|
Name |
Accession |
Description |
Interval |
E-value |
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
4-339 |
0e+00 |
|
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: 617.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEPLH 83
Cdd:cd02932 1 LFTPLTLRGVTLKNRIVVSPMCQYSAEDGVATDWHLVHYGSRALGGAGLVIVEATAVSPEGRITPGDLGLWNDEQIEALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 RITRFIESQGAVAGVQLAHAGRKASTWRPWLGKHGSVPIGDGGWIPVAPSAIPFDPQHTTPEALSEAQIEALVQAFVRAA 163
Cdd:cd02932 81 RIVDFIHSQGAKIGIQLAHAGRKASTAPPWEGGGPLLPPGGGGWQVVAPSAIPFDEGWPTPRELTREEIAEVVDAFVAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 164 ERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDGWNP 243
Cdd:cd02932 161 RRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAVRAVWPEDKPLFVRISATDWVEGGWDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 244 DETVELARHLKDLGVDLIDVSSGGTAANAEIPVGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQADLILLA 323
Cdd:cd02932 241 EDSVELAKALKELGVDLIDVSSGGNSPAQKIPVGPGYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALG 320
|
330
....*....|....*.
gi 489204771 324 RELLRDPYWPLHAADE 339
Cdd:cd02932 321 RELLRNPYWPLHAAAE 336
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-354 |
2.12e-165 |
|
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: 466.57 E-value: 2.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 1 MSLLFEPLSLRQITLPNRIAVSPMCQYSAQE-GLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHV 79
Cdd:COG1902 4 MPKLFSPLTLGGLTLKNRIVMAPMTRGRADEdGVPTDLHAAYYAQRARGGAGLIITEATAVSPEGRGYPGQPGIWDDEQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 80 EPLHRITRFIESQGAVAGVQLAHAGRKASTWRPwlgkhgsvpigdGGWIPVAPSAIPFDPQHTTPEALSEAQIEALVQAF 159
Cdd:COG1902 84 AGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLP------------GGWPPVAPSAIPAPGGPPTPRALTTEEIERIIEDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 160 VRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVED 239
Cdd:COG1902 152 AAAARRAKEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAVRAAVGPDFPVGVRLSPTDFVEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 240 GWNPDETVELARHLKDLGVDLIDVSSGGTAANAEIP--VGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQA 317
Cdd:COG1902 232 GLTLEESVELAKALEEAGVDYLHVSSGGYEPDAMIPtiVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489204771 318 DLILLARELLRDPYWPLHAADELRNEQMP-------WPPQYLRA 354
Cdd:COG1902 312 DLVALGRPLLADPDLPNKAAAGRGDEIRPcigcnqcLPTFYGGA 355
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
2-354 |
6.97e-161 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 454.16 E-value: 6.97e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 2 SLLFEPLSLRQITLPNRIAVSPMCQYSAQE--GLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHV 79
Cdd:PRK13523 1 SKLFSPYTIKDVTLKNRIVMSPMCMYSSENkdGKVTNFHLIHYGTRAAGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 80 EPLHRITRFIESQGAVAGVQLAHAGRKASTwrpwlgkhgsvpIGDggwiPVAPSAIPFDPQHTTPEALSEAQIEALVQAF 159
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAGRKAEL------------EGD----IVAPSAIPFDEKSKTPVEMTKEQIKETVLAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 160 VRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWpqELPLFVRLSATDWVED 239
Cdd:PRK13523 145 KQAAVRAKEAGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIIDAVKEVW--DGPLFVRISASDYHPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 240 GWNPDETVELARHLKDLGVDLIDVSSGGTaANAEIPVGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQADL 319
Cdd:PRK13523 223 GLTVQDYVQYAKWMKEQGVDLIDVSSGAV-VPARIDVYPGYQVPFAEHIREHANIATGAVGLITSGAQAEEILQNNRADL 301
|
330 340 350
....*....|....*....|....*....|....*
