|
Name |
Accession |
Description |
Interval |
E-value |
| mycofact_OYE_2 |
TIGR03997 |
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow ... |
11-657 |
3.70e-172 |
|
mycofactocin system FadH/OYE family oxidoreductase 2; The yeast protein called old yellow enzyme and FadH from Escherichia coli (2,4-dienoyl CoA reductase) are enzymes with 4Fe-4S, FMN, and FAD prosthetic groups, and interact with NADPH as well as substrate. Members of this related protein family occur in the vicinity of the putative mycofactocin biosynthesis operon in a number of Actinobacteria such as Frankia sp. and Rhodococcus sp., in Pelotomaculum thermopropionicum SI (Firmicutes), and in Geobacter uraniireducens Rf4 (Deltaproteobacteria). The function of this oxidoreductase is unknown.
Pssm-ID: 274912 [Multi-domain] Cd Length: 644 Bit Score: 506.15 E-value: 3.70e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFGEHHLPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPFRR 90
Cdd:TIGR03997 3 FSPLRIGPVTLPNRIVFGAHLTNYAVNNLPSERHAAYYAERAKGGAGLIITEELSVHPSDRPYEKLIDGYRPAVIPGYRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 91 ITDPVKADGAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIELQ 170
Cdd:TIGR03997 83 ITDAVHAHGVKIFAQLNHNGGQGDSSYSRLPVWAPSAVPDPLFREVPKAMEESDIAEVVAGFARVAGHVVAGGFDGIEIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 171 MAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQIVPMLARQT 250
Cdd:TIGR03997 163 ASHSSLVRQFLSPLTNRRTDEYGGSLENRARFLLEVLEAVRKAIGPDRALGVRLCGDELVPGGLTLADAVEIARLLEALG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 251 KIDFVNVshSAYVASYSLATQMADMAFDPAPFRALPARIRHELRargfqTPVFAVCRFTGLDEADAMIAAGDADAVGMAR 330
Cdd:TIGR03997 243 LVDYINT--SIGVATYTLHLVEASMHVPPGYAAFLAAAIREAVD-----LPVFAVGRINDPAQAERALAEGQADLVGMVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 331 AHLAEPAIVRKSIEGRTHEIRRCIGCNQGCAGMLERNLPIRCLINPIAGLEgrFDEPEALPRGATRKVLVVGGGPAGLEA 410
Cdd:TIGR03997 316 GQIADPDFAAKALEGREEDIRTCLSCNQECIGRVGLNRWLGCVVNPRAGRE--FGTVTLPPPRRPKRVLVVGGGPAGLEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 411 ARVAAALGHEVTLWERSDQLGGQLRTAWLMPKRANFKAFVEFQSAALTRLGATVVFNKNADAAGISAFGADRIVLATGST 490
Cdd:TIGR03997 394 AATAARRGHRVTLFEREDRLGGQVRLAARLPGRGEFADLIRNLASELRRAGVEVRLGVEADAELVLAEKPDAVVVATGSR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 491 TAALPVSG-NGP-VFTLPDALRAPEQLGACVAVFDRTGEWGTLAALEHFADLGKAVTLFVPATSYAWRTTIYSTLANSRR 568
Cdd:TIGR03997 474 PVRPPWAGaDGPrVVTVREVLTGRAEPGGRVLVVDELGFHQATSVAEFLAARGKKVTIITPSLFVGQDLGPTLDLEGWYR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 569 -LRERRVRIATLRAVRSYDGQILAVEDLSTGDIERLTGFSALVAVDHNSTDQTLYLSLRRAGLPVLQAGDNNAPRTALEA 647
Cdd:TIGR03997 554 rAFQKGIEQTTDSLVTAVDGGTVTVVHHPTGRVRVLTGVDWVVLAAPPRPDDELYLSLKGRVPEVYRIGDCLAPRRVHAA 633
|
650
....*....|
gi 496250708 648 IYQGHMAARA 657
Cdd:TIGR03997 634 IREGHRVGLA 643
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
11-357 |
3.45e-156 |
|
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: 453.99 E-value: 3.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFGEHHLPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPFRR 90
Cdd:cd04734 2 LSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 91 ITDPVKADGAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIELQ 170
Cdd:cd04734 82 LAEAVHAHGAVIMIQLTHLGRRGDGDGSWLPPLAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADAARRCQAGGLDGVELQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 171 MAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQIVPMLARQT 250
Cdd:cd04734 162 AAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLSPDEALEIAARLAAEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 251 KIDFVNVSHSAYVASYSLATQMADMAFDPAPFRALPARIRHELRArgfqtPVFAVCRFTGLDEADAMIAAGDADAVGMAR 330
Cdd:cd04734 242 LIDYVNVSAGSYYTLLGLAHVVPSMGMPPGPFLPLAARIKQAVDL-----PVFHAGRIRDPAEAEQALAAGHADMVGMTR 316
|
330 340
....*....|....*....|....*..
