEIRT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 450 NRRVG----VDDLVAgGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYLDAI-----LERKPVGGKVAVIGAGGIGFDV 516
Cdd:PRK11749 210 NTEVGrditLDELRA-GYDAVFIGTGAgLPRFLGIPGENLGGVysaVDFLTRVnqavaDYDLPVGKRVVVIGGGNTAMDA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 517 SefithagpSTSLereafwkewgidtRLEA-------RGGIAGIKA---EVHPAA---RQVFLLQRKKSKVGDGLGKTtg 583
Cdd:PRK11749 289 A--------RTAK-------------RLGAesvtivyRRGREEMPAseeEVEHAKeegVEFEWLAAPVEILGDEGRVT-- 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 584 wihraglknkqvqmvnAVEYLRI-----DDAGLHIRVAEGEPQVLPVDTVIVCAGQDPLRELQDGLLAAG 648
Cdd:PRK11749 346 ----------------GVEFVRMelgepDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLE 399
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
379-516 |
2.42e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 60.27 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG--QFNV-AKRVPgkeefHETLRYFRNKLESTGVELHLNRRVGV 455
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRYGIpAYRLP-----REVLDAEIQRILDLGVEVRLGVRVGE 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 456 D---DLVAGGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYLDAI--LERKPVGGKVAVIGAGGIGFDV 516
Cdd:PRK12771 213 DitlEQLEGEFDAVFVAIGAqLGKRLPIPGEDAAGVldaVDFLRAVgeGEPPFLGKRVVVIGGGNTAMDA 282
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
379-636 |
5.97e-09 |
|
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: 58.61 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 379 KKIAVVGAGpaglaaatvaaeRGHRVSLFDAAGEIGGqfnvakrvpgkeefheTLRY----FR----------NKLESTG 444
Cdd:COG0493 122 KKVAVVGSGpaglaaayqlarAGHEVTVFEALDKPGG----------------LLRYgipeFRlpkdvldreiELIEALG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 445 VELHLNRRVGVD----DLVAgGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YL------DAILERKPVGGKVAVIGAG 510
Cdd:COG0493 186 VEFRTNVEVGKDitldELLE-EFDAVFLATGAgKPRDLGIPGEDLKGVHSamdFLtavnlgEAPDTILAVGKRVVVIGGG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 511 GIGFDVsefithAGpsTSLereafwkewgidtRLEA-------RGGIA---GIKAEVHPA----ARQVFLLQRKKSkVGD 576
Cdd:COG0493 265 NTAMDC------AR--TAL-------------RLGAesvtivyRRTREempASKEEVEEAleegVEFLFLVAPVEI-IGD 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598288 577 GLGKTTGwihraglknkqVQMVNaVEYLRIDDAG-LHIRVAEGEPQVLPVDTVIVCAGQDP 636
Cdd:COG0493 323 ENGRVTG-----------LECVR-MELGEPDESGrRRPVPIEGSEFTLPADLVILAIGQTP 371
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
145-316 |
6.36e-09 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 56.44 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 145 IADFVNCASLAQVAGYDGVEIMGSEGYfinqflvqhtnqrtdrwggsyenRMRLPVEIVRRVREAVgPNFIIIYRLSMLD 224
Cdd:cd04722 70 AAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAV-PDVKVVVKLSPTG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 225 lveggsswdeiVLLAKAVEKAGATLINTGIGWHEARIPTIATKVPRaaftkVTAKLRGEVGIPLITTNRINTPEVAEKVL 304
Cdd:cd04722 126 -----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADL-----LLILAKRGSKVPVIAGGGINDPEDAAEAL 189
|
170
....*....|..
gi 15598288 305 AEGdADMVSMAR 316
Cdd:cd04722 190 ALG-ADGVIVGS 200
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
370-517 |
3.25e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 56.70 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 370 LNYIPTTRPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQFNVAkrVPGKEEFHETLRYFRNKLESTGVELHL 449
Cdd:PRK13984 275 LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYG--IPSYRLPDEALDKDIAFIEALGVKIHL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 450 NRRVGVD---DLVAGGYDEIVLATGI-VPRTPAIPGIEHPKVISYLDAILE----------RKPVGGKVAVIGAGGIGFD 515
Cdd:PRK13984 353 NTRVGKDiplEELREKHDAVFLSTGFtLGRSTRIPGTDHPDVIQALPLLREirdylrgegpKPKIPRSLVVIGGGNVAMD 432
|
..