gi 489204771 320 ILLARELLRDPYWPLHAADELrNEQMPWPPQYLRA 354
Cdd:PRK13523 302 IFIGRELLRNPYFPRIAAKEL-GFEIEAPKQYERA 335
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
4-362 |
9.96e-144 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 425.51 E-value: 9.96e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEPLH 83
Cdd:PRK08255 399 MFTPFRLRGLTLKNRVVVSPMAMYSAVDGVPGDFHLVHLGARALGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEAAWK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 RITRFIESQG-AVAGVQLAHAGRKASTWRPWLGKhgSVPIGDGGWIPVAPSAIPFDPQHTTPEALSEAQIEALVQAFVRA 162
Cdd:PRK08255 479 RIVDFVHANSdAKIGIQLGHSGRKGSTRLGWEGI--DEPLEEGNWPLISASPLPYLPGSQVPREMTRADMDRVRDDFVAA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 163 AERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDGWN 242
Cdd:PRK08255 557 ARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFRAVRAVWPAEKPMSVRISAHDWVEGGNT 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 243 PDETVELARHLKDLGVDLIDVSSGGTAAnAEIPV-GPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQADLIL 321
Cdd:PRK08255 637 PDDAVEIARAFKAAGADLIDVSSGQVSK-DEKPVyGRMYQTPFADRIRNEAGIATIAVGAISEADHVNSIIAAGRADLCA 715
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489204771 322 LARELLRDPYWPLHAADELRNEQMPWPPQYLraAHRSTPPR 362
Cdd:PRK08255 716 LARPHLADPAWTLHEAAEIGYRDVAWPKQYL--AGKRQLER 754
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
5-338 |
2.96e-120 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 350.72 E-value: 2.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 5 FEPLSLRQITLPNRIAVSPMC-QYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEPLH 83
Cdd:cd02803 1 FSPIKIGGLTLKNRIVMAPMTeNMATEDGTPTDELIEYYEERAKGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 RITRFIESQGAVAGVQLAHAGRKAStwRPWLGKHgsvpigdggwiPVAPSAIPFDPQHTTPEALSEAQIEALVQAFVRAA 163
Cdd:cd02803 81 KLTEAVHAHGAKIFAQLAHAGRQAQ--PNLTGGP-----------PPAPSAIPSPGGGEPPREMTKEEIEQIIEDFAAAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 164 ERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDGWNP 243
Cdd:cd02803 148 RRAKEAGFDGVEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIVAAVREAVGPDFPVGVRLSADDFVPGGLTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 244 DETVELARHLKDLGVDLIDVSSGGTAANAEI----PVGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQADL 319
Cdd:cd02803 228 EEAIEIAKALEEAGVDALHVSGGSYESPPPIipppYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADL 307
|
330
....*....|....*....
gi 489204771 320 ILLARELLRDPYWPLHAAD 338
Cdd:cd02803 308 VALGRALLADPDLPNKARE 326
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
4-333 |
2.45e-81 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 251.99 E-value: 2.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQE--GLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEP 81
Cdd:pfam00724 2 LFEPIKIGNTTLKNRIVMAPMTRLRSLDdgTKATGLLAEYYSQRSRGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 82 LHRITRFIESQGAVAGVQLAHAGRKA-STWRPWLGKHGSVPIGDGGwipvAPSAIPFDPQHttpeALSEAQIEALVQAFV 160
Cdd:pfam00724 82 WRKLTEAVHKNGSKAGVQLWHLGREApMEYRPDLEVDGPSDPFALG----AQEFEIASPRY----EMSKEEIKQHIQDFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 161 RAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDG 240
Cdd:pfam00724 154 DAAKRAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVDAVKEAVGQERIVGYRLSPFDVVGPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 241 WNPDETVELARHLKDLGVDLIDVSSGGTA-ANAEIPVGPG----YQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTG 315
Cdd:pfam00724 234 LDFAETAQFIYLLAELGVRLPDGWHLAYIhAIEPRPRGAGpvrtRQQHNTLFVKGVWKGPLITVGRIDDPSVAAEIVSKG 313
|
330
....*....|....*...
