|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06481 |
PRK06481 |
flavocytochrome c; |
442-924 |
0e+00 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 442 AISGATSQSEAVKKAVAKAMLKSSKALAAEEGGNDAAPK----SYDVVVVGSGGAGLAAAIQAHDEGASVLIVEKMPTIG 517
Cdd:PRK06481 18 ILVGCGSNTTSKSDSSSSKESEKTEVTSGASKTSYTDPSelkdKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 518 GNTIKASAGMNAAETRFQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSID 597
Cdd:PRK06481 98 GNTMKASSGMNASETKFQKAQGIADSNDKFYEETLKGGGGTNDKALLRYFVDNSASAIDWLDSMGIKLDNLTITGGMSEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 598 RTHRPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSANSAMV 677
Cdd:PRK06481 178 RTHRPHDGSAVGGYLVDGLLKNVQERKIPLFVNADVTKITEKDGKVTGVKVKINGKETKTISSKAVVVTTGGFGANKDMI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 678 VKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRD 757
Cdd:PRK06481 258 AKYRPDLKGYVTTNQEGSTGDGIKMIEKLGGTTVDMDQIQIHPTVQQSKSYLIGEAVRGEGAILVNQKGKRFGNELDTRD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 758 KVSAAIIALPEHYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRT 837
Cdd:PRK06481 338 KVSAAINKLPEKYAYVVFDSGVKDRVKAIAQYEEKGFVEEGKTIDELAKKINVPAETLTKTLDTWNKAVKNKKDEAFGRT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 838 TALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGH 917
Cdd:PRK06481 418 TGMDNDLSTGPYYAIKIAPGIHYTMGGVKINTNTEVLKKDGSPITGLYAAGEVTGGLHGENRIGGNSVADIIIFGRQAGT 497
|
....*..
gi 802145477 918 QAAKRAR 924
Cdd:PRK06481 498 QSAEFAK 504
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
7-360 |
8.52e-164 |
|
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: 482.48 E-value: 8.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLPNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGL 86
Cdd:cd04735 1 LFEPFTLKNGVTLKNRFVMAPMTTYSSNPDGTITDDELAYYQRRAGGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 87 AKIAEAIKAEGSKAILQIYHGGRMVDPQLIGGRQPVAPSAVAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDG 166
Cdd:cd04735 81 RKLAQAIKSKGAKAILQIFHAGRMANPALVPGGDVVSPSAIAAFRPGAHTPRELTHEEIEDIIDAFGEATRRAIEAGFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 167 VEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDITHKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYL 246
Cdd:cd04735 161 VEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHADKDFILGYRFSPEEPEEPGIRMEDTLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 247 LEKLAARGVDYLHFSVGATLRPSIVDtSDPTPLIEKYCAMRSDtlAQVPVMGVGGVVNAADAEQGLDHGYDLIAVGRACI 326
Cdd:cd04735 241 VDKLADKGLDYLHISLWDFDRKSRRG-RDDNQTIMELVKERIA--GRLPLIAVGSINTPDDALEALETGADLVAIGRGLL 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 802145477 327 AYPDWASRIAAGEELE--LFIDSTQREALHIPEPLW 360
Cdd:cd04735 318 VDPDWVEKIKEGREDEinLEIDPDDLEELKIPPALW 353
|
|
| flavo_cyto_c |
TIGR01813 |
flavocytochrome c; This model describes a family of redox proteins related to the succinate ... |
498-916 |
1.62e-156 |
|
flavocytochrome c; This model describes a family of redox proteins related to the succinate dehydrogenases and fumarate reductases of E. coli, mitochondria, and other well-characterized systems. A member of this family from Shewanella frigidimarina NCIMB400 is characterized as a water-soluble periplasmic protein with four heme groups, a non-covalently bound FAD, and essentially unidirectional fumarate reductase activity. At least seven distinct members of this family are found in Shewanella oneidensis, a species able to use a wide variety of pathways for respiraton. [Energy metabolism, Electron transport]
Pssm-ID: 273816 [Multi-domain] Cd Length: 439 Bit Score: 466.82 E-value: 1.62e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEG-ASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIE 576
Cdd:TIGR01813 16 LSAKKAGaANVVLLEKMPVIGGNSAIAAGGMNAAGTDQQKALGIEDSPELFIKDTLKGGRGINDPELVRILAEESKDAVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 577 WLADR-GIMLNDITTTGGMSIDRTHRPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGD-EVSGVRLINDEKE 654
Cdd:TIGR01813 96 WLQDGvGARLDDLIQLGGHSVPRAHRPTGGAASGAEIVQTLYKKAKKEGIDTRLNSKVEDLIQDDQgSVVGVVVKGKGKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 655 VIEVQTKSIVVATGGFSANSAMVVKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQ-QTSYLISES 733
Cdd:TIGR01813 176 IYIKAAKAVVLATGGFGSNKEMIAKYDPTLKHLGSTNQPGATGDGLLMAEKIGAALVDMDYIQAHPTASPdEGGFLISEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 734 IRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYH 813
Cdd:TIGR01813 256 VRGYGAILVNKTGERFMNELATRDKVSDAILAQPGKDAYLIFDDDVYKKAKMVDNYYRLGVAYKGDSLEELAKQFGIPAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 814 AFLATLECYNGAVEKQHDEQFGRTTALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGG 893
Cdd:TIGR01813 336 ALKQTIKDYNGYVASGKDTPFGRPMDMPTDLSKAPYYAIKVTPGVHHTMGGVKINTKAEVLDANGKPIPGLFAAGEVTGG 415
|
410 420
....*....|....*....|...
gi 802145477 894 IHGGNRIGGNAVADIIIFGTLAG 916
Cdd:TIGR01813 416 VHGANRLGGNAIADCIVFGRIAG 438
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
498-925 |
2.03e-151 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 453.91 E-value: 2.03e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGiEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEW 577
Cdd:COG1053 20 LEAAEAGLKVLVLEKVPPRGGHTAAAQGGINAAGTNVQKAAG-EDSPEEHFYDTVKGGDGLADQDLVEALAEEAPEAIDW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 578 LADRGIMLN-----DITTTGGMSIDRTHRPRDGSavGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDE 652
Cdd:COG1053 99 LEAQGVPFSrtpdgRLPQFGGHSVGRTCYAGDGT--GHALLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVVARDRT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 653 KEVIEVQTKSIVVATGGFSANSAMVVKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISE 732
Cdd:COG1053 177 GEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEGALSTNAPGNTGDGIAMALRAGAALADMEFVQFHPTGLPGDGGLISE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 733 SIRGG-GAILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHVRaknKAADEYIAKGFVTSASSPRELAEKLGMD 811
Cdd:COG1053 257 GARGKpGGILVNKEGERFMNEYAPRDVVSRAILEEIDEPAYLVLDLRHR---RRLEEYLEAGYLVKADTIEELAAKLGID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 812 YHAFLATLECYNGAVEKQHDEqfgRTTALRaPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVV 891
Cdd:COG1053 334 AAELAATVARYNAAAKAGVDP---RGTCLG-PIKEGPFYAIPVRPGVHYTMGGLRVDADARVLDADGTPIPGLYAAGEAA 409
|
410 420 430
....*....|....*....|....*....|....
gi 802145477 892 GGIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG 925
Cdd:COG1053 410 GSVHGANRLGGNSLGDALVFGRIAGRHAAEYAKA 443
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-343 |
1.54e-116 |
|
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: 360.25 E-value: 1.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 1 MTSNERILQPFTLpNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDN 79
Cdd:COG1902 1 MMKMPKLFSPLTL-GGLTLKNRIVMAPMTRGRADEDGVPTDLHAAYYAQRArGGAGLIITEATAVSPEGRGYPGQPGIWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 80 DEKIAGLAKIAEAIKAEGSKAILQIYHGGRMVDPQLIGGRQPVAPSAVAAPrEGAAMPRALSGEEVEGMIAKFGDGVRRA 159
Cdd:COG1902 80 DEQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGGWPPVAPSAIPAP-GGPPTPRALTTEEIERIIEDFAAAARRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 160 ILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDIThkmaRQYADDAFIIGYRFSPEEMEVPGIR 239
Cdd:COG1902 159 KEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEAV----RAAVGPDFPVGVRLSPTDFVEGGLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 240 FDDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTSDP----------------TPLIekyCAMRSDTLAQvpvmgvggvv 303
Cdd:COG1902 235 LEESVELAKALEEAGVDYLHVSSGGYEPDAMIPTIVPegyqlpfaarirkavgIPVI---AVGGITTPEQ---------- 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 802145477 304 naadAEQGLDHGY-DLIAVGRACIAYPDWASRIAAGEELEL 343
Cdd:COG1902 302 ----AEAALASGDaDLVALGRPLLADPDLPNKAAAGRGDEI 338
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
8-338 |
5.85e-96 |
|
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: 304.88 E-value: 5.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 8 LQPFTLpNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGL 86
Cdd:cd02803 1 FSPIKI-GGLTLKNRIVMAPMTENMATEDGTPTDELIEYYEERAkGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 87 AKIAEAIKAEGSKAILQIYHGGRMVDPqLIGGRQPVAPSAVAAPREGAaMPRALSGEEVEGMIAKFGDGVRRAILAGFDG 166
Cdd:cd02803 80 RKLTEAVHAHGAKIFAQLAHAGRQAQP-NLTGGPPPAPSAIPSPGGGE-PPREMTKEEIEQIIEDFAAAARRAKEAGFDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 167 VEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLdithKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYL 246
Cdd:cd02803 158 VEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIV----AAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 247 LEKLAARGVDYLHFSVGATLRP-SIVDTSDPTPLIEKYCAMRSDTLAQVPVMGVGGVVNAADAEQGLDHGY-DLIAVGRA 324
Cdd:cd02803 234 AKALEEAGVDALHVSGGSYESPpPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKaDLVALGRA 313
|
330
....*....|....