gi 496250708 331 AHLAEPAIVRKSIEGRTHEIRRCIGCN 357
Cdd:cd04734 317 AHIADPHLVAKAREGREDDIRPCIGCN 343
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
5-379 |
3.48e-112 |
|
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: 341.76 E-value: 3.48e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 5 QPYAQALSPLDVGPLRWRNRIFVPAHTTNFGEH-HLPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPA 83
Cdd:COG1902 2 MKMPKLFSPLTLGGLTLKNRIVMAPMTRGRADEdGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 84 CIDPFRRITDPVKADGAAMLGQIIHLGRQVEGDF-ERTVSWGASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAA 162
Cdd:COG1902 82 QIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLpGGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDFAAAARRAKEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 163 GFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQI 242
Cdd:COG1902 162 GFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEGGLTLEESVEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 243 VPMLARQtKIDFVNVSHSAYVasyslATQMADMAFDPAPFRALPARIRHElrargFQTPVFAVCRFTGLDEADAMIAAGD 322
Cdd:COG1902 242 AKALEEA-GVDYLHVSSGGYE-----PDAMIPTIVPEGYQLPFAARIRKA-----VGIPVIAVGGITTPEQAEAALASGD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496250708 323 ADAVGMARAHLAEPAIVRKSIEGRTHEIRRCIGCNQGCAGMLernLPIRCLINPIAG 379
Cdd:COG1902 311 ADLVALGRPLLADPDLPNKAAAGRGDEIRPCIGCNQCLPTFY---GGASCYVDPRLG 364
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
11-345 |
8.70e-92 |
|
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: 287.55 E-value: 8.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFG-EHHLPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPFR 89
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTENMAtEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 90 RITDPVKADGAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIEL 169
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQAQPNLTGGPPPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAARRAKEAGFDGVEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 170 QMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQIVPMLARQ 249
Cdd:cd02803 161 HGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEIAKALEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 250 tKIDFVNVSHSAYvasYSLATQMADMAFDPAPFRALPARIRhelraRGFQTPVFAVCRFTGLDEADAMIAAGDADAVGMA 329
Cdd:cd02803 241 -GVDALHVSGGSY---ESPPPIIPPPYVPEGYFLELAEKIK-----KAVKIPVIAVGGIRDPEVAEEILAEGKADLVALG 311
|
330
....*....|....*.
gi 496250708 330 RAHLAEPAIVRKSIEG 345
Cdd:cd02803 312 RALLADPDLPNKAREG 327
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
11-376 |
4.95e-68 |
|
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: 226.40 E-value: 4.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFGE--HHLPSLQhlAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPF 88
Cdd:cd02930 2 LSPLDLGFTTLRNRVLMGSMHTGLEEldDGIDRLA--AFYAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 89 RRITDPVKADGAAMLGQIIHLGRqvEGDFERTVSwgASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIE 168
Cdd:cd02930 80 RLITDAVHAEGGKIALQILHAGR--YAYHPLCVA--PSAIRAPINPFTPRELSEEEIEQTIEDFARCAALAREAGYDGVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 169 LQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQivpmLAR 248
Cdd:cd02930 156 IMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVA----LAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 249 QTK---IDFVNVS---HSAYVASYSlatqmadMAFDPAPFRALPARIRHELrargfQTPVFAVCRFTGLDEADAMIAAGD 322
Cdd:cd02930 232 ALEaagADILNTGigwHEARVPTIA-------TSVPRGAFAWATAKLKRAV-----DIPVIASNRINTPEVAERLLADGD 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496250708 323 ADAVGMARAHLAEPAIVRKSIEGRTHEIRRCIGCNQGCAGMLERNLPIRCLINP 376
Cdd:cd02930 300 ADMVSMARPFLADPDFVAKAAAGRADEINTCIACNQACLDHIFTGQRASCLVNP 353
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
12-336 |
2.94e-67 |
|
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: 223.52 E-value: 2.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 12 SPLDVGPLRWRNRIFVP------AHTTNFGEHHLpslQHLAyhrARARGGVGAIIFESIRVHANslGR--PQAVCGFDPA 83
Cdd:cd02932 3 TPLTLRGVTLKNRIVVSpmcqysAEDGVATDWHL---VHYG---SRALGGAGLVIVEATAVSPE--GRitPGDLGLWNDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 84 CIDPFRRITDPVKADGAAMLGQIIHLGR---------------QVEGDFERTVswGASAVPWSISALPPRPMDEFDMEQV 148
Cdd:cd02932 75 QIEALKRIVDFIHSQGAKIGIQLAHAGRkastappwegggpllPPGGGGWQVV--APSAIPFDEGWPTPRELTREEIAEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 149 IEGHLVTARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEE 228
Cdd:cd02932 153 VDAFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 229 YAEGGLGIDEAAQIVPMLARQTkIDFVNVSHSAYVASyslatqmADMAFDPAPFRALPARIRHELRargfqTPVFAVCRF 308
Cdd:cd02932 233 WVEGGWDLEDSVELAKALKELG-VDLIDVSSGGNSPA-------QKIPVGPGYQVPFAERIRQEAG-----IPVIAVGLI 299
|
330 340
....*....|....*....|....*...