gi 15598288 516 VS 517
Cdd:PRK13984 433 IA 434
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
466-513 |
1.45e-05 |
|
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: 48.16 E-value: 1.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15598288 466 IVLATGIVPRTPAIPGIEHPKVISYlDAILERKPVGGKVAVIGAGGIG 513
Cdd:COG1249 134 IVIATGSRPRVPPIPGLDEVRVLTS-DEALELEELPKSLVVIGGGYIG 180
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
463-648 |
2.52e-05 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 47.52 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 463 YDEIVLATGIVPRTPAIPGIEHPKVISY-----LDAILERKPVGGKVAVIGAGGIGfdvsefithagpstslereafwke 537
Cdd:TIGR02374 97 YDKLILATGSYPFILPIPGADKKGVYVFrtiedLDAIMAMAQRFKKAAVIGGGLLG------------------------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 538 wgidtrLEARGGIAGIKAEVHPAARQVFLLQRKkskvgdgLGKTTGWIHRAGLKNKQVQMVNAVEYLRI--DDAGLHIRV 615
Cdd:TIGR02374 153 ------LEAAVGLQNLGMDVSVIHHAPGLMAKQ-------LDQTAGRLLQRELEQKGLTFLLEKDTVEIvgATKADRIRF 219
|
170 180 190
....*....|....*....|....*....|....*
gi 15598288 616 AEGEpqVLPVDTVIVCAGQDPLREL--QDGLLAAG 648
Cdd:TIGR02374 220 KDGS--SLEADLIVMAAGIRPNDELavSAGIKVNR 252
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
379-636 |
3.24e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 46.93 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEEFhetlryfrNKLESTGVELHLNR 451
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGvlvygipEFRLPKETVVKKEI--------ENIKKLGVKIETNV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 452 RVG----VDDLVA-GGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YLDAI-LER--KP-------VGGKVAVIGAGGI 512
Cdd:PRK12831 213 VVGktvtIDELLEeEGFDAVFIGSGAgLPKFMGIPGENLNGVFSaneFLTRVnLMKayKPeydtpikVGKKVAVVGGGNV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 513 GFDVSefithagpstsleREAFwkEWGIDTRLEARGGIAGIKA---EVHPAARQ--VF-LLQRKKSKVGDglgkTTGWih 586
Cdd:PRK12831 293 AMDAA-------------RTAL--RLGAEVHIVYRRSEEELPArveEVHHAKEEgvIFdLLTNPVEILGD----ENGW-- 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598288 587 raglknkqvqmVNAVEYLRI-----DDAGLH-IRVAEGEPQVLPVDTVIVCAGQDP 636
Cdd:PRK12831 352 -----------VKGMKCIKMelgepDASGRRrPVEIEGSEFVLEVDTVIMSLGTSP 396
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
374-518 |
6.10e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 45.75 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 374 PTTRPKKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQ--FNVAK-RVPgKEEFHETLRyfrnKLESTGVELHLN 450
Cdd:PRK12770 14 PPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLmlFGIPEfRIP-IERVREGVK----ELEEAGVVFHTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 451 -------------------RRVGVDDLVaGGYDEIVLATGI-VPRTPAIPGIEHPKVISYLDAIL------------ERK 498
Cdd:PRK12770 89 tkvccgeplheeegdefveRIVSLEELV-KKYDAVLIATGTwKSRKLGIPGEDLPGVYSALEYLFriraaklgylpwEKV 167
|
170 180
....*....|....*....|..
gi 15598288 499 P--VGGKVAVIGAGGIGFDVSE 518
Cdd:PRK12770 168 PpvEGKKVVVVGAGLTAVDAAL 189
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
367-515 |
7.96e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 45.89 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 367 ETELNYIPTTRPK---KIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGqfnVAK------RVPGKEEFHETlryfr 437
Cdd:PRK12778 417 ESGNISVPEVAEKngkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG---VLKygipefRLPKKIVDVEI----- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 438 NKLESTGVELHLNRRVG----VDDLVAGGYDEIVLATGI-VPRTPAIPGIEHPKVIS---YL------DAILE--RKPV- 500
Cdd:PRK12778 489 ENLKKLGVKFETDVIVGktitIEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVMSsneYLtrvnlmDAASPdsDTPIk 568
|
170
....*....|....*.