gi 802145477 325 CIAYPDWASRIAAG 338
Cdd:cd02803 314 LLADPDLPNKAREG 327
|
|
| OYE_like_FMN |
cd02933 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
7-341 |
4.55e-81 |
|
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: 265.49 E-value: 4.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLPNgTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARAgSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGL 86
Cdd:cd02933 2 LFSPLKLGN-LTLKNRIVMAPLTRSRADPDGVPTDLMAEYYAQRA-SAGLIITEATQISPQGQGYPNTPGIYTDEQVEGW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 87 AKIAEAIKAEGSKAILQIYHGGRMVDPQLI-GGRQPVAPSAVAAP--------REGAAMPRALSGEEVEGMIAKFGDGVR 157
Cdd:cd02933 80 KKVTDAVHAKGGKIFLQLWHVGRVSHPSLLpGGAPPVAPSAIAAEgkvftpagKVPYPTPRALTTEEIPGIVADFRQAAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 158 RAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLdithkmarqyadDAFI-------IGYRFSP 230
Cdd:cd02933 160 NAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVV------------DAVAeaigadrVGIRLSP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 231 eEMEVPGIRFDDTM----YLLEKLAARGVDYLHFSVGATLRPSIVDTSDPTPLIEKYCA---MRSDTLaqvpvmgvggvv 303
Cdd:cd02933 228 -FGTFNDMGDSDPEatfsYLAKELNKRGLAYLHLVEPRVAGNPEDQPPDFLDFLRKAFKgplIAAGGY------------ 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 802145477 304 NAADAEQGLDHGY-DLIAVGRACIAYPDWASRIAAGEEL 341
Cdd:cd02933 295 DAESAEAALADGKaDLVAFGRPFIANPDLVERLKNGAPL 333
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
496-920 |
3.09e-71 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 256.63 E-value: 3.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 496 AAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELFYQETL---KGGHnkNNPQLLRRFVENAP 572
Cdd:PTZ00306 424 AAIEAASCGAQVILLEKEAKLGGNSAKATSGINGWGTRAQAKQDVLDGGKFFERDTHlsgKGGH--CDPGLVKTLSVKSA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 573 QAIEWLADRGIMLNDITTTGGMSIDRTHRP---RDGSAVG-GYLI----SGLVRNITKRGIDVLLDTSVEEILMRGDE-- 642
Cdd:PTZ00306 502 DAISWLSSLGVPLTVLSQLGGASRKRCHRApdkKDGTPVPiGFTImrtlEDHIRTKLSGRVTIMTETTVTSLLSESSArp 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 643 -------VSGVRLIND---EKEVIEVQTKSIVVATGGFS----ANSaMVVKYRPDLEGFVTTNHKGATGSGIALLERIGA 708
Cdd:PTZ00306 582 dgvreirVTGVRYKQAsdaSGQVMDLLADAVILATGGFSndhtPNS-LLREYAPQLSGFPTTNGPWATGDGVKLARKLGA 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 709 GTVDMGEIQIHPT-------VEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPEHY--------AYI 773
Cdd:PTZ00306 661 TLVDMDKVQLHPTglidpkdPSNRTKYLGPEALRGSGGVLLNKNGERFVNELDLRSVVSQAIIAQGNEYpgsggskfAYC 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 774 VF-DEHVRAKNKAADEYIAK--GFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALRAPI-NEGPF 849
Cdd:PTZ00306 741 VLnEAAAKLFGKNSLGFYWKrlGLFQRVDDVKGLAKLIGCPVENLHRTLETYERLSTKKVACPLTGKVVFPCVVgTQGPY 820
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802145477 850 HAIRIAPGVHHTMGGVTINTDGEVL------NV--AQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAA 920
Cdd:PTZ00306 821 YVAFVTPSIHYTMGGCLISPSAEMQmednsvNIfeDRRPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGKIAGDRAA 899
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
7-342 |
2.21e-68 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 231.18 E-value: 2.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLPNgTELKNRLLMAPMTTCTGYFDGTV-TSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIA 84
Cdd:pfam00724 2 LFEPIKIGN-TTLKNRIVMAPMTRLRSLDDGTKaTGLLAEYYSQRSrGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 85 GLAKIAEAIKAEGSKAILQIYHGGRMV----DPQLiGGRQPVAPSAVAAPREGAAMPR-ALSGEEVEGMIAKFGDGVRRA 159
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGREApmeyRPDL-EVDGPSDPFALGAQEFEIASPRyEMSKEEIKQHIQDFVDAAKRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 160 ILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDithkMARQYADDAFIIGYRFSPEEMEVPGIR 239
Cdd:pfam00724 160 REAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVD----AVKEAVGQERIVGYRLSPFDVVGPGLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 240 FDDTMYLLEKLAARGVDYLHFSVGAtlrpsIVDTSDPTPL----IEKYCAMRSDTLAQVPVMGVGGVVNAAD----AEQG 311
Cdd:pfam00724 236 FAETAQFIYLLAELGVRLPDGWHLA-----YIHAIEPRPRgagpVRTRQQHNTLFVKGVWKGPLITVGRIDDpsvaAEIV 310
|
330 340 350
....*....|....*....|....*....|.
gi 802145477 312 LDHGYDLIAVGRACIAYPDWASRIAAGEELE 342
Cdd:pfam00724 311 SKGRADLVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
7-337 |
1.12e-57 |
|
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: 201.57 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLpNGTELKNRLLMAPMttCTgY--FDGTVTS-ELVeYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEK 82
Cdd:cd02932 1 LFTPLTL-RGVTLKNRIVVSPM--CQ-YsaEDGVATDwHLV-HYGSRAlGGAGLVIVEATAVSPEGRITPGDLGLWNDEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 83 IAGLAKIAEAIKAEGSKAILQIYHGGR------------MVDPQLIGGRQPVAPSAVAApREGAAMPRALSGEEVEGMIA 150
Cdd:cd02932 76 IEALKRIVDFIHSQGAKIGIQLAHAGRkastappwegggPLLPPGGGGWQVVAPSAIPF-DEGWPTPRELTREEIAEVVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 151 KFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDIThkmaRQYADDAFIIGYRFSP 230
Cdd:cd02932 155 AFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDAV----RAVWPEDKPLFVRISA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 231 EEMEVPGIRFDDTMYLLEKLAARGVDYLHFSVGATLrPSIVDTSDP---TPLIEkycAMRSDtlAQVPVMGVGGVVNAAD 307
Cdd:cd02932 231 TDWVEGGWDLEDSVELAKALKELGVDLIDVSSGGNS-PAQKIPVGPgyqVPFAE---RIRQE--AGIPVIAVGLITDPEQ 304
|
330 340 350
....*....|....*....|....*....|.
gi 802145477 308 AEQGLDHG-YDLIAVGRACIAYPDWASRIAA 337
Cdd:cd02932 305 AEAILESGrADLVALGRELLRNPYWPLHAAA 335
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
5-341 |
2.55e-56 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 198.80 E-value: 2.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 5 ERILQPFTLPNGTeLKNRLLMAPMTTCTGYFDGTVTSELV-EYYRARAGSiGTIIVECCFIDDYGLAFPGAIGIDNDEKI 83
Cdd:PRK10605 1 EKLFSPLKVGAIT-APNRVFMAPLTRLRSIEPGDIPTPLMaEYYRQRASA-GLIISEATQISAQAKGYAGAPGLHSPEQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 84 AGLAKIAEAIKAEGSKAILQIYHGGRMVDPQL-IGGRQPVAPSAVAAP-------------REGAAMPRALSGEEVEGMI 149
Cdd:PRK10605 79 AAWKKITAGVHAEGGHIAVQLWHTGRISHASLqPGGQAPVAPSAINAGtrtslrdengqaiRVETSTPRALELEEIPGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 150 AKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDIThkMARQYADDafiIGYRFS 229
Cdd:PRK10605 159 NDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAG--IAEWGADR---IGIRIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 230 P----EEMEVPGIRFDDTMYLLEKLAARGVDYLHFSvgatlRPsivDTSDPTPLIEkycAMRSDTLAQVPVMGVGGVVNA 305
Cdd:PRK10605 234 PlgtfNNVDNGPNEEADALYLIEQLGKRGIAYLHMS-----EP---DWAGGEPYSD---AFREKVRARFHGVIIGAGAYT 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 802145477 306 AD-AEQGLDHGY-DLIAVGRACIAYPDWASRIAAGEEL 341
Cdd:PRK10605 303 AEkAETLIGKGLiDAVAFGRDYIANPDLVARLQRKAEL 340
|
|
| OYE_like_3_FMN |
cd04734 |
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ... |
7-340 |
2.98e-55 |
|
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: 195.14 E-value: 2.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLpNGTELKNRLLMAPMTTctGY-FDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIA 84
Cdd:cd04734 1 LLSPLQL-GHLTLRNRIVSTAHAT--NYaEDGLPSERYIAYHEERArGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 85 GLAKIAEAIKAEGSKAILQIYHGGRMVDPQlIGGRQPVAPSAVAAPReGAAMPRALSGEEVEGMIAKFGDGVRRAILAGF 164
Cdd:cd04734 78 GFRRLAEAVHAHGAVIMIQLTHLGRRGDGD-GSWLPPLAPSAVPEPR-HRAVPKAMEEEDIEEIIAAFADAARRCQAGGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 165 DGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDithKMARQYADDaFIIGYRFSPEEMEVPGIRFDDTM 244
Cdd:cd04734 156 DGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLA---AVRAAVGPD-FIVGIRISGDEDTEGGLSPDEAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 245 YLLEKLAARG-VDYLHFSVG--------ATLRPSIVDTSDPT-PLIEK---------YCAMRSDTLAQvpvmgvggvvna 305
Cdd:cd04734 232 EIAARLAAEGlIDYVNVSAGsyytllglAHVVPSMGMPPGPFlPLAARikqavdlpvFHAGRIRDPAE------------ 299
|
330 340 350
....*....|....*....|....*....|....*.
gi 802145477 306 adAEQGLDHGY-DLIAVGRACIAYPDWASRIAAGEE 340
Cdd:cd04734 300 --AEQALAAGHaDMVGMTRAHIADPHLVAKAREGRE 333
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
7-353 |
1.48e-53 |
|
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: 190.61 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLpNGTELKNRLLMAPMTTctgYF--DGTVTSELVEYYRARA-GSIGTIIVECCFIDDYG-LAFPGAIGIDNDEK 82
Cdd:cd04747 1 LFTPFTL-KGLTLPNRIVMAPMTR---SFspGGVPGQDVAAYYRRRAaGGVGLIITEGTAVDHPAaSGDPNVPRFHGEDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 83 IAGLAKIAEAIKAEGSKAILQIYHGG--RMVDPQLIGGRQPVAPSAVAAPreGAAMPRALSGEEVEGMIAKFGDGVRRAI 160
Cdd:cd04747 77 LAGWKKVVDEVHAAGGKIAPQLWHVGamRKLGTPPFPDVPPLSPSGLVGP--GKPVGREMTEADIDDVIAAFARAAADAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 161 LAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLdithKMARQYADDAFIIGYRFS----------- 229
Cdd:cd04747 155 RLGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVV----KAIRAAVGPDFPIILRFSqwkqqdytarl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 230 ---PEEMEVpgirfddtmyLLEKLAARGVDYLHFSV---------GATL-----------RPSIVDTSdptpliekyCAM 286
Cdd:cd04747 231 adtPDELEA----------LLAPLVDAGVDIFHCSTrrfwepefeGSELnlagwtkkltgLPTITVGS---------VGL 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802145477 287 RSDTLAQVPVMGVGGVVNAADAEQGLDHG-YDLIAVGRACIAYPDWASRIAAGEELELFIDStqREAL 353
Cdd:cd04747 292 DGDFIGAFAGDEGASPASLDRLLERLERGeFDLVAVGRALLSDPAWVAKVREGRLDELIPFS--RAAL 357
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
7-263 |
1.78e-53 |
|
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: 189.72 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLPNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIG---IDNDEK 82
Cdd:cd04733 1 LGQPLTLPNGATLPNRLAKAAMSERLADGRGLPTPELIRLYRRWAeGGIGLIITGNVMVDPRHLEEPGIIGnvvLESGED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 83 IAGLAKIAEAIKAEGSKAILQIYHGGRMVdpQLIGGRQPVAPSAVAAPREGA---AMPRALSGEEVEGMIAKFGDGVRRA 159
Cdd:cd04733 81 LEAFREWAAAAKANGALIWAQLNHPGRQS--PAGLNQNPVAPSVALDPGGLGklfGKPRAMTEEEIEDVIDRFAHAARLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 160 ILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFplaVLDITHKMARQYADDaFIIGYRFSPEEMEVPGIR 239
Cdd:cd04733 159 QEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARL---LLEIYDAIRAAVGPG-FPVGIKLNSADFQRGGFT 234
|
250 260
....*....|....*....|....
gi 802145477 240 FDDTMYLLEKLAARGVDYLHFSVG 263
Cdd:cd04733 235 EEDALEVVEALEEAGVDLVELSGG 258
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
489-905 |
6.82e-53 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 190.19 E-value: 6.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 489 SGGAGLAAAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrFQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFV 568
Cdd:pfam00890 7 GGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDAL---GNPPQGGIDSPELHPTDTLKGLDELADHPYVEAFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 569 ENAPQAIEWLADRGIMLN-------DITTTGGMSIDRTH-----RPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEI 636
Cdd:pfam00890 84 EAAPEAVDWLEALGVPFSrtedghlDLRPLGGLSATWRTphdaaDRRRGLGTGHALLARLLEGLRKAGVDFQPRTAADDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 637 LMRGDEVSGVRLIN--DEKEVIEVQTKSIVVATGGFSANsamVVKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVD-- 712
Cdd:pfam00890 164 IVEDGRVTGAVVENrrNGREVRIRAIAAVLLATGGFGRL---AELLLPAAGYADTTNPPANTGDGLALALRAGAALTDdl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 713 MGEIQIHPTVE---QQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIalpehyayivfdEHVRAKNKAADEY 789
Cdd:pfam00890 241 MEFVQFHPTSLvgiRLGSGLLIEALRGEGGILVNKDGRRFMNELASRDVVSRAIT------------RNEIDEGRGANVY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 790 -IAKGfvtsassprelaeklGMDYHAFLATLECYNgavekqhdeqfgRTTALRAPINegPFH-AIRIAPGVHHTMGGVTI 867
Cdd:pfam00890 309 lDASG---------------SLDAEGLEATLPAIN------------EEAIFGLDVD--PYDrPIPVFPAQHYTMGGVRT 359
|
410 420 430
....*....|....*....|....*....|....*....