gi 496250708 309 TGLDEADAMIAAGDADAVGMARAHLAEP 336
Cdd:cd02932 300 TDPEQAEAILESGRADLVALGRELLRNP 327
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
23-345 |
8.43e-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: 203.97 E-value: 8.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 23 NRIFVPAHTTNFGE-HHLPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQA---VCGFDPACIDPFRRITDPVKAD 98
Cdd:cd04733 15 NRLAKAAMSERLADgRGLPTPELIRLYRRWAEGGIGLIITGNVMVDPRHLEEPGIignVVLESGEDLEAFREWAAAAKAN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 99 GAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISAL---PPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIELQMAHGH 175
Cdd:cd04733 95 GALIWAQLNHPGRQSPAGLNQNPVAPSVALDPGGLGKlfgKPRAMTEEEIEDVIDRFAHAARLAQEAGFDGVQIHAAHGY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 176 LLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQIVPMLArQTKIDFV 255
Cdd:cd04733 175 LLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPVGIKLNSADFQRGGFTEEDALEVVEALE-EAGVDLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 256 NVSHSAYVASYSLATQMADMAFDPAPFRALPARIRhelraRGFQTPVFAVCRFTGLDEADAMIAAGDADAVGMARAHLAE 335
Cdd:cd04733 254 ELSGGTYESPAMAGAKKESTIAREAYFLEFAEKIR-----KVTKTPLMVTGGFRTRAAMEQALASGAVDGIGLARPLALE 328
|
330
....*....|
gi 496250708 336 PAIVRKSIEG 345
Cdd:cd04733 329 PDLPNKLLAG 338
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
13-346 |
5.50e-57 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 196.52 E-value: 5.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 13 PLDVGPLRWRNRIFVPAHTtNFGEHH---LPSLQHLAYHRARARGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPFR 89
Cdd:pfam00724 5 PIKIGNTTLKNRIVMAPMT-RLRSLDdgtKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEGWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 90 RITDPVKADGAAMLGQIIHLGRQVEGDF-ERTVSWGASAV-----PWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAG 163
Cdd:pfam00724 84 KLTEAVHKNGSKAGVQLWHLGREAPMEYrPDLEVDGPSDPfalgaQEFEIASPRYEMSKEEIKQHIQDFVDAAKRAREAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 164 FDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGGLGIDEAAQIV 243
Cdd:pfam00724 164 FDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPGLDFAETAQFI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 244 PMLArQTKIDFVNVSHSAYVAsyslatqmadmAFDPAPFRALPARIRHELRAR----GFQTPVFAVCRFTGLDEADAMIA 319
Cdd:pfam00724 244 YLLA-ELGVRLPDGWHLAYIH-----------AIEPRPRGAGPVRTRQQHNTLfvkgVWKGPLITVGRIDDPSVAAEIVS 311
|
330 340
....*....|....*....|....*..
gi 496250708 320 AGDADAVGMARAHLAEPAIVRKSIEGR 346
Cdd:pfam00724 312 KGRADLVAMGRPFLADPDLPFKAKKGR 338
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
13-381 |
7.23e-53 |
|
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.
Pssm-ID: 239239 [Multi-domain] Cd Length: 370 Bit Score: 186.41 E-value: 7.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 13 PLDVGPLRWRNRIFVPAHTTNFGEHHlPSLQhlAYHRA-RARGGVGAIIFESIRVHANS--LGRPQAVCgFDPACIDPFR 89
Cdd:cd02929 11 PIKIGPVTARNRFYQVPHCNGMGYRK-PSAQ--AAMRGiKAEGGWGVVNTEQCSIHPSSddTPRISARL-WDDGDIRNLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 90 RITDPVKADGAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISALPP---RPMDEFDMEQVIEGHLVTARNLVAAGFDG 166
Cdd:cd02929 87 AMTDAVHKHGALAGIELWHGGAHAPNRESRETPLGPSQLPSEFPTGGPvqaREMDKDDIKRVRRWYVDAALRARDAGFDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 167 IELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEE-YAEGGLGI-DEAAQIVP 244
Cdd:cd02929 167 VYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDElIGPGGIESeGEGVEFVE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 245 MLARQTKIDFVNVShsayvasySLATQMADMAFDPAPFR-ALPARIRhelraRGFQTPVFAVCRFTGLDEADAMIAAGDA 323
Cdd:cd02929 247 MLDELPDLWDVNVG--------DWANDGEDSRFYPEGHQePYIKFVK-----QVTSKPVVGVGRFTSPDKMVEVVKSGIL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496250708 324 DAVGMARAHLAEPAIVRKSIEGRTHEIRRCIGCNQgCAGMLERNLPIRCLINPIAGLE 381
Cdd:cd02929 314 DLIGAARPSIADPFLPKKIREGRIDDIRECIGCNI-CISGDEGGVPMRCTQNPTAGEE 370
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
22-351 |
5.20e-51 |
|
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: 180.49 E-value: 5.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 22 RNRIFVPAHTTN--FGEHHLpSLQHLAYHRARArGGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPFRRITDPVKADG 99
Cdd:cd04735 14 KNRFVMAPMTTYssNPDGTI-TDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGLRKLAQAIKSKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 100 AAMLGQIIHLGRQVEGDFER-TVSWGASAV-PWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIELQMAHGHLL 177
Cdd:cd04735 92 AKAILQIFHAGRMANPALVPgGDVVSPSAIaAFRPGAHTPRELTHEEIEDIIDAFGEATRRAIEAGFDGVEIHGANGYLI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 178 QQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRA----ELGATFCLGIRISGEEYAEGGLGIDEAAQIVPMLARQtKID 253
Cdd:cd04735 172 QQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEvidkHADKDFILGYRFSPEEPEEPGIRMEDTLALVDKLADK-GLD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 254 FVNVShSAYVASYSLATQMADMAFDPAPFRALPARIrhelrargfqtPVFAVCRFTGLDEADAMIAAGdADAVGMARAHL 333
Cdd:cd04735 251 YLHIS-LWDFDRKSRRGRDDNQTIMELVKERIAGRL-----------PLIAVGSINTPDDALEALETG-ADLVAIGRGLL 317
|
330
....*....|....*...