gi 15598288 501 -GGKVAVIGAGGIGFD 515
Cdd:PRK12778 569 fGKKVAVVGGGNTAMD 584
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
322-515 |
1.47e-04 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 45.10 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 322 PDFVNKAAAGH---AERI------------NTCIG-CNQACLDHTFGGKLTSC-LVNPRACHETELN--YIPTTRP---K 379
Cdd:PRK12814 115 PGFIAAIARGDdreAIRIiketiplpgilgRICPApCEEACRRHGVDEPVSICaLKRYAADRDMESAerYIPERAPksgK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 380 KIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGGQfnvakrvpgkeefhetLRY----FR----------NKLESTGV 445
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGM----------------MRYgiprFRlpesvidadiAPLRAMGA 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598288 446 ELHLNRRVGVDDLVAG---GYDEIVLATGI-VPRTPAIPGIEHPKVISYLD-----AILERKPVGGKVAVIGAGGIGFD 515
Cdd:PRK12814 259 EFRFNTVFGRDITLEElqkEFDAVLLAVGAqKASKMGIPGEELPGVISGIDflrnvALGTALHPGKKVVVIGGGNTAID 337
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
466-636 |
1.01e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 42.09 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 466 IVLATGivPRTPAIPGIEHP--KVISYLDAILERKPVGGKVAVIGAGGIGfdvsefithagpstsLEREAFWKEWGIDTR 543
Cdd:PRK06292 134 IVIATG--SRVPPIPGVWLIlgDRLLTSDDAFELDKLPKSLAVIGGGVIG---------------LELGQALSRLGVKVT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 544 -LEARGGIAGIK-AEVHPAARQVFllqrkkskvgdglgkttgwihraglkNKQVQM---VNAVEYLRIDDAGLHIRVAEG 618
Cdd:PRK06292 197 vFERGDRILPLEdPEVSKQAQKIL--------------------------SKEFKIklgAKVTSVEKSGDEKVEELEKGG 250
|
170
....*....|....*...
gi 15598288 619 EPQVLPVDTVIVCAGQDP 636
Cdd:PRK06292 251 KTETIEADYVLVATGRRP 268
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
399-633 |
1.02e-03 |
|
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: 42.16 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 399 ERGHRVSLFDAAGEIGG-------------------QF------NVAKRVPGKEEFHETLRYFRNKLestGVELHLNRRV 453
Cdd:COG2072 27 RAGIDFVVLEKADDVGGtwrdnrypglrldtpshlySLpffpnwSDDPDFPTGDEILAYLEAYADKF---GLRRPIRFGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 454 GVDDL------------VAGG----YDEIVLATGI--VPRTPAIPGIEHPKVIS-----YldaileRKPV---GGKVAVI 507
Cdd:COG2072 104 EVTSArwdeadgrwtvtTDDGetltARFVVVATGPlsRPKIPDIPGLEDFAGEQlhsadW------RNPVdlaGKRVLVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 508 GAGGIGFDVSEFITHAG---------PSTSLEREAFWKEWGidtRLEARGGIAGIKAEVHPAARQvFLLQRKKSKVGD-G 577
Cdd:COG2072 178 GTGASAVQIAPELARVAahvtvfqrtPPWVLPRPNYDPERG---RPANYLGLEAPPALNRRDARA-WLRRLLRAQVKDpE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598288 578 LGKTTGWIH------------RAGLKNKQVQMVN-AVEylRIDDAGlhIRVAEGEpqVLPVDTVIVCAG 633
Cdd:COG2072 254 LGLLTPDYPpgckrpllstdyYEALRRGNVELVTgGIE--RITEDG--VVFADGT--EHEVDVIVWATG 316
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
436-513 |
1.04e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 42.07 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 436 FRNKLESTGVELHLNRRVGVDD---LVAGGY---DEIVLATGIVPRTPAIPGIEHpkVIS-----YLDAILERkpvggkV 504
Cdd:PRK06116 99 YRNGLENNGVDLIEGFARFVDAhtvEVNGERytaDHILIATGGRPSIPDIPGAEY--GITsdgffALEELPKR------V 170
|
....*....