gi 802145477 868 NTDGEVLNVAQQPIRGAYAAGEVV-GGIHGGNRIGGNAV 905
Cdd:pfam00890 360 DENGRVLDADGQPIPGLYAAGEVAcGGVHGANRLGGNSL 398
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
498-923 |
1.42e-48 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 180.08 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNA-AETRFQRVKGIEDSKELFY---QETLKGG--HNKnnpqlLRRFVENA 571
Cdd:PRK07121 37 IEAAAAGARVLVLERAAGAGGATALSGGVIYLgGGTAVQKAAGFEDSPENMYaylRVAVGPGvdEEK-----LRRYCEGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 572 PQAIEWLADRGI-----------------------------MLNDITTtggmSIDRTHRP--RDGSAVGGYLISGLVRNI 620
Cdd:PRK07121 112 VEHFDWLEGLGVpfersffpektsyppndeglyysgnekawPFAEIAK----PAPRGHRVqgPGDSGGGAMLMDPLAKRA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 621 TKRGIDVLLDTSVEE-ILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPDLEGFVTTNHKGATGSG 699
Cdd:PRK07121 188 AALGVQIRYDTRATRlIVDDDGRVVGVEARRYGETVAIRARKGVVLAAGGFAMNREMVARYAPAYAGGLPLGTTGDDGSG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 700 IALLERIGAGTVDMGEIQIhptveqqTSYLISESIRGGGaILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHV 779
Cdd:PRK07121 268 IRLGQSAGGATAHMDQVFA-------WRFIYPPSALLRG-ILVNARGQRFVNEDTYGARIGQFILEQPGGTAYLIVDEAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 780 RAKNKAADEYIAKGFVT---SASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALRAPINEGPFHAIRIAP 856
Cdd:PRK07121 340 FEEARAQLRPQIDGRTPgawKAETVEELARKLGIPPGGLQATVDAYNRAAAGGEDPPFHKQPEWLRPLDTGPFAAIDLSL 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802145477 857 GV----HHTMGGVTINTD-GEVLNVAQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRA 923
Cdd:PRK07121 420 GKaptpGFTLGGLRVDEDtGEVLRADGAPIPGLYAAGRCASGIASNGYVSGLSLADCSFFGRRAGRHAAARA 491
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
7-263 |
8.12e-47 |
|
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: 171.32 E-value: 8.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 7 ILQPFTLpNGTELKNRLLMAPMTTctGYFDGTVTSE-LVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIA 84
Cdd:cd02930 1 LLSPLDL-GFTTLRNRVLMGSMHT--GLEELDDGIDrLAAFYAERArGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 85 GLAKIAEAIKAEGSKAILQIYHGGRMvdpqligGRQP--VAPSAVAAPREGAAmPRALSGEEVEGMIAKFGDGVRRAILA 162
Cdd:cd02930 78 GHRLITDAVHAEGGKIALQILHAGRY-------AYHPlcVAPSAIRAPINPFT-PRELSEEEIEQTIEDFARCAALAREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 163 GFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLdithKMARQYADDAFIIGYRFSPEEMEVPGIRFDD 242
Cdd:cd02930 150 GYDGVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIV----RAVRAAVGEDFIIIYRLSMLDLVEGGSTWEE 225
|
250 260
....*....|....*....|.
gi 802145477 243 TMYLLEKLAARGVDYLHFSVG 263
Cdd:cd02930 226 VVALAKALEAAGADILNTGIG 246
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
6-339 |
4.27e-45 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 166.03 E-value: 4.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 6 RILQPFTLPNGTeLKNRLLMAPMTTCTGY-FDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKI 83
Cdd:PRK13523 2 KLFSPYTIKDVT-LKNRIVMSPMCMYSSEnKDGKVTNFHLIHYGTRAaGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 84 AGLAKIAEAIKAEGSKAILQIYHGGRmvDPQLIGgrQPVAPSAVAApREGAAMPRALSGEEVEGMIAKFGDGVRRAILAG 163
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAGR--KAELEG--DIVAPSAIPF-DEKSKTPVEMTKEQIKETVLAFKQAAVRAKEAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 164 FDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDithkMARQYADDAFIIgyRFSPEEMEVPGIRFDDT 243
Cdd:PRK13523 156 FDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIID----AVKEVWDGPLFV--RISASDYHPGGLTVQDY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 244 MYLLEKLAARGVDYLHFSVGATLRPSIvdtsdptPLIEKYCAMRSDTL---AQVPVMGVGGVVNAADAEQGLDHGY-DLI 319
Cdd:PRK13523 230 VQYAKWMKEQGVDLIDVSSGAVVPARI-------DVYPGYQVPFAEHIrehANIATGAVGLITSGAQAEEILQNNRaDLI 302
|
330 340
....*....|....*....|
gi 802145477 320 AVGRACIAYPDWAsRIAAGE 339
Cdd:PRK13523 303 FIGRELLRNPYFP-RIAAKE 321
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
498-924 |
3.79e-44 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 167.98 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGaSVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEW 577
Cdd:COG0029 21 LKLAERG-RVTLLTKGELGESNTRWAQGGIAA-------VLDPGDSPELHIADTLAAGAGLCDPEAVRVLVEEGPERIRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 578 LADRGImlnDITTTGGMSIDRT-----HRPR-----DgsAVGGYLISGLVRNITKR-GIDVLLDTSVEEILMRGD-EVSG 645
Cdd:COG0029 93 LIELGV---PFDRDEDGELALTregghSRRRilhagD--ATGREIERALLEAVRAHpNITVLENHFAVDLITDADgRCVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 646 VRLIN-DEKEVIEVQTKSIVVATGGFSAnsamVvkYRpdlegfVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV-- 722
Cdd:COG0029 168 AYVLDeKTGEVETIRAKAVVLATGGAGQ----L--YA------YTTNPDVATGDGIAMAYRAGARLADMEFVQFHPTAly 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 723 -EQQTSYLISESIRGGGAILVNQQGNRFfneME---------TRDKVSAAIIA----LPEHYAYIvfDehVRAKNKaadE 788
Cdd:COG0029 236 hPGAPSFLISEAVRGEGAVLRNADGERF---MPdyhpraelaPRDVVARAIDAemkkTGGDCVYL--D--ISHLDA---E 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 789 YIAKGFvtsassPR--ELAEKLGMDyhaflatlecyngaVEKQhdeqfgrttalraPInegPfhairIAPGVHHTMGGVT 866
Cdd:COG0029 306 FIRERF------PTiyARCLELGID--------------ITKE-------------PI---P-----VAPAAHYTMGGVA 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 802145477 867 INTDGEVlnvaqqPIRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAGHQAAKRAR 924
Cdd:COG0029 345 TDLDGRT------SIPGLYAVGEVAcTGVHGANRLASNSLLEGLVFGRRAAEDIAARLA 397
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
498-925 |
2.21e-42 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 161.58 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPtiggntiKASAGMNAAETRFQRV--KGIED------SKELFYQETLKGGHNKNNPQLLRRFVE 569
Cdd:PRK08274 21 LAAREAGASVLLLEAAP-------REWRGGNSRHTRNLRCmhDAPQDvlvgayPEEEFWQDLLRVTGGRTDEALARLLIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 570 NAPQAIEWLADRGIMLNDITTTGGMSIDRTHRPRDGsavGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLI 649
Cdd:PRK08274 94 ESSDCRDWMRKHGVRFQPPLSGALHVARTNAFFWGG---GKALVNALYRSAERLGVEIRYDAPVTALELDDGRFVGARAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 650 NDEKEVIEVQTKSIVVATGGFSANSAMVVKY-RPDLEGFVTTNHKGATGSGIALLERIGAGTV-DMGEIQIHPT------ 721
Cdd:PRK08274 171 SAAGGAERIRAKAVVLAAGGFESNREWLREAwGQPADNFLVRGTPYNQGDLLKALLDAGADRIgDPSQCHAVAIdarapl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 722 -----VEQQTSYLIsesirgggAILVNQQGNRFFNEME-----TRDKVSAAIIALPEHYAYIVFDEhvraknKAADEYIA 791
Cdd:PRK08274 251 ydggiCTRIDCVPL--------GIVVNRDGERFYDEGEdfwpkRYAIWGRLVAQQPGQIAYQIFDA------KAIGRFMP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 792 KGFV-TSASSPRELAEKLGMDYHAFLATLECYNGAVEK---QHDEQFGRTTALRAP--------INEGPFHAIRIAPGVH 859
Cdd:PRK08274 317 PVFPpIQADTLEELAEKLGLDPAAFLRTVAAFNAAVRPgpfDPTVLDDCGTEGLTPpkshwarpIDTPPFYAYPVRPGIT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802145477 860 HTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGG-IHGGNRIGGNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK08274 397 FTYLGLKVDEDARVRFADGRPSPNLFAAGEMMAGnVLGKGYPAGVGLTIGAVFGRIAGEEAARHAQH 463
|
|
| sdhA |
PRK06263 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
503-923 |
3.36e-40 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 235758 [Multi-domain] Cd Length: 543 Bit Score: 156.68 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 503 EGASVLIVEKmpTI---GGNTIKASAGMNAaetrfqrVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLA 579
Cdd:PRK06263 28 RGKNVVIVSK--GLfgkSGCTVMAEGGYNA-------VLNPEDSFEKHFEDTMKGGAYLNDPKLVEILVKEAPKRLKDLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 580 DRGiMLNDITTT--------GGMSIDRThrPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDE--VSGVRLI 649
Cdd:PRK06263 99 KFG-ALFDRTEDgeiaqrpfGGQSFNRT--CYAGDRTGHEMMMGLMEYLIKERIKILEEVMAIKLIVDENRevIGAIFLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 650 NDEKEVIEVQTKSIVVATGGFSansamvvKYRPdlegfVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPT----VEQQ 725
Cdd:PRK06263 176 LRNGEIFPIYAKATILATGGAG-------QLYP-----ITSNPIQKTGDGFAIAYRAGAELIDMEMVQFHPTgmvyPYSG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 726 TSYLISESIRGGGAILVNQQGNRFFN-------EMETRDKVSAAIialpehyayivFDEhvraknkaadeyIAKGFVTSA 798
Cdd:PRK06263 244 RGILVTEAVRGEGGILYNKNGERFMKrydpermELSTRDVVARAI-----------YTE------------IQEGRGTNH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 799 SS--------PRELAE-KLGMDYHAFLatlecyngavekqhdeQFGrttalrAPINEGPfhaIRIAPGVHHTMGGVTINT 869
Cdd:PRK06263 301 GGvyldvthlPDEVIEeKLETMLEQFL----------------DVG------VDIRKEP---MEVAPTAHHFMGGIRINE 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 802145477 870 DGEVlnvaqqPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRA 923