gi 496250708 334 AEPAIVRKSIEGRTHEIR 351
Cdd:cd04735 318 VDPDWVEKIKEGREDEIN 335
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
11-337 |
1.27e-46 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 176.67 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFGEHHLPSLQHLAYHRARARGGVGAIIFESIRVHANslGRPQAVCG--FDPACIDPF 88
Cdd:PRK08255 400 FTPFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPE--GRITPGCPglYNDEQEAAW 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 89 RRITDPVKADGAAMLG-QIIHLGR----QV----------EGDFERTvswGASAVPWSISALPPRPMDEFDMEQVIEGHL 153
Cdd:PRK08255 478 KRIVDFVHANSDAKIGiQLGHSGRkgstRLgwegidepleEGNWPLI---SASPLPYLPGSQVPREMTRADMDRVRDDFV 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 154 VTARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRISGEEYAEGG 233
Cdd:PRK08255 555 AAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGG 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 234 LGIDEAAQIVPMLArQTKIDFVNVS--------HSAYVASYSlaTQMADmafdpapfralpaRIRHELRargfqTPVFAV 305
Cdd:PRK08255 635 NTPDDAVEIARAFK-AAGADLIDVSsgqvskdeKPVYGRMYQ--TPFAD-------------RIRNEAG-----IATIAV 693
|
330 340 350
....*....|....*....|....*....|..
gi 496250708 306 CRFTGLDEADAMIAAGDADAVGMARAHLAEPA 337
Cdd:PRK08255 694 GAISEADHVNSIIAAGRADLCALARPHLADPA 725
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
11-341 |
2.97e-44 |
|
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: 161.49 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIfVPAHTTNF--GEHHLPSLQHLAYHRARArgGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPF 88
Cdd:cd02933 3 FSPLKLGNLTLKNRI-VMAPLTRSraDPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEGW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 89 RRITDPVKADGAAMLGQIIHLGRQ----VEGDFERTVSwgASAVPWSISAL---------PPRPMDEFDMEQVIEGHLVT 155
Cdd:cd02933 80 KKVTDAVHAKGGKIFLQLWHVGRVshpsLLPGGAPPVA--PSAIAAEGKVFtpagkvpypTPRALTTEEIPGIVADFRQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 156 ARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATfCLGIRISGEEYAEGGLG 235
Cdd:cd02933 158 ARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGAD-RVGIRLSPFGTFNDMGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 236 IDEAAQIVPMLAR--QTKIDFVNVSHsayvasyslatqmADMAFDPAPfraLPARIRHELRARgFQTPVFAVCRFTgLDE 313
Cdd:cd02933 237 SDPEATFSYLAKElnKRGLAYLHLVE-------------PRVAGNPED---QPPDFLDFLRKA-FKGPLIAAGGYD-AES 298
|
330 340
....*....|....*....|....*...
gi 496250708 314 ADAMIAAGDADAVGMARAHLAEPAIVRK 341
Cdd:cd02933 299 AEAALADGKADLVAFGRPFIANPDLVER 326
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
11-351 |
7.64e-42 |
|
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: 155.55 E-value: 7.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTTNFGEHHLPSLQHLAYHRARARGGVGAIIFESIRV-HANSLGRPQAVCGFDPACIDPFR 89
Cdd:cd04747 2 FTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAVdHPAASGDPNVPRFHGEDALAGWK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 90 RITDPVKADGAAMLGQIIHLGrqveGDFERTVSWGASAVPWSISALPP------RPMDEFDMEQVIEGHLVTARNLVAAG 163
Cdd:cd04747 82 KVVDEVHAAGGKIAPQLWHVG----AMRKLGTPPFPDVPPLSPSGLVGpgkpvgREMTEADIDDVIAAFARAAADARRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 164 FDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRIS---GEEY-AEGGLGIDEA 239
Cdd:cd04747 158 FDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFSqwkQQDYtARLADTPDEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 240 AQIVPMLArQTKIDFVNVSHSAYV------ASYSLA------TQMADMAFDPApfrALPARIRHELRARGFQTPvfavcr 307
Cdd:cd04747 238 EALLAPLV-DAGVDIFHCSTRRFWepefegSELNLAgwtkklTGLPTITVGSV---GLDGDFIGAFAGDEGASP------ 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 496250708 308 fTGLDEADAMIAAGDADAVGMARAHLAEPAIVRKSIEGRTHEIR 351
Cdd:cd04747 308 -ASLDRLLERLERGEFDLVAVGRALLSDPAWVAKVREGRLDELI 350
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
44-350 |
1.85e-39 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 148.31 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 44 HLAYHRARARGGVGAIIFESIRVHANslGR--PQAVCGFDPACIDPFRRITDPVKADGAAMLGQIIHLGR--QVEGDfer 119
Cdd:PRK13523 39 HLIHYGTRAAGQVGLVIVEATAVLPE--GRisDKDLGIWDDEHIEGLHKLVTFIHDHGAKAAIQLAHAGRkaELEGD--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 120 tvSWGASAVPWSISALPPRPMDEFDMEQVIEGHLVTARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENR 199