gi 489204771 316 QADLILLARELLRDPYWP 333
Cdd:pfam00724 314 RADLVAMGRPFLADPDLP 331
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
4-331 |
2.36e-78 |
|
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: 244.06 E-value: 2.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEPLH 83
Cdd:cd04734 1 LLSPLQLGHLTLRNRIVSTAHATNYAEDGLPSERYIAYHEERARGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIPGFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 RITRFIESQGAVAGVQLAHAGRKAStwrpwlgkhgsvpiGDGGWIPV-APSAIPFDPQHTTPEALSEAQIEALVQAFVRA 162
Cdd:cd04734 81 RLAEAVHAHGAVIMIQLTHLGRRGD--------------GDGSWLPPlAPSAVPEPRHRAVPKAMEEEDIEEIIAAFADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 163 AERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDGWN 242
Cdd:cd04734 147 ARRCQAGGLDGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLAAVRAAVGPDFIVGIRISGDEDTEGGLS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 243 PDETVELARHLKDLG-VDLIDVSSGGTAANAE----IP---VGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRT 314
Cdd:cd04734 227 PDEALEIAARLAAEGlIDYVNVSAGSYYTLLGlahvVPsmgMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAEQALAA 306
|
330
....*....|....*..
gi 489204771 315 GQADLILLARELLRDPY 331
Cdd:cd04734 307 GHADMVGMTRAHIADPH 323
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
4-343 |
2.30e-67 |
|
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: 216.38 E-value: 2.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMcqYSAQEGLANDWHLVHL--GSRAVGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEP 81
Cdd:cd02930 1 LLSPLDLGFTTLRNRVLMGSM--HTGLEELDDGIDRLAAfyAERARGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 82 LHRITRFIESQGAVAGVQLAHAGRKAstwrpwlgKHGsvpigdggwIPVAPSAIPFDPQHTTPEALSEAQIEALVQAFVR 161
Cdd:cd02930 79 HRLITDAVHAEGGKIALQILHAGRYA--------YHP---------LCVAPSAIRAPINPFTPRELSEEEIEQTIEDFAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 162 AAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATDWVEDGW 241
Cdd:cd02930 142 CAALAREAGYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIVRAVRAAVGEDFIIIYRLSMLDLVEGGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 242 NPDETVELARHLKDLGVDLIDVSSGGtaANAEIP-----VGPGYQTEFAERVKKEAGIASGTVGMITEPVQAEHILRTGQ 316
Cdd:cd02930 222 TWEEVVALAKALEAAGADILNTGIGW--HEARVPtiatsVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGD 299
|
330 340
....*....|....*....|....*..
gi 489204771 317 ADLILLARELLRDPYWPLHAADELRNE 343
Cdd:cd02930 300 ADMVSMARPFLADPDFVAKAAAGRADE 326
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
4-343 |
5.87e-66 |
|
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: 212.46 E-value: 5.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQ-ITLPNRIAVSPMCQYSA-QEGLANDWHLVHLGSRAvGGAGLVIVEATAVLPEGRITADDLGIWSDAHVEP 81
Cdd:cd04735 1 LFEPFTLKNgVTLKNRFVMAPMTTYSSnPDGTITDDELAYYQRRA-GGVGMVITGATYVSPSGIGFEGGFSADDDSDIPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 82 LHRITRFIESQGAVAGVQLAHAGRKAStwrPWLGKHGSVpigdggwipVAPSAI-PFDPQHTTPEALSEAQIEALVQAFV 160
Cdd:cd04735 80 LRKLAQAIKSKGAKAILQIFHAGRMAN---PALVPGGDV---------VSPSAIaAFRPGAHTPRELTHEEIEDIIDAFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 161 RAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQEL-PLFV---RLSATDW 236
Cdd:cd04735 148 EATRRAIEAGFDGVEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHAdKDFIlgyRFSPEEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 237 VEDGWNPDETVELARHLKDLGVDLIDVSSGGTAANAeiPVGPGYQTEFAERVKKEAG-----IASGTvgmITEPVQAEHI 311
Cdd:cd04735 228 EEPGIRMEDTLALVDKLADKGLDYLHISLWDFDRKS--RRGRDDNQTIMELVKERIAgrlplIAVGS---INTPDDALEA 302
|
330 340 350
....*....|....*....|....*....|..