Cdd:PRK06263 356 DCET------NIPGLFACGEVAGGVHGANRLGGNALADTQVFGAIAGKSAAKNA 403
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
607-925 |
2.74e-35 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 142.20 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 607 AVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPD-LE 685
Cdd:PRK12844 205 TNGAALIGRMLEAALAAGVPLWTNTPLTELIVEDGRVVGVVVVRDGREVLIRARRGVLLASGGFGHNAEMRKRYQPQpNS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 686 GFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGG----GAILVNQQGNRFFNE--------- 752
Cdd:PRK12844 285 GDWTNANPGDTGEVIEAAMRLGAALDLMDEAWWVPGAPLPNGGPRPYMHNSErskpGSIIVDRAGRRFVNEagsymevgr 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 753 -METRDKVSAAIIALPEHYAYIVFDEhvRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHD 831
Cdd:PRK12844 365 aMYAQDAVPAWMIMDSRYRKRYLFGT--IPPGPTPQEWLDSGYMKRADTIEELAGKTGIDPAGLAATVERFNGFAATGTD 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 832 EQFGR---------------TTALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHG 896
Cdd:PRK12844 443 PDFHRgesaydryygdptnkPNPSLGPLDKPPFYAVRMVPGDVGTSGGLLTDEHARVLREDGSVIPGLYATGNCTASVMG 522
|
330 340 350
....*....|....*....|....*....|
gi 802145477 897 GNRIG-GNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK12844 523 RTYPGaGASIGNSFVFGYIAALHAAGARSA 552
|
|
| PRK06175 |
PRK06175 |
L-aspartate oxidase; Provisional |
502-923 |
3.11e-35 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 180442 [Multi-domain] Cd Length: 433 Bit Score: 139.82 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 502 DEGASVLIVEKMPTIGGNTIKASAGMNAAetrfqrvKGIEDsKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADR 581
Cdd:PRK06175 24 RKDLKILMVSKGKLNECNTYLAQGGISVA-------RNKDD-ITSFVEDTLKAGQYENNLEAVKILANESIENINKLIDM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 582 GIMLN------DITTTGGMSIDRTHRPRDgsAVGGYLISGLVRNITKR-GIDVLLDTSVEEILMRGDEVSGVRLINDEkE 654
Cdd:PRK06175 96 GLNFDkdekelSYTKEGAHSVNRIVHFKD--NTGKKVEKILLKKVKKRkNITIIENCYLVDIIENDNTCIGAICLKDN-K 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 655 VIEVQTKSIVVATGGFSA---NSamvvkyrpdlegfvtTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV-----EQQT 726
Cdd:PRK06175 173 QINIYSKVTILATGGIGGlfkNS---------------TNQRIITGDGIAIAIRNNIKIKDLDYIQIHPTAfyeetIEGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 727 SYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPE--HYAYIVFDehVRAKNKaadEYIAKGFVTsassprel 804
Cdd:PRK06175 238 KFLISESVRGEGGKLLNSKGERFVDELLPRDVVTKAILEEMKktGSNYVYLD--ITFLDK---DFLKNRFPT-------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 805 aeklgmdyhaflatleCYNGAVEKQHDeqfgrttalraPINEgpfhAIRIAPGVHHTMGGVTINTDGevlnvaQQPIRGA 884
Cdd:PRK06175 305 ----------------IYEECLKRGID-----------ITKD----AIPVSPAQHYFMGGIKVDLNS------KTSMKNL 347
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 802145477 885 YAAGEV-VGGIHGGNRIGGNAVADIIIFgtlaghqaAKRA 923
Cdd:PRK06175 348 YAFGEVsCTGVHGANRLASNSLLEGLVF--------SKRG 379
|
|
| sdhA |
PRK06069 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
505-923 |
1.87e-33 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 235689 [Multi-domain] Cd Length: 577 Bit Score: 136.72 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 505 ASVLIVEKMPTIGGNTIKASAGMNAA---ETrfqrvkgiEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWL--- 578
Cdd:PRK06069 32 LSVAVVSKTQPMRSHSVSAEGGTAAVlypEK--------GDSFDLHAYDTVKGSDFLADQDAVEVFVREAPEEIRFLdhw 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 579 -------ADRGIMLNDItttGGMSIDRTHRPRDGSavGGYLISGLVRNiTKR--GIDVLLDTSVEEILMRGDEVSGVRLI 649
Cdd:PRK06069 104 gvpwsrrPDGRISQRPF---GGMSFPRTTFAADKT--GFYIMHTLYSR-ALRfdNIHFYDEHFVTSLIVENGVFKGVTAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 650 NDEK-EVIEVQTKSIVVATGGFSAnsamvvkyrpdLEGFVTTNHKgATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSY 728
Cdd:PRK06069 178 DLKRgEFKVFQAKAGIIATGGAGR-----------LYGFTTYAHS-VTGDGLAIAYRAGIPLKDMEFVQFHPTGLVPSGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 729 LISESIRGGGAILVNQQGNRFF-----NEME--TRDKVSAAIIAlpehyayivfdehvraknkaadEYIA-KGFVTSAss 800
Cdd:PRK06069 246 LITEAARGEGGYLINKEGERFMkryapQKMElaPRDVVSRAIMT----------------------EIMEgRGFKHES-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 801 prelaeklGMDYHAflatLECYNGAVEKQHDE-----QFGRTTALRAPINEgpfhAIRIAPGVHHTMGGVTINTDGEVLN 875
Cdd:PRK06069 302 --------GLCYVG----LDLRHLGEEKINERlplirEIAKKYAGIDPVTE----PIPVRPAAHYTMGGIHTDVYGRVLT 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 802145477 876 VAQQPIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAKRA 923
Cdd:PRK06069 366 ADGEWVRGLWAAGEAAAvSVHGANRLGSNSTAECLVWGRIAGEQAAEYA 414
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
503-925 |
3.82e-33 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 136.02 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 503 EGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELFYQeTLKGGHNKNNPQLLRR-FVENAPQAIEWLAD- 580
Cdd:PRK12843 38 AGLKVLLVERTEYVGGTTATSAGTTWIPGTRHGLAVGPDDSLEAART-YLDALVGDRSPEELRDaFLASGPRAIAFLEAn 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 581 -----------------------RGIMLN---------------------DITTTGGMSIDRT----------------- 599
Cdd:PRK12843 117 sevkfrayashpdyesdlpgatlRGRALEplpfdgrklgadfalirppipEFTVLGGMMVDRTdvghllaltkswrafrh 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 600 ------HRPRD------GS--AVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVV 665
Cdd:PRK12843 197 avrllaRYARDrisyarGTrlVMGNALIGRLLYSLRARGVRILTQTDVESLETDHGRVIGATVVQGGVRRRIRARGGVVL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 666 ATGGFSANSAMVVKYRPDLEGFVTTNHKGATGSGIALLERIGA----GTVDMG---EIQIHPTVEQQTS---YLISESIR 735
Cdd:PRK12843 277 ATGGFNRHPQLRRELLPAAVARYSPGAPGHTGAAIDLALDAGArygrGLLSNAfwaPVSVRRRADGSTAvfpHFYLDRGK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 736 GGgAILVNQQGNRFFNE----------METRDKVSAAIialPehyAYIVFDEH---------VRAKNKAADEYIAKGFVT 796
Cdd:PRK12843 357 PG-TIAVNQQGRRFVNEstsyhlfgtaMFAAGKTSPGI---P---AYLITDAEflrkyglgmVRPGGRGLAPFLRDGYLT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 797 SASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGR-TTALR--------------APINEGPFHAIRIAPGVHHT 861
Cdd:PRK12843 430 VASTLDELAPKLGIDPAALAATVQRHNQYARTGIDPDFGRgATAYQrmngdamigpnpnlGPIETAPFYAVRLYPGDIGA 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802145477 862 MGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNRIG-GNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK12843 510 ATGLVTDASARVLNADGQPISGLYACGNDMASIMGGTYPGpGITLGPAIVFAYLAARHAAKRTLA 574
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
3-230 |
5.74e-32 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 129.20 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 3 SNERILQPFTLPNgTELKNRLLMAPMTTCTGyFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEK 82
Cdd:PLN02411 8 SNETLFSPYKMGR-FDLSHRVVLAPMTRCRA-LNGIPNAALAEYYAQRSTPGGFLISEGTLISPTAPGFPHVPGIYSDEQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 83 IAGLAKIAEAIKAEGSKAILQIYHGGR----MVDPqliGGRQPVAP-SAVAAPREGAAMP----------RALSGEEVEG 147
Cdd:PLN02411 86 VEAWKKVVDAVHAKGSIIFCQLWHVGRashqVYQP---GGAAPISStNKPISERWRILMPdgsygkypkpRALETSEIPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 148 MIAKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDithkmARQYADDAFIIGYR 227
Cdd:PLN02411 163 VVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRFLMQVVQ-----AVVSAIGADRVGVR 237
|
...
gi 802145477 228 FSP 230
Cdd:PLN02411 238 VSP 240
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
18-338 |
1.03e-29 |
|
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: 122.23 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 18 ELKNRLLMAPMTT---CTGyfDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFP-GAIGIDNDEK---IAGLAKI 89
Cdd:cd02931 11 EIKNRFAMAPMGPlglADN--DGAFNQRGIDYYVERAkGGTGLIITGVTMVDNEIEQFPmPSLPCPTYNPtafIRTAKEM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 90 AEAIKAEGSKAILQIYHG-GRMVDPQLIGGRQPVAPSAVAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDGVE 168
Cdd:cd02931 89 TERVHAYGTKIFLQLTAGfGRVCIPGFLGEDKPVAPSPIPNRWLPEITCRELTTEEVETFVGKFGESAVIAKEAGFDGVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 169 IHGANT-YLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLD-ITHKMAR------QYADDAFIIGYR---FSPEEMEVPG 237
Cdd:cd02931 169 IHAVHEgYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIVEeIKARCGEdfpvslRYSVKSYIKDLRqgaLPGEEFQEKG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 238 IRFDDTMYLLEKLAARGVDYLHFSVGAtlrpsiVDT---SDPtPLIEK------YCAMRSDTLaQVPVMGVGGVVNAADA 308
Cdd:cd02931 249 RDLEEGLKAAKILEEAGYDALDVDAGS------YDAwywNHP-PMYQKkgmylpYCKALKEVV-DVPVIMAGRMEDPELA 320
|
330 340 350
....*....|....*....|....*....|.