Cdd:PRK13523 114 --IVAPSAIPFDEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 200 LRFPARVLAALRaEL--GATFclgIRISGEEYAEGGLGIDEAAQIVPMLARQtKIDFVNVSHSAYVasyslatqmadmaf 277
Cdd:PRK13523 192 YRFLREIIDAVK-EVwdGPLF---VRISASDYHPGGLTVQDYVQYAKWMKEQ-GVDLIDVSSGAVV-------------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 278 dPAPFRALPA-------RIRHELrargfQTPVFAVCRFTGLDEADAMIAAGDADAVGMARAHLAEPAIVRKSIEGRTHEI 350
Cdd:PRK13523 253 -PARIDVYPGyqvpfaeHIREHA-----NIATGAVGLITSGAQAEEILQNNRADLIFIGRELLRNPYFPRIAAKELGFEI 326
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
13-376 |
1.47e-37 |
|
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: 144.19 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 13 PLDVGPLRWRNRI-FVPAHTTNFGEHHLPSLQH-LAYHRARARGGVGAIIfESIRVHANSLGR---PQAVC-GFDP-ACI 85
Cdd:cd02931 4 PIKIGKVEIKNRFaMAPMGPLGLADNDGAFNQRgIDYYVERAKGGTGLII-TGVTMVDNEIEQfpmPSLPCpTYNPtAFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 86 DPFRRITDPVKADGAAMLGQIihlgrqvegdferTVSWGASAVPWSISALPP----------------RPMDEFDMEQVI 149
Cdd:cd02931 83 RTAKEMTERVHAYGTKIFLQL-------------TAGFGRVCIPGFLGEDKPvapspipnrwlpeitcRELTTEEVETFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 150 EGHLVTARNLVAAGFDGIELQMAH-GHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFCLGIRIS--- 225
Cdd:cd02931 150 GKFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRYSvks 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 226 -----------GEEYAEGGLGIDEAAQIVPMLaRQTKIDFVNVSHSAYVASYslaTQMADMAFDPAPFRALPARIRHELR 294
Cdd:cd02931 230 yikdlrqgalpGEEFQEKGRDLEEGLKAAKIL-EEAGYDALDVDAGSYDAWY---WNHPPMYQKKGMYLPYCKALKEVVD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 295 argfqTPVFAVCRFTGLDEADAMIAAGDADAVGMARAHLAEPAIVRKSIEGRTHEIRRCIGCNQGCAGMLERNLPIRCLI 374
Cdd:cd02931 306 -----VPVIMAGRMEDPELASEAINEGIADMISLGRPLLADPDVVNKIRRGRFKNIRPCISCHDGCLGRMALGGNLSCAV 380
|
..
gi 496250708 375 NP 376
Cdd:cd02931 381 NP 382
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
11-339 |
5.77e-28 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 115.98 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 11 LSPLDVGPLRWRNRIFVPAHTT--NFGEHHLPSLQHLAYHRARArgGVGAIIFESIRVHANSLGRPQAVCGFDPACIDPF 88
Cdd:PRK10605 4 FSPLKVGAITAPNRVFMAPLTRlrSIEPGDIPTPLMAEYYRQRA--SAGLIISEATQISAQAKGYAGAPGLHSPEQIAAW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 89 RRITDPVKADGAAMLGQIIHLGR----QVEGDFERTVSwgASAVPWS--------------ISALPPRPMDEFDMEQVIE 150
Cdd:PRK10605 82 KKITAGVHAEGGHIAVQLWHTGRishaSLQPGGQAPVA--PSAINAGtrtslrdengqairVETSTPRALELEEIPGIVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 151 GHLVTARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFcLGIRIS---GE 227
Cdd:PRK10605 160 DFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGADR-IGIRISplgTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 228 EYAEGGLGIDEAA-QIVPMLARQtKIDFVNVSHSayvasyslatqmadmafDPAPFRALPARIRHELRARgFQTPVFAVC 306
Cdd:PRK10605 239 NNVDNGPNEEADAlYLIEQLGKR-GIAYLHMSEP-----------------DWAGGEPYSDAFREKVRAR-FHGVIIGAG 299
|
330 340 350
....*....|....*....|....*....|...
gi 496250708 307 RFTGlDEADAMIAAGDADAVGMARAHLAEPAIV 339
Cdd:PRK10605 300 AYTA-EKAETLIGKGLIDAVAFGRDYIANPDLV 331
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
2-225 |
2.26e-22 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 99.93 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 2 SQHQPYAQALSPLDVGPLRWRNRIFVPAHTTNFGEHHLPSLQHLAYHRARARGGvGAIIFESIRVHANSLGRPQAVCGFD 81
Cdd:PLN02411 4 AQGNSNETLFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 82 PACIDPFRRITDPVKADGAAMLGQIIHLGRQVEGDFERTVSWGASAVPWSISA-----LP---------PRPMDEFDMEQ 147
Cdd:PLN02411 83 DEQVEAWKKVVDAVHAKGSIIFCQLWHVGRASHQVYQPGGAAPISSTNKPISErwrilMPdgsygkypkPRALETSEIPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496250708 148 VIEGHLVTARNLVAAGFDGIELQMAHGHLLQQFMSPLSNKRSDEYGGSLENRLRFPARVLAALRAELGATFcLGIRIS 225
Cdd:PLN02411 163 VVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSAIGADR-VGVRVS 239
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
396-498 |
6.79e-11 |
|
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: 64.77 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTAwlMPkraNF---KAFVEFQSAALTRLGATVVFN----K 468
Cdd:COG0493 122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRYG--IP---EFrlpKDVLDREIELIEALGVEFRTNvevgK 196
|
90 100 110
....*....|....*....|....*....|..