gi 489204771 312 LRTGqADLILLARELLRDPYWPLHAADELRNE 343
Cdd:cd04735 303 LETG-ADLVAIGRGLLVDPDWVEKIKEGREDE 333
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
4-333 |
3.27e-63 |
|
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: 205.13 E-value: 3.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQ-ITLPNRIAVSPMcqysaQEGLANDWH-----LVHLGSR-AVGGAGLVI-----VEATAvlPEGRITADDL 71
Cdd:cd04733 1 LGQPLTLPNgATLPNRLAKAAM-----SERLADGRGlptpeLIRLYRRwAEGGIGLIItgnvmVDPRH--LEEPGIIGNV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 72 GIWSDAHVEPLHRITRFIESQGAVAGVQLAHAGRKASTwrpwlgkhgsvPIGDGgwiPVAPSAIPF----DPQHTTPEAL 147
Cdd:cd04733 74 VLESGEDLEAFREWAAAAKANGALIWAQLNHPGRQSPA-----------GLNQN---PVAPSVALDpgglGKLFGKPRAM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 148 SEAQIEALVQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPL 227
Cdd:cd04733 140 TEEEIEDVIDRFAHAARLAQEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARLLLEIYDAIRAAVGPGFPV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 228 FVRLSATDWVEDGWNPDETVELARHLKDLGVDLIDVsSGGT--------AANAEIPVGPGYQTEFAERVKKEAGIASGTV 299
Cdd:cd04733 220 GIKLNSADFQRGGFTEEDALEVVEALEEAGVDLVEL-SGGTyespamagAKKESTIAREAYFLEFAEKIRKVTKTPLMVT 298
|
330 340 350
....*....|....*....|....*....|....
gi 489204771 300 GMITEPVQAEHILRTGQADLILLARELLRDPYWP 333
Cdd:cd04733 299 GGFRTRAAMEQALASGAVDGIGLARPLALEPDLP 332
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
4-320 |
2.40e-61 |
|
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: 200.01 E-value: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPM--CQySAQEGLANDWHLVHLGSRAvgGAGLVIVEATAVLPEGRITADDLGIWSDAHVEP 81
Cdd:cd02933 2 LFSPLKLGNLTLKNRIVMAPLtrSR-ADPDGVPTDLMAEYYAQRA--SAGLIITEATQISPQGQGYPNTPGIYTDEQVEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 82 LHRITRFIESQGAVAGVQLAHAGRKAstwrpwlgkHGSVpIGDGGwIPVAPSAIPFDPQ---------HTTPEALSEAQI 152
Cdd:cd02933 79 WKKVTDAVHAKGGKIFLQLWHVGRVS---------HPSL-LPGGA-PPVAPSAIAAEGKvftpagkvpYPTPRALTTEEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 153 EALVQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELpLFVRLS 232
Cdd:cd02933 148 PGIVADFRQAARNAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVVDAVAEAIGADR-VGIRLS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 233 --ATDWVEDGWNPDETVE-LARHLKDLGVDLIDVSSGGTAANAEIPVGpgyqtEFAERVKKeagIASGTV---GMITePV 306
Cdd:cd02933 227 pfGTFNDMGDSDPEATFSyLAKELNKRGLAYLHLVEPRVAGNPEDQPP-----DFLDFLRK---AFKGPLiaaGGYD-AE 297
|
330
....*....|....
gi 489204771 307 QAEHILRTGQADLI 320
Cdd:cd02933 298 SAEAALADGKADLV 311
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
4-334 |
2.85e-47 |
|
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: 164.03 E-value: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVlpegritaDDLGIWSDAHVEPLH 83
Cdd:cd04747 1 LFTPFTLKGLTLPNRIVMAPMTRSFSPGGVPGQDVAAYYRRRAAGGVGLIITEGTAV--------DHPAASGDPNVPRFH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 ---------RITRFIESQGAVAGVQLAHAGrkaSTWRPWLGKHGSVPigdggwiPVAPSAIpFDPQHTTPEALSEAQIEA 154
Cdd:cd04747 73 gedalagwkKVVDEVHAAGGKIAPQLWHVG---AMRKLGTPPFPDVP-------PLSPSGL-VGPGKPVGREMTEADIDD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 155 LVQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSat 234
Cdd:cd04747 142 VIAAFARAAADARRLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVVKAIRAAVGPDFPIILRFS-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 235 DWVEDGW------NPDETVELARHLKDLGVDLIDVSSggtaANAEIPVGPGYQTEFAERVKKEAG---IASGTVGMITEP 305
Cdd:cd04747 220 QWKQQDYtarladTPDELEALLAPLVDAGVDIFHCST----RRFWEPEFEGSELNLAGWTKKLTGlptITVGSVGLDGDF 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489204771 306 VQAEHI---------------LRTGQADLILLARELLRDPYWPL 334
Cdd:cd04747 296 IGAFAGdegaspasldrllerLERGEFDLVAVGRALLSDPAWVA 339
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
3-333 |
1.32e-43 |
|
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis.The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine.