gi 802145477 309 EQGLDHGY-DLIAVGRACIAYPDWASRIAAG 338
Cdd:cd02931 321 SEAINEGIaDMISLGRPLLADPDVVNKIRRG 351
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
8-208 |
1.13e-28 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 123.51 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 8 LQPFTLpNGTELKNRLLMAPMT--TCTgyfDGTVTSELVEYYRARA-GSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIA 84
Cdd:PRK08255 400 FTPFRL-RGLTLKNRVVVSPMAmySAV---DGVPGDFHLVHLGARAlGGAGLVMTEMTCVSPEGRITPGCPGLYNDEQEA 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 85 GLAKIAEAIKAEGSKAI-LQIYHGGRM---------VDPQLIGGRQP-VAPSAVAApREGAAMPRALSGEEVEGMIAKFG 153
Cdd:PRK08255 476 AWKRIVDFVHANSDAKIgIQLGHSGRKgstrlgwegIDEPLEEGNWPlISASPLPY-LPGSQVPREMTRADMDRVRDDFV 554
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802145477 154 DGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLD 208
Cdd:PRK08255 555 AAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFR 609
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
498-925 |
1.17e-28 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 122.11 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELFY----QETlkgGHNKNNPQLlRRFVENAPQ 573
Cdd:PRK12842 26 ITARKLGLDVVVLEKEPVFGGTTAFSGGVLWIPGNPHAREAGVADSREAARtylkHET---GAFFDAAAV-EAFLDNGPE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 574 AIEWLAD-------------------------RGIM-------------------LNDITTTGGMS----------IDRT 599
Cdd:PRK12842 102 MVEFFERetevkfvptlypdyhpdapggvdigRSILaapydirglgkdmarlrppLKTITFIGMMFnssnadlkhfFNAT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 600 HRP--------------------RDGSAV--GGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRlINDEKEVIE 657
Cdd:PRK12842 182 RSLtsfiyvakrlathlkdlalyRRGTQVtsGNALAARLAKSALDLGIPILTGTPARELLTEGGRVVGAR-VIDAGGERR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 658 VQTKSIVV-ATGGFSANSAMVVKYRPDLEgfVTTNH-----KGATGSGIALLERIGA---------------GTVDM--G 714
Cdd:PRK12842 261 ITARRGVVlACGGFSHDLARIARAYPHLA--RGGEHlspvpAGNTGDGIRLAEAVGGavdirfpdaaawmpvSKVPLggG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 715 EIQIHPTVEQQTSylisesirgGGAILVNQQGNRFFNEMETRDKVSAAIIA----LPEHYAYIVFDEHVRAK-----NKA 785
Cdd:PRK12842 339 RTGVFPHLLDRYK---------PGVIGVLRNGKRFTNESNSYHDVGAAMIRacegQKETAMWLICDRATLRKyglgyAKP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 786 A----DEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGR-TTALR--------------APINE 846
Cdd:PRK12842 410 ApmpvGPLLRNGYLIKGDTLAELAGKAGIDAAGLEATVRRYNEGAVKGIDPAFGRgSTSFNrylgdpdhkpnpcvAPIGS 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 847 GPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNRIG-GNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK12842 490 GPFYAVKVIMGDLGTFDGLRTDVTGEVLDADGTPIAGLYAVGNDRASIMGGNYPGaGITLGPIMTFGYITGRHLAGVAGG 569
|
|
| PRK08071 |
PRK08071 |
L-aspartate oxidase; Provisional |
519-917 |
5.89e-28 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236147 [Multi-domain] Cd Length: 510 Bit Score: 119.32 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 519 NTIKASAGMNAAETRfqrvkgiEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGiMLNDITTTGGMSIDR 598
Cdd:PRK08071 40 NSHLAQGGIAAAVAT-------YDSPNDHFEDTLVAGCHHNNERAVRYLVEEGPKEIQELIENG-MPFDGDETGPLHLGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 599 --THRPR-----DGSAVGGYLISGLVRNITKRgIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFS 671
Cdd:PRK08071 112 egAHRKRrilhaGGDATGKNLLEHLLQELVPH-VTVVEQEMVIDLIIENGRCIGVLTKDSEGKLKRYYADYVVLASGGCG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 672 ANSAmvvkyrpdlegfVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPT---VEQQTSYLISESIRGGGAILVNQQGNR 748
Cdd:PRK08071 191 GLYA------------FTSNDKTITGDGLAMAYRAGAELVDLEFIQFHPTmlyANGRCVGLVSEAVRGEGAVLINEDGRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 749 FfneMET---------RDKVSAAIIA--LPEHYAYIvfdehvrakNKAADEYIAKGFVTSASspreLAEKLGMDYHAfla 817
Cdd:PRK08071 259 F---MMGihpladlapRDVVARAIHEelLSGEKVYL---------NISSIQNFEERFPTISA----LCEKNGVDIET--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 818 tlecyngavekqhdeqfGRttalrapinegpfhaIRIAPGVHHTMGGVTINTDGEVlnvaqqPIRGAYAAGEVV-GGIHG 896
Cdd:PRK08071 320 -----------------KR---------------IPVVPGAHFLMGGVKTNLDGET------SIPGLYAIGEVAcTGVHG 361
|
410 420
....*....|....*....|.
gi 802145477 897 GNRIGGNAVADIIIFGTLAGH 917
Cdd:PRK08071 362 ANRLASNSLLEGLVFGKRAAE 382
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
529-924 |
1.68e-27 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 118.58 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 529 AAETRFQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAP----QAIEW------LADRGImlnDITTTGGMSIDR 598
Cdd:PRK09231 47 AAEGGSAAVAQDHDSFDYHFHDTVAGGDWLCEQDVVEYFVHHCPtemtQLEQWgcpwsrKPDGSV---NVRRFGGMKIER 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 599 THRPRDGSavGGYLISGLV-RNITKRGIDVLLDTSVEEILMRGDEVSGVRLIN-DEKEVIEVQTKSIVVATGGfsanSAM 676
Cdd:PRK09231 124 TWFAADKT--GFHMLHTLFqTSLKYPQIQRFDEHFVLDILVDDGHVRGLVAMNmMEGTLVQIRANAVVMATGG----AGR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 677 VVKYrpdlegfvTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFNE---- 752
Cdd:PRK09231 198 VYRY--------NTNGGIVTGDGMGMAYRHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKDGYRYLQDyglg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 753 ------------ME--TRDKVSAAiialpehyayivFDEHVRAKNKAADeyiAKGFVTSASSpRELAEKLGMDYHAFLAT 818
Cdd:PRK09231 270 petplgepknkyMElgPRDKVSQA------------FWHEWRKGNTIST---PRGDVVYLDL-RHLGEKKLHERLPFICE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 819 L-ECYNGaVEkqhdeqfgrttalraPINEgpfhAIRIAPGVHHTMGGVTINTDGEVlnvaqqPIRGAYAAGEVVG-GIHG 896
Cdd:PRK09231 334 LaKAYVG-VD---------------PVKE----PIPVRPTAHYTMGGIETDQNCET------RIKGLFAVGECSSvGLHG 387
|
410 420
....*....|....*....|....*...
gi 802145477 897 GNRIGGNAVADIIIFGTLAGHQAAKRAR 924
Cdd:PRK09231 388 ANRLGSNSLAELVVFGRVAGEQAAERAA 415
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
607-923 |
2.92e-27 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 117.44 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 607 AVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPDLEG 686
Cdd:PRK07843 205 GMGQALAAGLRIGLQRAGVPVLLNTPLTDLYVEDGRVTGVHAAESGEPQLIRARRGVILASGGFEHNEQMRAKYQRAPIG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 687 FV-TTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV--EQQTSYLISESIRGGGaILVNQQGNRFFNEMETRDKVSAAI 763
Cdd:PRK07843 285 TEwTVGAKANTGDGILAGEKLGAALDLMDDAWWGPTIplPGGPWFALSERNLPGS-IIVNMSGKRFMNESAPYVEAVHHM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 764 IALP--------EHY-AYIVFDEHVRAKNKAAD---------EYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGA 825
Cdd:PRK07843 364 YGGEygqgpgpgENIpAWLVFDQRYRDRYLFAGlqprqpipsRWLESGVIVKADTLAELAAKIGVPADALTATVQRFNGF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 826 VEKQHDEQFGRTTALR---------------APINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEV 890
Cdd:PRK07843 444 ARSGVDEDFHRGESAYdryygdptnkpnpnlGELSHAPFYAAKMVPGDLGTKGGLRTDVRGRVLRDDGSVIEGLYAAGNV 523
|
330 340 350
....*....|....*....|....*....|....
gi 802145477 891 VGGIHGGNRIG-GNAVADIIIFGTLAGHQAAKRA 923
Cdd:PRK07843 524 SAPVMGHTYAGpGATIGPAMTFGYLAALDIAAQA 557
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
498-920 |
4.34e-27 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 117.24 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKELF---YQETLkgGHNKNNPQLlRRFVENAPQA 574
Cdd:PRK12839 25 VAAAYGGAKVLVVEKASTCGGATAWSGGWMWTPGNSLARADGVVEDKEEPrtyLEHRL--GENYDADKV-DALLDGAPEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 575 IEWLADR-------GIMLNDI--------------------------------------TTTGGMSI----DRT---HRP 602
Cdd:PRK12839 102 VDFFEKKtalqfvpGAKIADIygdlpgagtghrsvgpkpvnlrklgpdvaallrhqlyeTSFLGMGImagpDLQaflHAT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 603 RDGSAV-------------------------GGYLISGLVRNITKRGIDVLLDTSVEEILM-RGDEVSGVRLINDEKEVI 656
Cdd:PRK12839 182 QDPKGFvhaarrvivhmwdlathrrgmqlvnGTALTGRLLRSADDLGVDLRVSTSATSLTTdKNGRVTGVRVQGPDGAVT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 657 EVQTKSIVVATGGFSANsamvVKYRPDLEGFVTTNH-------KGATGSGIALLERIGAG-------TVDMGEIQIHPTV 722
Cdd:PRK12839 262 VEATRGVVLATGGFPND----VDRRKELFPRTPTGRehwtlapAETTGDGISLAESVGARldrdlasPAAWCPVSLVPYR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 723 EQQTSYLISESIRGG-GAILVNQQGNRFFNEMET-RDKVSAAIIALPEH---YAYIVFDE-HVR------AKNKAAD--E 788
Cdd:PRK12839 338 NGKVGTFPHIMDRGKpGSIGVLATGKRFVNEANGyYDYTLAMVKAAPEGepvCSWLIADSrFVRkyplgmAKPLPVPltP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 789 YIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGR-TTALR--------------APINEGPFHAIR 853
Cdd:PRK12839 418 YLRSGYLTRGRTIEELAEKCGIDPAGLEATVAEFNENARDGEDPEFGRgTTPFNrgsgdpdngpnpslAPLEKGPFYAVK 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802145477 854 IAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNR-IGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK12839 498 VVPGSFGTFAGLVADGKSRVLRDDDTPIDGLYAAGNDQASVMGGHYpSGGINLGPAMTFGYIAGRELA 565
|
|
| PRK07395 |
PRK07395 |
L-aspartate oxidase; Provisional |
541-912 |
4.44e-27 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236010 [Multi-domain] Cd Length: 553 Bit Score: 117.07 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 541 EDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSIDRTH-RPR---DGSAVGGYLISGL 616
Cdd:PRK07395 61 DDSPKLHYEDTLKAGAGLCDPEAVRFLVEQAPEAIASLVEMGVAFDRHGQHLALTLEAAHsRPRvlhAADTTGRAIVTTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 617 VRNITKRG-IDVLLDTSVEEILMRGD--EVSGVRLINDEKevIE-VQTKSIVVATGG----FSAnsamvvkyrpdlegfv 688
Cdd:PRK07395 141 TEQVLQRPnIEIISQALALSLWLEPEtgRCQGISLLYQGQ--ITwLRAGAVILATGGggqvFAQ---------------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 689 TTNHKGATGSGIALLERIGAGTVDMGEIQIHPT---VEQQTSYLISESIRGGGAILVNQQGNRF-FN-----EMETRDKV 759
Cdd:PRK07395 203 TTNPAVSTGDGVALAWRAGAQLRDLEFFQFHPTaltKPGAPRFLISEAVRGEGAHLVDAQGRRFaFDyhpagELAPRDVV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 760 SAAIialpehYAYIvfdehvraKNKAADEYIAKGFVTSASSPRELAEklgmdyHAFLATLE-CyngavekqhdEQFGrtt 838
Cdd:PRK07395 283 SRAI------FSHL--------QKTATDPATAHVWLDLRPIPAERIR------RRFPNIIRvC----------QKWG--- 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802145477 839 alrapINegPFH-AIRIAPGVHHTMGGVTINTDGevlnvaQQPIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFG 912
Cdd:PRK07395 330 -----ID--VFQePIPVAPAAHYWMGGVVTDLNN------QTSIPGLYAVGETAStGVHGANRLASNSLLECLVFA 392
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
595-920 |
7.91e-27 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 116.36 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 595 SIDRTHRPRDGSAVGGY-LISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFSAN 673
Cdd:PRK06134 201 LIDLARHGRGMHLVNGNaLVARLLKSAEDLGVRIWESAPARELLREDGRVAGAVVETPGGLQEIRARKGVVLAAGGFPHD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 674 SAMvvkyRPDLEGFVTTNH-------KGATGSGIALLERIGaGTVDM------------------GEIQIHPtveqqtsY 728
Cdd:PRK06134 281 PAR----RAALFPRAPTGHehlslppPGNSGDGLRLGESAG-GVVATdlaspvawapvslvphadGSVGHFP-------H 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 729 LISesiRGG-GAILVNQQGNRFFNEMET-RDKVSAAIIALP---EHYAYIVFDE---------HVRAKNKAADEYIAKGF 794
Cdd:PRK06134 349 IIE---RGKpGLIGVLANGKRFVNEADSyHDYVAAMFAATPpgqPVRSWLICDHrflrryglgHIRPAPLPLGPYVRSGY 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 795 VTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGR-TTALR---------------APINEGPFHAIRIAPGV 858
Cdd:PRK06134 426 LKRGASLEELARACGIDPDGLEATVARYNRHARNGQDPDFGRgSTPYNrkqgdpahggpnpcvAPIEHGPFYAVKVLPGC 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802145477 859 HHTMGGVTINTDGEVLNVAQQPIRGAYAAG----EVVGGIHGGnriGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK06134 506 LGTFAGLKTDADARVLDQAGQPIPGLYAAGndmaSVMGGFYPS---GGITLGPALTFGYIAGRHIA 568
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
498-925 |
1.87e-26 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 115.52 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrfQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEW 577
Cdd:PRK07803 25 IEARERGLRVAVVCKSLFGKAHTVMAEGGCAAA----MGNVNPKDNWQVHFRDTMRGGKFLNNWRMAELHAKEAPDRVWE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 578 LADRGiMLNDITTTGGMSiDRT---HR-PR---DGSAVGGYLISGLVRNITK-------------RGIDVLLDTSVEEIL 637
Cdd:PRK07803 101 LETYG-ALFDRTKDGRIS-QRNfggHTyPRlahVGDRTGLELIRTLQQKIVSlqqedhaelgdyeARIKVFAECTITELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 638 MRGDEVSGVRLINDEK-EVIEVQTKSIVVATGGFSANsamvvkYRpdlegfVTTNHKGATGSGIALLERIGAGTVDMGEI 716
Cdd:PRK07803 179 KDGGRIAGAFGYWRESgRFVLFEAPAVVLATGGIGKS------FK------VTSNSWEYTGDGHALALRAGATLINMEFV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 717 QIHPT-------VEqqtSYLISESIRGGGAILVNQQGNRF-FN-------------------------------EMETRD 757
Cdd:PRK07803 247 QFHPTgmvwppsVK---GILVTEGVRGDGGVLKNSEGKRFmFDyipdvfkgqyaeteeeadrwykdndnnrrppELLPRD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 758 KVSAAIialpehyayivfdehvRAKNKAADEYIAKGF---VTSASSPRELAEKLGMDYHAF--LATLECYNGAVEkqhde 832
Cdd:PRK07803 324 EVARAI----------------NSEVKAGRGSPHGGVyldIASRLPAEEIKRRLPSMYHQFkeLADVDITKEPME----- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 833 qfgrttalrapinegpfhairIAPGVHHTMGGVTINTDGEVLNVAqqpirGAYAAGEVVGGIHGGNRIGGNAVADIIIFG 912
Cdd:PRK07803 383 ---------------------VGPTCHYVMGGVEVDPDTGAATVP-----GLFAAGECAGGMHGSNRLGGNSLSDLLVFG 436
|
490
....*....|...