gi 496250708 469 NADAAGISA-FgaDRIVLATGSTTA-ALPVSG 498
Cdd:COG0493 197 DITLDELLEeF--DAVFLATGAGKPrDLGIPG 226
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
386-498 |
7.76e-11 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 64.80 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 386 EPEALPRGatRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLR--------TAWLMPKRAN-FKAF-VEFqsa 455
Cdd:PRK12810 136 DPPVKRTG--KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRygipdfklEKEVIDRRIElMEAEgIEF--- 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 496250708 456 altRLGATVvfNKNADAAGISA-FgaDRIVLATGSTTA-ALPVSG 498
Cdd:PRK12810 211 ---RTNVEV--GKDITAEELLAeY--DAVFLGTGAYKPrDLGIPG 248
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
383-435 |
8.66e-11 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 64.88 E-value: 8.66e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 496250708 383 RFDEP-EALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLR 435
Cdd:COG1148 127 KLLEPlEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAA 180
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
397-546 |
1.11e-10 |
|
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: 63.11 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWE-RSDQLGGQ-------LRTAWLMPKRANFKAFVEFQSAALTRLGATVVFNK 468
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGcvlskalLGAAEAPEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 469 NADAAGI-----------------SAFGADRIVLATGSTTAALPVSGNGP-----VFTLPDALR-APEQLGACVAVfdrT 525
Cdd:pfam07992 82 GTEVVSIdpgakkvvleelvdgdgETITYDRLVIATGARPRLPPIPGVELnvgflVRTLDSAEAlRLKLLPKRVVV---V 158
|
170 180
....*....|....*....|....
gi 496250708 526 GewGTLAALEH---FADLGKAVTL 546
Cdd:pfam07992 159 G--GGYIGVELaaaLAKLGKEVTL 180
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
381-488 |
2.07e-09 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 60.19 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 381 EGRFDEPEALPRGatRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT---AWLMPKRanfkaFVEFQSAAL 457
Cdd:PRK11749 128 TGWVLFKRAPKTG--KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLRYgipEFRLPKD-----IVDREVERL 200
|
90 100 110
....*....|....*....|....*....|....*
gi 496250708 458 TRLGATVVFN----KNADAAGISAfGADRIVLATG 488
Cdd:PRK11749 201 LKLGVEIRTNtevgRDITLDELRA-GYDAVFIGTG 234
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
396-436 |
2.28e-09 |
|
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: 60.23 E-value: 2.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRT 42
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
396-435 |
1.06e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 58.35 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLR 435
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMR 177
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
397-432 |
2.12e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 56.82 E-value: 2.12e-08
10 20 30
....*....|....*....|....*....|....*.
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
396-493 |
7.10e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 55.50 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTAwlMPKRANFKAFVEFQSAALTRLGATVVFN----KNAD 471
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYG--IPRFRLPESVIDADIAPLRAMGAEFRFNtvfgRDIT 271
|
90 100
....*....|....*....|...
gi 496250708 472 AAGI-SAFgaDRIVLATGSTTAA 493
Cdd:PRK12814 272 LEELqKEF--DAVLLAVGAQKAS 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
397-434 |
1.40e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 49.12 E-value: 1.40e-07
10 20 30
....*....|....*....|....*....|....*...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQL 434
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGF 38
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
398-548 |
6.88e-07 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 52.01 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERsDQLGGQ------------LRTAWLM--------------PKRANFKAFVE 451
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGTclnvgcipskalLHAAEVAhearhaaefgisagAPSVDWAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 452 FQSAALTRLGATVVFN-KNADAAGISAFG-----------------ADRIVLATGSTTAALPVSG--NGPVFTLPDALRA 511
Cdd:COG1249 85 RKDKVVDRLRGGVEELlKKNGVDVIRGRArfvdphtvevtggetltADHIVIATGSRPRVPPIPGldEVRVLTSDEALEL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496250708 512 PEQ------LGACV-AVfdrtgEWGTLaalehFADLGKAVTLFV 548
Cdd:COG1249 165 EELpkslvvIGGGYiGL-----EFAQI-----FARLGSEVTLVE 198
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
392-436 |
9.26e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 51.85 E-value: 9.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 496250708 392 RGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:COG1231 4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWT 48
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
397-451 |
1.21e-06 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 48.66 E-value: 1.21e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERS--------DQLGGQLRTawLMPKRANFKAFVE 451
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRparlrqleSLLGARFTT--LYSQAELLEEAVK 82
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
388-493 |
1.29e-06 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 51.30 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 388 EALPRGatRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDqlggqlrtaWLMPKRANfKAFVEFQSAALTRLGATVVFN 467
Cdd:COG1251 137 AALAPG--KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAP---------RLLPRQLD-EEAGALLQRLLEALGVEVRLG 204
|
90 100 110
....*....|....*....|....*....|
gi 496250708 468 knadaAGISAFGAD----RIVLATGSTTAA 493
Cdd:COG1251 205 -----TGVTEIEGDdrvtGVRLADGEELPA 229
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
398-441 |
1.67e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 51.07 E-value: 1.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTAWLMP 441
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSGLVGP 45
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
400-436 |
2.01e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 45.60 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*..
gi 496250708 400 VVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYS 37
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
396-488 |
2.36e-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: 400379 [Multi-domain] Cd Length: 301 Bit Score: 50.01 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGgqlrtawlmpkRANFKAFVEFQSAALTRLGATVVFNK-----NA 470
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL-----------RAFDEEISAALEKALEKNGVEVRLGTsvkeiIG 221
|
90 100
....*....|....*....|....*
gi 496250708 471 DAAGISAFG-------ADRIVLATG 488
Cdd:pfam07992 222 DGDGVEVILkdgteidADLVVVAIG 246
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
388-488 |
3.58e-06 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 49.42 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 388 EALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLggqlrtawLMPKRANFKAFVEfqsAALTRLGATVVFN 467
Cdd:COG0446 117 EALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL--------LGVLDPEMAALLE---EELREHGVELRLG 185
|
90 100 110
....*....|....*....|....*....|..