Pssm-ID: 239239 [Multi-domain] Cd Length: 370 Bit Score: 154.82 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 3 LLFEPLSLRQITLPNRIAVSPMCQ---YSAQEGLANdwhlvHLGSRAVGGAGLVIVEATAVLPEGRIT-ADDLGIWSDAH 78
Cdd:cd02929 7 ILFEPIKIGPVTARNRFYQVPHCNgmgYRKPSAQAA-----MRGIKAEGGWGVVNTEQCSIHPSSDDTpRISARLWDDGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 79 VEPLHRITRFIESQGAVAGVQLAHAGRKASTWRPWLgkhgsvpigdggwIPVAPSAIPFDPQH---TTPEALSEAQIEAL 155
Cdd:cd02929 82 IRNLAAMTDAVHKHGALAGIELWHGGAHAPNRESRE-------------TPLGPSQLPSEFPTggpVQAREMDKDDIKRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 156 VQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRLSATD 235
Cdd:cd02929 149 RRWYVDAALRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAVGDDCAVATRFSVDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 236 WVEDGWN--PDETVELARHLKDLgVDLIDVSSGGTAANAE-IPVGP-GYQTEFAERVKKEAGIASGTVGMITEPVQAEHI 311
Cdd:cd02929 229 LIGPGGIesEGEGVEFVEMLDEL-PDLWDVNVGDWANDGEdSRFYPeGHQEPYIKFVKQVTSKPVVGVGRFTSPDKMVEV 307
|
330 340
....*....|....*....|..
gi 489204771 312 LRTGQADLILLARELLRDPYWP 333
Cdd:cd02929 308 VKSGILDLIGAARPSIADPFLP 329
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
4-333 |
9.08e-43 |
|
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: 153.05 E-value: 9.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPM--CQYSAQEGLANDWHLVHLGSRAVGGAGLVIVEATAVlpEGRITADDLGIWSDAHVEP 81
Cdd:cd02931 1 LFEPIKIGKVEIKNRFAMAPMgpLGLADNDGAFNQRGIDYYVERAKGGTGLIITGVTMV--DNEIEQFPMPSLPCPTYNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 82 LHRI------TRFIESQGAVAGVQL-AHAGRKastwrpwlgkhgSVPIGDGGWIPVAPSAIP--FDPQHTTPEaLSEAQI 152
Cdd:cd02931 79 TAFIrtakemTERVHAYGTKIFLQLtAGFGRV------------CIPGFLGEDKPVAPSPIPnrWLPEITCRE-LTTEEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 153 EALVQAFVRAAERSLAAGFKVAEVHAAH-GYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQELPLFVRL 231
Cdd:cd02931 146 ETFVGKFGESAVIAKEAGFDGVEIHAVHeGYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEEIKARCGEDFPVSLRY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 232 SATDWVED--------------GWNPDETVELARHLKDLGVDLIDVSSGGTAA--NAEIPV--GPGYQTEFAERVKKEAG 293
Cdd:cd02931 226 SVKSYIKDlrqgalpgeefqekGRDLEEGLKAAKILEEAGYDALDVDAGSYDAwyWNHPPMyqKKGMYLPYCKALKEVVD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489204771 294 IASGTVGMITEPVQAEHILRTGQADLILLARELLRDPYWP 333
Cdd:cd02931 306 VPVIMAGRMEDPELASEAINEGIADMISLGRPLLADPDVV 345
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
4-224 |
1.70e-42 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 151.80 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQE------GLANDWHlvhlgsRAVGGAGLVIVEATAVLPEGRITADDLGIWSDA 77
Cdd:PRK10605 3 LFSPLKVGAITAPNRVFMAPLTRLRSIEpgdiptPLMAEYY------RQRASAGLIISEATQISAQAKGYAGAPGLHSPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 78 HVEPLHRITRFIESQGAVAGVQLAHAGRKAstwrpwlgkHGSVPigDGGWIPVAPSAIPFDP--------------QHTT 143
Cdd:PRK10605 77 QIAAWKKITAGVHAEGGHIAVQLWHTGRIS---------HASLQ--PGGQAPVAPSAINAGTrtslrdengqairvETST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 144 PEALSEAQIEALVQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKAWPQ 223
Cdd:PRK10605 146 PRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAGIAEWGA 225
|
.