gi 802145477 913 TLAGHQAAKRARG 925
Cdd:PRK07803 437 RRAGLGAADYVRG 449
|
|
| PRK12845 |
PRK12845 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
592-922 |
1.05e-24 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237226 [Multi-domain] Cd Length: 564 Bit Score: 109.86 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 592 GGMSIDRTHrprdgSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEVQTKSIVVATGGFS 671
Cdd:PRK12845 204 GGLALGRRY-----AAGGQALAAGLFAGVLRAGIPIWTETSLVRLTDDGGRVTGAVVDHRGREVTVTARRGVVLAAGGFD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 672 ANSAMVVKYR-PDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVE----QQTSYLISE-SIrgGGAILVNQQ 745
Cdd:PRK12845 279 HDMEMRWKFQsESLGEHASLGAEGNTGDAIRIAQDLGAAIGLMDQAWWFPAVAplpgGAPAVMLAErSL--PGSLIVDQT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 746 GNRFFNEMETRDKVSAAIIAL-----PEHYAYIVFDEHVRAKNKAADEYIAK----------GFVTSASSPRELAEKLGM 810
Cdd:PRK12845 357 GRRFVNEATDYMSFGQRVLEReragdPVESMWIVFDQQYRNSYVFAAELFPRmpipqawydaGIAHRADSLADLARKIGV 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 811 DYHAFLATLECYNGAVEKQHDEQFGRTTA----------------LRaPINEGPFHAIRIAPGVHHTMGGVTINTDGEVL 874
Cdd:PRK12845 437 PVDTFVATMRRFNEMAAAGVDSDFGRGRSaydryygdptvtpnpnLR-PLDKGPFYAVKMVLSDLGTCGGLRADERARVL 515
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 802145477 875 NVAQQPIRGAYAAGEVVGGIHGGNRIGGNA-VADIIIFGTLAGHQAAKR 922
Cdd:PRK12845 516 REDGSVIDGLYAIGNTAANAFGATYPGAGAtIGQGLVYGYIAAQDAAAR 564
|
|
| PRK07804 |
PRK07804 |
L-aspartate oxidase; Provisional |
500-925 |
3.83e-24 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236102 [Multi-domain] Cd Length: 541 Bit Score: 107.75 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 500 AHDEGASVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLA 579
Cdd:PRK07804 35 ARRAGRRVLVVTKAALDDGSTRWAQGGIAA-------VLDPGDSPEAHVADTLVAGAGLCDPDAVRSLVAEGPRAVRELV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 580 DRGIMLnDITTTGGMSIDRT---HRPR----DGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDE-VSGVRL--- 648
Cdd:PRK07804 108 ALGARF-DESPDGRWALTREgghSRRRivhaGGDATGAEVQRALDAAVRADPLDIREHALALDLLTDGTGaVAGVTLhvl 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 649 -INDEKEVIEVQTKSIVVATGG----FSAnsamvvkyrpdlegfvTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV- 722
Cdd:PRK07804 187 gEGSPDGVGAVHAPAVVLATGGlgqlYAA----------------TTNPAGSTGDGVALALRAGAAVSDLEFVQFHPTVl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 723 -------EQQTsyLISESIRGGGAILVNQQGNRF------FNEMETRDKVSAAIIalpehyayivfdehvraknkaadey 789
Cdd:PRK07804 251 flgpaagGQRP--LISEAVRGEGAILVDAQGNRFmagvhpLADLAPRDVVAKAID------------------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 790 iakgfvtsasspRELAEkLGMDyHAFLatlecyngavEKQHDEQFGR-----TTALRA----PINEgpfhAIRIAPGVHH 860
Cdd:PRK07804 304 ------------RRMKA-TGDD-HVYL----------DARGIEGFARrfptiTASCRAagidPVRQ----PIPVAPAAHY 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802145477 861 TMGGVTINTDGevlnvaQQPIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK07804 356 SCGGVVTDVYG------RTSVPGLYAAGEVACtGVHGANRLASNSLLEGLVVGERAGAAAAAHAAA 415
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
498-925 |
5.54e-24 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 107.58 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIEDSKE--LFYQETLKGGhnKNNPQLLRRFVENAPQAI 575
Cdd:PRK12835 28 LTAAARGLDTLVVEKSAHFGGSTALSGGGIWVPGAPAQRREGYVPDPEdvRRYLKQITGG--LVSAARLRAYVDAAPQMM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 576 EWLADRGIMLNDITTTG--------------GMSID-------------RTHRP-------------------------- 602
Cdd:PRK12835 106 EFLENLSPWLEFVWKPGyadyypelpggsplGSTINvppidlrklgedeQHLLPplalapkgiwftpkdlrlfymvrqtw 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 603 -------------------RDGSAVGGYLISGLVRNITK-RGIDVLLDTSVEEILMRGD-EVSGVRLINDEKEVIEVQTK 661
Cdd:PRK12835 186 agkavllkliwrmvrarvfGRRMAAIGQSLVARLRLALKdAGVPLWLDSPMTELITDPDgAVVGAVVEREGRTLRIGARR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 662 SIVVATGGFSANSAMVVKYRPDLEGF-VTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV---EQQTSYLISESIRGG 737
Cdd:PRK12835 266 GVILATGGFDHDMDWRKEYLPELERKdWSFGNPANTGDGIRAGEKVGAATDLLDEAWWFPAIcwpDGRMQFMLNERMMPA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 738 GAIlVNQQGNRFFNEMETRDKVSAAIIA----LPEHY-AYIVFDehVRAKN----------------------KAADEYI 790
Cdd:PRK12835 346 QFI-VNGAGKRFINEAAPYMDFVHAMIAgqrsGVGHIpCWLVTD--IRSFSryvfgghlpipkipfapvptgrKFPQAWL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 791 AKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALR--------------APINEGPFHAIRIAP 856
Cdd:PRK12835 423 ESGVVKKADTWDELAAKIGVPAENLRATAERFNGLARKGHDDDFNRGDSAYdnyygdptlpnpnlDPLGKPPYYAFRIEL 502
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 857 GVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVGGIHGGNRIGGNA-VADIIIFGTLAGHQAAKRARG 925
Cdd:PRK12835 503 GDLGTSGGLRTDEHARVLREDDSVIPGLYAVGNTSASVMGRSYAGAGAtIGPAMTFGYVAARHAAAVVAA 572
|
|
| PRK07512 |
PRK07512 |
L-aspartate oxidase; Provisional |
539-925 |
2.75e-23 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236036 [Multi-domain] Cd Length: 513 Bit Score: 104.99 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 539 GIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLnDITTTGG--MSIDRTH-RPR------DGSavG 609
Cdd:PRK07512 59 GPDDSPALHAADTLAAGAGLCDPAVAALITAEAPAAIEDLLRLGVPF-DRDADGRlaLGLEAAHsRRRivhvggDGA--G 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 610 GYLISGLVRNITK-RGIDVLLDTSVEEILMRGDEVSGVRLINDEKEViEVQTKSIVVATGGFSANSAmvvkyrpdlegfV 688
Cdd:PRK07512 136 AAIMRALIAAVRAtPSITVLEGAEARRLLVDDGAVAGVLAATAGGPV-VLPARAVVLATGGIGGLYA------------V 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 689 TTNHKGATGSGIALLERIGAGTVDMGEIQIHPT---VEQQTSYLISESIRGGGAILVNQQGNRFF------NEMETRDKV 759
Cdd:PRK07512 203 TTNPAGAFGQGLALAARAGAVIADPEFVQFHPTaidIGRDPAPLATEALRGEGAILINEDGERFMadihpgAELAPRDVV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 760 SAAIIAlpehyayivfdehvraknkaadeyiakgfvtsassprELAEKLGmdyhAFLATLEcyngAVEKQHDEQFGRTTA 839
Cdd:PRK07512 283 ARAVFA-------------------------------------EIAAGRG----AFLDARA----ALGAHFATRFPTVYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 840 L--RAPINegPFHA-IRIAPGVHHTMGGVTINTDGevlnvaQQPIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFGTLA 915
Cdd:PRK07512 318 AcrSAGID--PARQpIPVAPAAHYHMGGIAVDADG------RSSLPGLWAAGEVAStGLHGANRLASNSLLEAVVFAARA 389
|
410
....*....|
gi 802145477 916 GHQAAKRARG 925
Cdd:PRK07512 390 AEDIAGTPAA 399
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
79-237 |
4.67e-22 |
|
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: 98.97 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 79 NDEKIAGLAKIAEAIKAEGSKAILQIYHGGrMVDPQLIGGRQPVAPS--AVAAPREGAAMPRALSGEEVEGMIAKFGDGV 156
Cdd:cd02929 78 DDGDIRNLAAMTDAVHKHGALAGIELWHGG-AHAPNRESRETPLGPSqlPSEFPTGGPVQAREMDKDDIKRVRRWYVDAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 157 RRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDithKMARQYADDAfIIGYRFSPEEMEVP 236
Cdd:cd02929 157 LRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLE---DTKDAVGDDC-AVATRFSVDELIGP 232
|
.