gi 15598288 505 AVIGAGGIG 513
Cdd:PRK06116 171 AVVGAGYIA 179
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
379-515 |
1.38e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 41.69 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 379 KKIAVVGAGPAGLAAATVAAERGHRVSLFDAAGEIGG-------QFNVAKRVPGKEefhetlryfRNKLESTGVELHLNR 451
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipDFKLEKEVIDRR---------IELMEAEGIEFRTNV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 452 RVGVD----DLVAgGYDEIVLATGI-VPRTPAIPGIEHPKV---ISYL-------------DAILerkPVGGKVAVIGAG 510
Cdd:PRK12810 215 EVGKDitaeELLA-EYDAVFLGTGAyKPRDLGIPGRDLDGVhfaMDFLiqntrrvlgdetePFIS---AKGKHVVVIGGG 290
|
....*
gi 15598288 511 GIGFD 515
Cdd:PRK12810 291 DTGMD 295
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
425-612 |
3.25e-03 |
|
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: 40.48 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 425 GKEEFHETLRyfRNK----LESTGVELHLNRRVGVDD---LVAGG-----YDEIVLATGIVPRTPAIPGIehpKVISYLD 492
Cdd:TIGR02053 81 GKREVVEELR--HEKyedvLSSYGVDYLRGRARFKDPktvKVDLGrevrgAKRFLIATGARPAIPPIPGL---KEAGYLT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 493 A--ILERKPVGGKVAVIGAGGIGFDVSE-----------------FITHAGPSTSLEREAFWKEWGID-------TRLEA 546
Cdd:TIGR02053 156 SeeALALDRIPESLAVIGGGAIGVELAQafarlgsevtilqrsdrLLPREEPEISAAVEEALAEEGIEvvtsaqvKAVSV 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 547 RGGIAGIKAEVHPAARQV----FLLQRKKSKVGDGLGkttgwIHRAGLKNKQVQMVNAVEYLRIDDAGLH 612
Cdd:TIGR02053 236 RGGGKIITVEKPGGQGEVeadeLLVATGRRPNTDGLG-----LEKAGVKLDERGGILVDETLRTSNPGIY 300
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
187-312 |
3.99e-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: 39.90 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 187 RWGGSYENR--MRLPVEIVRRVREAVGPNFIIiyrlsmldLVEGGSSWD--EIVLLAKAVEKAgatlintGIGWHEARIP 262
Cdd:cd03316 161 KVGGPDSGGedLREDLARVRAVREAVGPDVDL--------MVDANGRWDlaEAIRLARALEEY-------DLFWFEEPVP 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15598288 263 tiatkvprAAFTKVTAKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMV 312
Cdd:cd03316 226 --------PDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDII 267
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
466-519 |
4.69e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 40.13 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598288 466 IVLATGIVPRTpaIPGIE--HPKVISYLDAI-LERKPvgGKVAVIGAGGIGfdvSEF 519
Cdd:PRK06416 138 IILATGSRPRE--LPGIEidGRVIWTSDEALnLDEVP--KSLVVIGGGYIG---VEF 187
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
200-343 |
7.22e-03 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 39.03 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 200 VEIVRRVREAVGPNFIIiyrlsmldLVEGGSSWD--EIVLLAKAVEKAgatlintGIGWHEAriPTiatkvpRAAFTKVT 277
Cdd:COG4948 169 VERVRAVREAVGPDARL--------RVDANGAWTleEAIRLLRALEDL-------GLEWIEQ--PL------PAEDLEGL 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598288 278 AKLRGEVGIPLITTNRINTPEVAEKVLAEGDADMVsmarpfLADPDFVN-----KAAAGHAER--INTCIGCN 343
Cdd:COG4948 226 AELRRATPVPIAADESLTSRADFRRLIEAGAVDIV------NIKLSKVGglteaLRIAALAEAhgVPVMPHCM 292
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
609-668 |
9.54e-03 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 38.60 E-value: 9.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598288 609 AGLHIRVAEGEPQVLPVDTVIVCAGQDPLRELQDGLL-----AAGQSVHLIG---GADVAAE---LDAKRA 668
Cdd:COG4977 51 SGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLawlrrAAARGARLASictGAFLLAAaglLDGRRA 121
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
440-514 |
9.97e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 38.96 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598288 440 LESTGVELHLNRRVGVDD-----LVAGG----YDEIVLATGIVPRTPAIPGIE---------------HPKVISYLDAIL 495
Cdd:COG1252 66 LRRAGVRFIQGEVTGIDPeartvTLADGrtlsYDYLVIATGSVTNFFGIPGLAehalplktledalalRERLLAAFERAE 145
|
90
....*....|....*....
gi 15598288 496 ERKPvgGKVAVIGAGGIGF 514
Cdd:COG1252 146 RRRL--LTIVVVGGGPTGV 162
|
|
| |