gi 489204771 224 E 224
Cdd:PRK10605 226 D 226
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
4-220 |
2.01e-29 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 116.88 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 4 LFEPLSLRQITLPNRIAVSPMCQYSAQEGLANDWHLVHLGSRAVGGaGLVIVEATAVLPEGRITADDLGIWSDAHVEPLH 83
Cdd:PLN02411 12 LFSPYKMGRFDLSHRVVLAPMTRCRALNGIPNAALAEYYAQRSTPG-GFLISEGTLISPTAPGFPHVPGIYSDEQVEAWK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 84 RITRFIESQGAVAGVQLAHAGRKA-STWRPwlgkHGSVPIGDGG------WIPVAPsaipfDPQHTT---PEALSEAQIE 153
Cdd:PLN02411 91 KVVDAVHAKGSIIFCQLWHVGRAShQVYQP----GGAAPISSTNkpiserWRILMP-----DGSYGKypkPRALETSEIP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489204771 154 ALVQAFVRAAERSLAAGFKVAEVHAAHGYLLHQFLSPLSNQRRDQYGGCFENRIRLLLQVTAAVRKA 220
Cdd:PLN02411 162 EVVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQAVVSA 228
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
247-289 |
1.99e-03 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 40.01 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489204771 247 VELARHLKDLGVDLIdvSSGGTA---ANAEIPVgpgyqTE------FAE----RVK 289
Cdd:COG0138 17 VEFARALVELGVEII--STGGTAkalREAGIPV-----TEvsevtgFPEildgRVK 65
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
152-324 |
2.74e-03 |
|
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: 38.72 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 152 IEALVQAFVRAAERSLAAGFKVAEVHAAHGYllhqflsplsnqrrdqyggcfenRIRLLLQVTAAVRKAWPqELPLFVRL 231
Cdd:cd04722 66 INDAAAAVDIAAAAARAAGADGVEIHGAVGY-----------------------LAREDLELIRELREAVP-DVKVVVKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 232 SATDwvedgwnpdetVELARHLKDLGVDLIDVSSGGTAANAEIPVGPgyQTEFAERVKKEAGIASGTVGMITEPVQAEHI 311
Cdd:cd04722 122 SPTG-----------ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPI--ADLLLILAKRGSKVPVIAGGGINDPEDAAEA 188
|
170
....*....|...
gi 489204771 312 LRTGqADLILLAR 324
Cdd:cd04722 189 LALG-ADGVIVGS 200
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
247-276 |
3.27e-03 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 39.30 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|...
gi 489204771 247 VELARHLKDLGVDLIdvSSGGTA---ANAEIPV 276
Cdd:PRK00881 18 VEFAKALVELGVEIL--STGGTAkllAEAGIPV 48
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
156-322 |
4.61e-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: 38.65 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 156 VQAFVRAAERSLAAGFKVAEVHAAHGYLlhqflsplsnqRRDqyggcfENRIRlllqvtaAVRKAWPQELPLFVrlsatd 235
Cdd:COG4948 138 PEEMAEEAREAVARGFRALKLKVGGPDP-----------EED------VERVR-------AVREAVGPDARLRV------ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204771 236 wveD---GWNPDETVELARHLKDLGVDLIdvssggtaanaEIPVGPGYQTEFAErVKKEAG--IASGTVgmITEPVQAEH 310
Cdd:COG4948 188 ---DangAWTLEEAIRLLRALEDLGLEWI-----------EQPLPAEDLEGLAE-LRRATPvpIAADES--LTSRADFRR 250
|
170
....*....|..
gi 489204771 311 ILRTGQADLILL 322
Cdd:COG4948 251 LIEAGAVDIVNI 262
|
|
| |