gi 802145477 237 G 237
Cdd:cd02929 233 G 233
|
|
| PRK12837 |
PRK12837 |
FAD-binding protein; |
592-924 |
6.13e-22 |
|
FAD-binding protein;
Pssm-ID: 237222 [Multi-domain] Cd Length: 513 Bit Score: 100.67 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 592 GGMSIDRTHRPRDGSAVGGY-LISGLVRNITK-RGIDVLLDTSVEEILMRGDEVSGVrLINDEKEVIEVQT-KSIVVATG 668
Cdd:PRK12837 154 GPLDTERLGAPPPDYLVGGRaLIGRFLAALARfPNARLRLNTPLVELVVEDGRVVGA-VVERGGERRRVRArRGVLLAAG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 669 GFSANSAMVVKYRPDLEGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHP--TVEQQTSYLiseSIRGGGAILVNQQG 746
Cdd:PRK12837 233 GFEQNDDMRARYGVPGSARDTMGGPGNTGLAHQAAIAVGADTDLMDQAWWSPglTHPDGRSAF---ALWFTGGIFVDQHG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 747 NRFFNEMETRDKVSAAIIA--------LPehyAYIVFDEH------VRAKNKA---ADEYIAKGFVTSASSPRELAEKLG 809
Cdd:PRK12837 310 ERFVNESAPYDRLGRAVIAemdsggmtLP---FWMIYDDRegevppVKATNVSmveTAQYVAAGLWRTADTLEELAAKIG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 810 MDYHAFLATLECYNGAVEKQHDEQFGR--TTALRA---------PINEGPFHAirIAPGVHH--TMGGVTINTDGEVLNV 876
Cdd:PRK12837 387 VPADALTATVARFNGFAAAGVDEDFGRgdEAYDRAfsggasplvPIDTPPFHA--AAFGVSDlgTKGGLRTDTAARVLDT 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 802145477 877 AQQPIRGAYAAGEVVGGIHGGNRI-GGNAVADIIIFGTLAGHQAAKRAR 924
Cdd:PRK12837 465 DGRPIPGLYAAGNTMAAVSGTTYPgGGNPIGASMLFSHLAALDMAGRGP 513
|
|
| COG3976 |
COG3976 |
Uncharacterized conserved protein, contains FMN-binding domain [General function prediction ... |
373-466 |
8.91e-22 |
|
Uncharacterized conserved protein, contains FMN-binding domain [General function prediction only];
Pssm-ID: 443175 Cd Length: 116 Bit Score: 91.50 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 373 SMGDAKFKPGTFVETVHDDANELVINVSLENDHIADIELAASPVQTVEFTTSFEEIRERILTANTPHVDAISGATSQSEA 452
Cdd:COG3976 23 SSAAAKYKDGTYTGTAQGFNGDVTVEVTVSDGKITDIEVLEHGETPGIGDKAIEELPDEIVEAQSLDVDAVSGATLTSKA 102
|
90
....*....|....
gi 802145477 453 VKKAVAKAMLKSSK 466
Cdd:COG3976 103 IKEAVEDALEQAGG 116
|
|
| sdhA |
PRK05945 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
507-925 |
1.62e-21 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 180319 [Multi-domain] Cd Length: 575 Bit Score: 99.81 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 507 VLIVEKMPTIGGNTIKASAGMNAAetrFQRVKGiEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLN 586
Cdd:PRK05945 31 VAVVAKTHPIRSHSVAAQGGIAAS---LKNVDP-EDSWEAHAFDTVKGSDYLADQDAVAILTQEAPDVIIDLEHLGVLFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 587 DIT-------TTGGMSIDRTHRPRDGSavGGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRLINDEKEVIEV- 658
Cdd:PRK05945 107 RLPdgriaqrAFGGHSHNRTCYAADKT--GHAILHELVNNLRRYGVTIYDEWYVMRLILEDNQAKGVVMYHIADGRLEVv 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 659 QTKSIVVATGGFsansamvvkyrpdleGFV---TTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIR 735
Cdd:PRK05945 185 RAKAVMFATGGY---------------GRVfntTSNDYASTGDGLAMTAIAGLPLEDMEFVQFHPTGLYPVGVLISEAVR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 736 GGGAILVNQQGNRFF-----NEME--TRDKVSAAIIAlpehyayivfdeHVRA-KNKAADEYIAKGFVTsaSSPRELAEK 807
Cdd:PRK05945 250 GEGAYLINSEGDRFMadyapSRMElaPRDITSRAITL------------EIRAgRGINPDGSAGGPFVY--LDLRHMGKE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 808 LGMDYHAFlatleCYngavEKQHdeqfgRTTALRApINEgpfhAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAA 887
Cdd:PRK05945 316 KIMSRVPF-----CW----EEAH-----RLVGVDA-VTE----PMPVRPTVHYCMGGIPVNTDGRVRRSADGLVEGFFAA 376
|
410 420 430
....*....|....*....|....*....|....*....
gi 802145477 888 GEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK05945 377 GECACvSVHGANRLGSNSLLECVVYGRRTGAAIAEYVQG 415
|
|
| PRK08401 |
PRK08401 |
L-aspartate oxidase; Provisional |
541-912 |
3.19e-21 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236259 [Multi-domain] Cd Length: 466 Bit Score: 97.95 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 541 EDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSIDRTHRPRdgSAVGGYLISGLVRNI 620
Cdd:PRK08401 53 GDSIRAHVLDTIRAGKYINDEEVVWNVISKSSEAYDFLTSLGLEFEGNELEGGHSFPRVFTIK--NETGKHIIKILYKHA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 621 TKRGIDvLLDTSVEEILMRGDEVSGVRLindEKEVIEVQtkSIVVATGGFSAnsamVVKYrpdlegfvTTNHKGATGSGI 700
Cdd:PRK08401 131 RELGVN-FIRGFAEELAIKNGKAYGVFL---DGELLKFD--ATVIATGGFSG----LFKF--------TAGSPLNLGTLI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 701 ALLERIGAGTVDMGEIQIHPT--VEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIialpehyaYIVFDEh 778
Cdd:PRK08401 193 GDAVMKGAPARDLEFVQFHPTgfIGKRGTYLISEAVRGAGAKLVTGDGERFVNELETRDIVARAI--------YRKMQE- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 779 vraknkaadeyiAKGFVTSASSPRELAEKLGMDYhAFLAtlecyngavekqhdeqfgrttalRAPINEGPfHAIRIAPGV 858
Cdd:PRK08401 264 ------------GKGVFLDATGIEDFKRRFPQIY-AFLR-----------------------KEGIDPSR-DLIPVTPIA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 802145477 859 HHTMGGVTINTdgevlnVAQQPIRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFG 912
Cdd:PRK08401 307 HYTIGGISVDT------FYRTGIKNLYAIGEAAsNGFHGANRLASNSLLECIVSG 355
|
|
| PRK09077 |
PRK09077 |
L-aspartate oxidase; Provisional |
507-915 |
2.42e-19 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236374 [Multi-domain] Cd Length: 536 Bit Score: 92.67 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 507 VLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLN 586
Cdd:PRK09077 33 VAVLSKGPLSEGSTFYAQGGIAA-------VLDETDSIESHVEDTLIAGAGLCDEDAVRFIAENAREAVQWLIDQGVPFT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 587 -----------DITTTGGMSIDRTHRPRD--GSAVGGYLISGLVR--NIT--KRGIDVLLDTSvEEILMRGDEVSGVRLI 649
Cdd:PRK09077 106 tdeqangeegyHLTREGGHSHRRILHAADatGKAVQTTLVERARNhpNITvlERHNAIDLITS-DKLGLPGRRVVGAYVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 650 NDEKE-VIEVQTKSIVVATGGfsanSAMVVKYrpdlegfvTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV---EQQ 725
Cdd:PRK09077 185 NRNKErVETIRAKFVVLATGG----ASKVYLY--------TTNPDIASGDGIAMAWRAGCRVANMEFNQFHPTClyhPQA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 726 TSYLISESIRGGGAILVNQQGNRF---FN---EMETRDKVSAAIialpEHyayivfdehvRAKNKAAD-----------E 788
Cdd:PRK09077 253 RSFLITEALRGEGAYLKLPDGTRFmpdFDeraELAPRDIVARAI----DH----------EMKRLGADcvyldishkpaD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 789 YIAKGFVTSASSPRElaekLGMDyhaflatlecyngavekqhdeqfgrttalrapINEGPfhaIRIAPGVHHTMGGVTIN 868
Cdd:PRK09077 319 FIRQHFPTIYERCLE----LGID--------------------------------ITKEP---IPVVPAAHYTCGGVMVD 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 802145477 869 TDGevlnvaQQPIRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFGTLA 915
Cdd:PRK09077 360 LHG------RTDLDGLYAIGEVSyTGLHGANRMASNSLLECLVYGRSA 401
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
636-916 |
3.01e-17 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 86.33 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 636 ILMRGDEVSGVRLINDEKEVIEV-QTKSIVVATGGFSAnsamvvKYrpdlegFVTTNHKGATGSGIALLERIGAGTVDMG 714
Cdd:PTZ00139 193 IMDEDGECRGVIAMSMEDGSIHRfRAHYTVIATGGYGR------AY------FSCTSAHTCTGDGGAMVSRAGLPLQDLE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 715 EIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFnemetrdkvsaaiialpEHYAyivfdehvrakNKAADeyIAKGF 794
Cdd:PTZ00139 261 FVQFHPTGIYGAGCLITEGCRGEGGILRNSEGERFM-----------------ERYA-----------PTAKD--LASRD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 795 VTSASSPRELAEKLGM----DyHAFL-------ATL-ECYNGAVEKQHdeQFGRTTALRAPInegPfhairIAPGVHHTM 862
Cdd:PTZ00139 311 VVSRAMTIEILEGRGCgpnkD-HIYLdlthlppETLhERLPGISETAK--IFAGVDVTKEPI---P-----VLPTVHYNM 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 802145477 863 GGVTINTDGEVLNVAQ----QPIRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAG 916
Cdd:PTZ00139 380 GGIPTNWKTQVLTQRNgdddKIVPGLLAAGEAAcASVHGANRLGANSLLDIVVFGRAAA 438
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
635-924 |
1.22e-15 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 81.44 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 635 EILMRGD-EVSGVRLINDEKEVIE-VQTKSIVVATGG-----FSANSAMVvkyrpdlegfvttnhkgATGSGIALLERIG 707
Cdd:PLN00128 212 DLIMDSDgACQGVIALNMEDGTLHrFRAHSTILATGGygrayFSATSAHT-----------------CTGDGNAMVARAG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 708 AGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFnemetrdkvsaaiialpEHYAyivfdehVRAKNKAAD 787
Cdd:PLN00128 275 LPLQDLEFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFM-----------------ERYA-------PTAKDLASR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 788 EyiakgfVTSASSPRELAEKLG---MDYHAFLAtLECYNGAVEKQHDEQFGRTTALRAPINEGPfHAIRIAPGVHHTMGG 864
Cdd:PLN00128 331 D------VVSRSMTMEIREGRGvgpEKDHIYLH-LNHLPPEVLKERLPGISETAAIFAGVDVTK-EPIPVLPTVHYNMGG 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802145477 865 VTINTDGEVLNV-AQQP---IRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAGHQAAKRAR 924
Cdd:PLN00128 403 IPTNYHGEVVTIkGDDPdavVPGLMAAGEAAcASVHGANRLGANSLLDIVVFGRACANRVAEIAK 467
|
|
| sdhA |
PRK06452 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
646-921 |
5.74e-15 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 180567 [Multi-domain] Cd Length: 566 Bit Score: 79.16 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 646 VRLINDEKEVIEV-------------QTKSIVVATGGFsansAMVVKYrpdlegfvTTNHKGATGSGIALLERIGAGTVD 712