gi 496250708 468 KNADA----AGISA-------FGADRIVLATG 488
Cdd:COG0446 186 ETVVAidgdDKVAVtltdgeeIPADLVVVAPG 217
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
394-436 |
7.55e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 7.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 496250708 394 ATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRART 44
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
386-488 |
9.07e-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: 48.54 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 386 EPEALPRgatrKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG----QLRTAWlmpKRANFKAFVEFQ-SAALTRL 460
Cdd:COG1249 163 ELEELPK----SLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPgedpEISEAL---EKALEKEGIDILtGAKVTSV 235
|
90 100 110
....*....|....*....|....*....|...
gi 496250708 461 -----GATVVFNknaDAAGISAFGADRIVLATG 488
Cdd:COG1249 236 ektgdGVTVTLE---DGGGEEAVEADKVLVATG 265
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
394-432 |
1.07e-05 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 48.31 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*....
gi 496250708 394 ATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
397-432 |
1.15e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 48.32 E-value: 1.15e-05
10 20 30
....*....|....*....|....*....|....*.
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERsDQLGG 432
Cdd:PRK07845 3 RIVIIGGGPGGYEAALVAAQLGADVTVIER-DGLGG 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
396-437 |
1.24e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 47.96 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTA 437
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKILIS 42
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
399-437 |
2.08e-05 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 47.21 E-value: 2.08e-05
10 20 30
....*....|....*....|....*....|....*....
gi 496250708 399 LVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTA 437
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGKKLLIS 39
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
397-498 |
4.22e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.88 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERsDQLGGQLRTAWLMpkrANFKAFVEFQSAA---------LTRLGATVVF- 466
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTKEI---ENYPGFPEGISGPelaerlreqAERFGAEILLe 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496250708 467 ----------NKNADAAGISAFGADRIVLATGSTTAALPVSG 498
Cdd:COG0492 78 evtsvdkddgPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPG 119
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
397-436 |
4.61e-05 |
|
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 46.16 E-value: 4.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERS--------DQLGGQLRT 436
Cdd:COG0686 170 KVVILGGGVVGTNAARMALGLGADVTVLDINldrlrrldDIFGGRVTT 217
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
397-436 |
5.46e-05 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 45.86 E-value: 5.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERS--------DQLGGQLRT 436
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINlerlryldDIFGGRVTT 217
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
387-438 |
5.51e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 46.25 E-value: 5.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 496250708 387 PEALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQlrTAW 438
Cdd:PRK06134 4 AAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT--TAW 53
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
399-431 |
8.80e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 45.43 E-value: 8.80e-05
10 20 30
....*....|....*....|....*....|...
gi 496250708 399 LVVGGGPAGLEAARVAAALGHEVTLWERSDQLG 431
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
386-467 |
9.58e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.39 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 386 EPEALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQL-------RtawlMPKranfKAFVEFQSAALT 458
Cdd:PRK12831 131 DLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLvygipefR----LPK----ETVVKKEIENIK 202
|
....*....
gi 496250708 459 RLGATVVFN 467
Cdd:PRK12831 203 KLGVKIETN 211
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
395-505 |
1.01e-04 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 45.13 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 395 TRKVLVVGGGPAGLEAARVAAALGH--EVTL--------WER---SDQLGGQLRTAWLMPKRANFkafveFQSAALT-RL 460
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPdgEITVigaephppYNRpplSKVLAGETDEEDLLLRPADF-----YEENGIDlRL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 496250708 461 GATVV----FNKNADAAGISAFGADRIVLATGSTTAALPVSGNGP--VFTL 505
Cdd:COG1251 76 GTRVTaidrAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLpgVFTL 126
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
396-437 |
1.22e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.88 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTA 437
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTV 46
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
395-441 |
1.34e-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: 44.54 E-value: 1.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 496250708 395 TRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTAWLMP 441
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSP 49
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
362-501 |
1.44e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 45.21 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 362 GMLERNLPIR-CLINPIAGL--EGRFDepealPRGATRK--VLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:PRK12779 273 GQLEWYLPQHeKLVNPNANErfAGRIS-----PWAAAVKppIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRY 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496250708 437 AwlMPKRANFKAFVEFQSAALTRLGATVVFN----KNADAAGISAFGADRIVLATGsttAALPVSGNGP 501
Cdd:PRK12779 348 G--IPEFRLPNQLIDDVVEKIKLLGGRFVKNfvvgKTATLEDLKAAGFWKIFVGTG---AGLPTFMNVP 411
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
397-451 |
1.51e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 43.64 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERS--------DQLGGQlrtaWLMPKRANFKAFVE 451
Cdd:pfam01262 30 KVLVIGGGVAGLNAAATAKGLGAIVTILDVRparleqleSILGAK----FVETLYSQAELIAE 88
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
388-435 |
1.55e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 44.76 E-value: 1.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 496250708 388 EALPRGatRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLR 435
Cdd:PRK13984 278 EPEKKN--KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMR 323
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
386-488 |
1.75e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.40 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 386 EPEALPRgatrKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG--------QLRTawLMPKRANFKAFVEFQSAAL 457
Cdd:PRK06292 164 ELDKLPK----SLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPledpevskQAQK--ILSKEFKIKLGAKVTSVEK 237
|
90 100 110
....*....|....*....|....*....|.