Cdd:PRK06452 160 LDLVTDNKKVVGIvamqmktltpfffKTKAVVLATGGM----GMLYRH--------TTNSYINTGDGFGIALRAGAALKD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 713 MGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFN-------EMETRDKVSAAII-------ALPEhyAYIVFD-E 777
Cdd:PRK06452 228 PEFVQFHPTALYPSDVLISEAARGEGGILKNVKGERFMTkyapkklDLAPRDIVSRAIIteiregrGFPG--GYVGLDlT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 778 HVraknkaADEYIakgfvtsassprelAEKLGMDYHAflatlecyngavekqhDEQFGRTTALRAPINegpfhairIAPG 857
Cdd:PRK06452 306 HL------GEEYI--------------KERLALAVEA----------------AKSFAGVDAFTEPIP--------VRPA 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802145477 858 VHHTMGGVTINTDGevlnvAQQPIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAK 921
Cdd:PRK06452 342 QHYYMGGIDVDIDG-----RNPDIVGLFSAGEAACvSVHGANRLGSNSLLDTLVFGQVTGRTVVQ 401
|
|
| PLN02815 |
PLN02815 |
L-aspartate oxidase |
506-923 |
4.25e-14 |
|
L-aspartate oxidase
Pssm-ID: 215436 [Multi-domain] Cd Length: 594 Bit Score: 76.29 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 506 SVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIML 585
Cdd:PLN02815 53 TVAIITKDEPHESNTNYAQGGVSA-------VLDPSDSVESHMRDTIVAGAFLCDEETVRVVCTEGPERVKELIAMGASF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 586 ND-------ITTTGGMSIDRTHRPRD--GSAVGGYLISGLV--RNITKRG----IDVLLDTSVEEILMRGDEVSGVRlin 650
Cdd:PLN02815 126 DHgedgnlhLAREGGHSHHRIVHAADmtGREIERALLEAVKndPNITFFEhhfaIDLLTSQDGGSIVCHGADVLDTR--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 651 dEKEVIEVQTKSIVVATGGfsansamvvkyrpdlEGFV---TTNHKGATGSGIALLERIGAGTVDMGEIQIHPTV----- 722
Cdd:PLN02815 203 -TGEVVRFISKVTLLASGG---------------AGHIypsTTNPLVATGDGIAMAHRAQAVVSNMEFVQFHPTAladeg 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 723 -------EQQTSYLISESIRGGGAILVNQQGNRFFN------EMETRDKVSAAIialpehyayivfDEHVRAKN------ 783
Cdd:PLN02815 267 lpikpakARENAFLITEAVRGDGGILYNLAGERFMPlyderaELAPRDVVARSI------------DDQLKKRNekyvll 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 784 ----KAADEyIAKGFvtsassPRELAE--KLGMDyhaflatlecyngavekqhdeqfgrttalrapINEGPfhaIRIAPG 857
Cdd:PLN02815 335 dishKPREE-ILSHF------PNIAAEclKRGLD--------------------------------ITKQP---IPVVPA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802145477 858 VHHTMGGVTINTDGEVlnvaqqPIRGAYAAGEVV-GGIHGGNRIGGNAVADIIIFgtlaghqaAKRA 923
Cdd:PLN02815 373 AHYMCGGVRTGLQGET------NVQGLYAAGEVAcTGLHGANRLASNSLLEALVF--------ARRA 425
|
|
| PRK08626 |
PRK08626 |
fumarate reductase flavoprotein subunit; Provisional |
498-921 |
2.46e-13 |
|
fumarate reductase flavoprotein subunit; Provisional
Pssm-ID: 181507 [Multi-domain] Cd Length: 657 Bit Score: 73.86 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETrfQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEW 577
Cdd:PRK08626 22 IAAAQRGLDTIVLSLVPAKRSHSAAAQGGMQASLG--NAVKGEGDNEDVHFADTVKGSDWGCDQEVARMFVHTAPKAVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 578 LADRGIMLNDIT------------TT----------------GGMSIDRTHRPRDGSavGGYLISGLVRNITKRGIDVLL 629
Cdd:PRK08626 100 LAAWGVPWTRVTagprtvvingekVTitekeeahglinardfGGTKKWRTCYTADGT--GHTMLYAVDNEAIKLGVPVHD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 630 DTSVEEILMRGDEVSG--VR-LINDEkeVIEVQTKSIVVATGGFSAnsamvvKYRpdlegfVTTNHKGATGSGIALLERI 706
Cdd:PRK08626 178 RKEAIALIHDGKRCYGavVRcLITGE--LRAYVAKATLIATGGYGR------IYK------VTTNAVICEGIGAAIALET 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 707 GAGTV-DMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFF-------NEMETRDKVSAAIIalpehyayivfdEH 778
Cdd:PRK08626 244 GVAPLgNMEAVQFHPTAIVPSGILVTEGCRGDGGLLRDKDGYRFMpdyepekKELASRDVVSRRMT------------EH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 779 VRAknkaadeyiAKGfVTSASSP------RELAEKlgmdyhaflatlecyngavekqHDEqfgrtTALR---------AP 843
Cdd:PRK08626 312 IRK---------GKG-VKSPYGPhlwldiRILGRK----------------------HIE-----TNLRevqeicenfLG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 844 INegPFHA-IRIAPGVHHTMGGVTINTDGEvlnvAQQpIRGAYAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAK 921
Cdd:PRK08626 355 ID--PAKDwIPVRPTQHYSMGGIRTNPTGE----SYG-LKGLFSAGEAACwDMHGFNRLGGNSLAETVVAGMIVGKYVAD 427
|
|
| sdhA |
PRK08641 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
498-925 |
3.85e-12 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236319 [Multi-domain] Cd Length: 589 Bit Score: 70.00 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrfQRVKGIEDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEW 577
Cdd:PRK08641 20 IKAAEAGVHVDLFSLVPVKRSHSVCAQGGINGA----VNTKGEGDSPWIHFDDTVYGGDFLANQPPVKAMCEAAPGIIHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 578 LADRGIMLN-------DITTTGGMSIDRTHRPrdGSAVGGYLISGL---VR------NITKR-GIDVLLDTSVEEILMRG 640
Cdd:PRK08641 96 LDRMGVMFNrtpegllDFRRFGGTLHHRTAFA--GATTGQQLLYALdeqVRryevagLVTKYeGWEFLGAVLDDEGVCRG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 641 deVSGVRLINDEKEVIevQTKSIVVATGGfsanSAMVVKyrpdlegfVTTNHKGATGSGIALLERIGAGTVDmGE-IQIH 719
Cdd:PRK08641 174 --IVAQDLFTMEIESF--PADAVIMATGG----PGIIFG--------KSTNSTINTGSAASRVYQQGAYYAN-GEfIQIH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 720 PTV--EQQTSYLISESIRG-GGAILVNQQGNR--FFNEME-------TRDkvsaaiIALPEhyayiVFDEHVRAKNKAAD 787
Cdd:PRK08641 237 PTAipGDDKLRLMSESARGeGGRVWTYKDGKPwyFLEEKYpaygnlvPRD------IATRE-----IFDVCVEQKLGING 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 788 EYIAKGFVTSASsPRELAEKLGmdyhaflATLECYngavekqhdEQFGRTTALRAPInegpfhaiRIAPGVHHTMGGVTI 867
Cdd:PRK08641 306 ENMVYLDLSHKD-PKELDIKLG-------GILEIY---------EKFTGDDPRKVPM--------KIFPAVHYSMGGLWV 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 802145477 868 NTDgevlnvAQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG 925
Cdd:PRK08641 361 DYD------QMTNIPGLFAAGECDYSYHGANRLGANSLLSAIYGGMVAGPNAVEYIKG 412
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
498-707 |
1.68e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 51.43 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKMPTIGgNTIKASAG--MNaaetrfqrVKGIEDSKELFYQetlkggHNKNNP----QLLRRFvenA 571
Cdd:pfam03486 17 ISAAKRGRRVLLIEKGKKLG-RKILISGGgrCN--------VTNLSEEPDNFLS------RYPGNPkflkSALSRF---T 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 572 PQA-IEWLADRGIMLndITTTGGmsidrthR--PRDGSAvgGYLISGLVRNITKRGIDVLLDTSVEEILMRGDEVSGVRL 648
Cdd:pfam03486 79 PWDfIAFFESLGVPL--KEEDHG-------RlfPDSDKA--SDIVDALLNELKELGVKIRLRTRVLSVEKDDDGRFRVKT 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802145477 649 iNDEkeviEVQTKSIVVATGGFSAnsamvvkyrPDLegfvttnhkGATGSGIALLERIG 707
Cdd:pfam03486 148 -GGE----ELEADSLVLATGGLSW---------PKT---------GSTGFGYPLAEQFG 183
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
779-896 |
1.32e-05 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 49.02 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 779 VRA-KNKAADeyiakgFVTsASSPRELAEKL-------GMDYHAFLATLECYNGAVEKQH--DEQFGRTTALRA------ 842
Cdd:COG3573 384 VEAfKDHGED------FVV-ADTLEELVAGMnaltgepLLDAATLRRQIEARDRQIDNPFskDAQIRAIRNARRyrgdrl 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802145477 843 -------PINE---GPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVVG----GIHG 896
Cdd:COG3573 457 irtakphRLLDpkaGPLIAVRLNILTRKTLGGLQTDLDSRVLDADGQPIPGLYAAGEAAGfgggGVHG 524
|
|
| FMN_bind |
smart00900 |
This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR ... |
424-461 |
3.83e-05 |
|
This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins;
Pssm-ID: 214897 [Multi-domain] Cd Length: 86 Bit Score: 43.10 E-value: 3.83e-05
10 20 30
....*....|....*....|....*....|....*....
gi 802145477 424 SFEEIRERILTANTPH-VDAISGATSQSEAVKKAVAKAM 461
Cdd:smart00900 48 ALEKLAKEIVKKQSGGdVDAISGATITSRAVKDAVKRAL 86
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
847-921 |
4.48e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 47.20 E-value: 4.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802145477 847 GPFHAIRIAPGVHHTMGGVTINTDGEVLNVAQQPIRGAYAAGEVV----GGIHGGNRIGGNAVADIIIFGTLAGHQAAK 921
Cdd:PRK12834 470 GPLIAVRLHILTRKTLGGLETDLDSRVLGADGTPLPGLYAAGEAAgfggGGVHGYNALEGTFLGGCIFSGRAAGRAAAR 548
|
|
| sdhA |
PRK07573 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
853-904 |
5.09e-04 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 236054 [Multi-domain] Cd Length: 640 Bit Score: 43.65 E-value: 5.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 802145477 853 RIAPGVHHTMGGVTINTDgevlnvAQQPIRGAYAAGEVVGGIHGGNRIGGNA 904
Cdd:PRK07573 397 RIYPAVHYTMGGLWVDYN------LMSTIPGLFVIGEANFSDHGANRLGASA 442
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
498-672 |
5.47e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 43.36 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 498 IQAHDEGASVLIVEKmPTIGGNTIKASAGM---------NAAETRF-----QRVKGIEDS--KELFYQET--LKGGHNKN 559
Cdd:COG0665 19 YHLARRGLDVTVLER-GRPGSGASGRNAGQlrpglaalaDRALVRLarealDLWRELAAElgIDCDFRRTgvLYLARTEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802145477 560 NPQLLRRFVENAPQA---IEWL-----ADRGIMLNDITTTGGMsidrtHRPRDGSAVGGYLISGLVRNITKRGIDVLLDT 631
Cdd:COG0665 98 ELAALRAEAEALRALglpVELLdaaelREREPGLGSPDYAGGL-----YDPDDGHVDPAKLVRALARAARAAGVRIREGT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 802145477 632 SVEEILMRGDEVSGVRLINDekeviEVQTKSIVVATGGFSA 672
Cdd:COG0665 173 PVTGLEREGGRVTGVRTERG-----TVRADAVVLAAGAWSA 208
|
|
| |