gi 496250708 458 TRLGATVVFNKNADAagiSAFGADRIVLATG 488
Cdd:PRK06292 238 SGDEKVEELEKGGKT---ETIEADYVLVATG 265
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
384-438 |
1.85e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.73 E-value: 1.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 496250708 384 FDEPEALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQlrTAW 438
Cdd:PRK12843 5 VSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT--TAT 57
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
374-443 |
3.86e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 43.67 E-value: 3.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 374 INPIAGLEGRFDEPeaLPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERsdqlggqlRTAWLMPKR 443
Cdd:PRK12779 428 VNLMRGLDDDYETP--LPEVKGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYR--------RTKSEMPAR 487
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
382-495 |
4.65e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.58 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 382 GRFDEPEALPRGAtRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRTA---WLMPKRAnfkAFVEFQSaaLT 458
Cdd:PRK12778 419 GNISVPEVAEKNG-KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGipeFRLPKKI---VDVEIEN--LK 492
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 496250708 459 RLGAT----VVFNKNADAAGISAFGADRIVLATGsttAALP 495
Cdd:PRK12778 493 KLGVKfetdVIVGKTITIEELEEEGFKGIFIASG---AGLP 530
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
398-436 |
6.57e-04 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 42.75 E-value: 6.57e-04
10 20 30
....*....|....*....|....*....|....*....
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT 41
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
398-467 |
6.94e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 42.31 E-value: 6.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERSDqLGGQLRTAWLMPKRANFKAFVEFQSAALTRLGATVVFN 467
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKS-FPRYKPCGGALSPRALEELDLPGELIVNLVRGARFFSP 71
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
396-432 |
9.40e-04 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 41.90 E-value: 9.40e-04
10 20 30
....*....|....*....|....*....|....*..
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:PRK12770 19 KKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGG 55
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
397-451 |
1.30e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 41.61 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLG--------GQLRTAWLMPKRANFKAFVE 451
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLEPSELARLAL 63
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
396-436 |
2.18e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 41.39 E-value: 2.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:PLN02976 694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYT 734
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
396-457 |
3.18e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 40.60 E-value: 3.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496250708 396 RKVLVVGGGPAGLEAA---RVAAaLGHEVTLWERSDQLGGQLRTAwlmpKRANF------KAFVEFQSAAL 457
Cdd:PRK11883 1 KKVAIIGGGITGLSAAyrlHKKG-PDADITLLEASDRLGGKIQTV----RKDGFpielgpESFLARKPSAP 66
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
394-431 |
3.55e-03 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 40.41 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 496250708 394 ATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLG 431
Cdd:PRK08163 3 KVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
396-485 |
3.63e-03 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 40.45 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERsdqlggqlrtawlmpkranfKAFVEFQSAALTRLGATVVFNKNADAAgi 475
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDD--------------------RPAPELAAAELEAPGVEVVLGEHPEEL-- 62
|
90
....*....|
gi 496250708 476 sAFGADRIVL 485
Cdd:COG0771 63 -LDGADLVVK 71
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
398-432 |
3.83e-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: 40.23 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|....*
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
|
|
| AdhP |
COG1064 |
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
393-492 |
3.94e-03 |
|
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];
Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 40.10 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 393 GATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQlggqlrtawlmpKRAnfkafvefqsAALtRLGATVVFN-KNAD 471
Cdd:COG1064 161 GPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPE------------KLE----------LAR-ELGADHVVNsSDED 217
|
90 100
....*....|....*....|...
gi 496250708 472 AAG--ISAFGADRIVLATGSTTA 492
Cdd:COG1064 218 PVEavRELTGADVVIDTVGAPAT 240
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
397-423 |
4.06e-03 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 39.84 E-value: 4.06e-03
10 20
....*....|....*....|....*..
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTL 423
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLL 27
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
397-432 |
4.29e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.53 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|....*.
gi 496250708 397 KVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:PTZ00306 411 RVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
392-478 |
4.84e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 40.20 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496250708 392 RGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGGQlrTAW-----LMPKRANFKA--FVEFQSAALTRLGATV 464
Cdd:PRK12839 5 MTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGA--TAWsggwmWTPGNSLARAdgVVEDKEEPRTYLEHRL 82
|
90
....*....|....
gi 496250708 465 vfNKNADAAGISAF 478
Cdd:PRK12839 83 --GENYDADKVDAL 94
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
393-436 |
5.37e-03 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 40.00 E-value: 5.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 496250708 393 GATRKVLVVGGGPAGLEAA-RVAAALGHEVTLWERSDQLGGQLRT 436
Cdd:PLN02576 10 ASSKDVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNITS 54
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
387-432 |
8.69e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 39.29 E-value: 8.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496250708 387 PEALPRGATRKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:PRK12842 1 EECMTNELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
398-432 |
9.06e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 38.98 E-value: 9.06e-03
10 20 30
....*....|....*....|....*....|....*
gi 496250708 398 VLVVGGGPAGLEAARVAAALGHEVTLWERSDQLGG 432
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
394-436 |
9.11e-03 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 38.94 E-value: 9.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 496250708 394 ATRKVLVVGGGPAGLEAARVAAALgHEVTLWERSDQLGGQLRT 436
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGGHTHT 43
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
396-430 |
9.59e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 39.03 E-value: 9.59e-03
10 20 30
....*....|....*....|....*....|....*
gi 496250708 396 RKVLVVGGGPAGLEAARVAAALGHEVTLWERSDQL 430
Cdd:PRK06370 172 EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL 206
|
|
| |
