|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06481 |
PRK06481 |
flavocytochrome c; |
498-924 |
0e+00 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 585.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:PRK06481 78 IEAKDAGMNPVILEKMPVAGGNTMKASSGMNASETKFQKAQGIADSNDKFYEETLKGGGGTNDKALLRYFVDNSASAIDW 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGIMLNDITTTGGMSIDRTHRPKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVI 657
Cdd:PRK06481 158 LDSMGIKLDNLTITGGMSEKRTHRPHDGSAVGGYLVDGLLKNVQERKIPLFVNADVTKITEKDGKVTGVKVKINGKETKT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 658 VATKSVIVATGGFSANSQMVVKYRPDLEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIRGG 737
Cdd:PRK06481 238 ISSKAVVVTTGGFGANKDMIAKYRPDLKGYVTTNQEGSTGDGIKMIEKLGGTTVDMDQIQIHPTVQQSKSYLIGEAVRGE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 738 GAILVNQKGERFYNEMSTRDKVSAQIIALPEKYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPKALAEALGMDHHAFLA 817
Cdd:PRK06481 318 GAILVNQKGKRFGNELDTRDKVSAAINKLPEKYAYVVFDSGVKDRVKAIAQYEEKGFVEEGKTIDELAKKINVPAETLTK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 818 TLERYNGFVEKQHDDDFGRTTALRAPINEGPFYAIQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGGIHGG 897
Cdd:PRK06481 398 TLDTWNKAVKNKKDEAFGRTTGMDNDLSTGPYYAIKIAPGIHYTMGGVKINTNTEVLKKDGSPITGLYAAGEVTGGLHGE 477
|
410 420
....*....|....*....|....*..
gi 504697314 898 NRIGGNAVADIIIFGTLAGHQAAMRAK 924
Cdd:PRK06481 478 NRIGGNSVADIIIFGRQAGTQSAEFAK 504
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
7-360 |
2.40e-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: 483.64 E-value: 2.40e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLPNGTELKNRLLMAPMTTCTGYYDGTVTSELVEYYRARSGSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIAGL 86
Cdd:cd04735 1 LFEPFTLKNGVTLKNRFVMAPMTTYSSNPDGTITDDELAYYQRRAGGVGMVITGATYVSPSGIGFEGGFSADDDSDIPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 87 AKIAEAIKSKGSKALLQIYHGGRMVDPKLIGGRTPVGPSAVAAPRDGAATPVALTAEEVEGMIGKFGEAVRRAIQAGFDG 166
Cdd:cd04735 81 RKLAQAIKSKGAKAILQIFHAGRMANPALVPGGDVVSPSAIAAFRPGAHTPRELTHEEIEDIIDAFGEATRRAIEAGFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 167 VEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDITHKMVRQYADDAFIIGYRFSPEELEVPGIRFEDTMYL 246
Cdd:cd04735 161 VEIHGANGYLIQQFFSPHSNRRTDEWGGSLENRMRFPLAVVKAVQEVIDKHADKDFILGYRFSPEEPEEPGIRMEDTLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 247 LEKLAARGVDYLHFSVGATLRPSIVDtQDPTPLIEKYCAMRSEtlAQVPVMGVGGVVNASDVNDALDHGYDLIAVGRATI 326
Cdd:cd04735 241 VDKLADKGLDYLHISLWDFDRKSRRG-RDDNQTIMELVKERIA--GRLPLIAVGSINTPDDALEALETGADLVAIGRGLL 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 504697314 327 AYPDWTDRIAAGESLE--LFMDSTKREELNIPEPLW 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 |
1.22e-163 |
|
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: 485.31 E-value: 1.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEG-ASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIE 576
Cdd:TIGR01813 16 LSAKKAGaANVVLLEKMPVIGGNSAIAAGGMNAAGTDQQKALGIEDSPELFIKDTLKGGRGINDPELVRILAEESKDAVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 577 WLATR-GIMLNDITTTGGMSIDRTHRPKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIF-ENGEVTGVRLTTEENE 654
Cdd:TIGR01813 96 WLQDGvGARLDDLIQLGGHSVPRAHRPTGGAASGAEIVQTLYKKAKKEGIDTRLNSKVEDLIQdDQGSVVGVVVKGKGKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 655 TVIVATKSVIVATGGFSANSQMVVKYRPDLEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTS-YLISES 733
Cdd:TIGR01813 176 IYIKAAKAVVLATGGFGSNKEMIAKYDPTLKHLGSTNQPGATGDGLLMAEKIGAALVDMDYIQAHPTASPDEGgFLISEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 734 IRGGGAILVNQKGERFYNEMSTRDKVSAQIIALPEKYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPKALAEALGMDHH 813
Cdd:TIGR01813 256 VRGYGAILVNKTGERFMNELATRDKVSDAILAQPGKDAYLIFDDDVYKKAKMVDNYYRLGVAYKGDSLEELAKQFGIPAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 814 AFLATLERYNGFVEKQHDDDFGRTTALRAPINEGPFYAIQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGG 893
Cdd:TIGR01813 336 ALKQTIKDYNGYVASGKDTPFGRPMDMPTDLSKAPYYAIKVTPGVHHTMGGVKINTKAEVLDANGKPIPGLFAAGEVTGG 415
|
410 420
....*....|....*....|...
gi 504697314 894 IHGGNRIGGNAVADIIIFGTLAG 916
Cdd:TIGR01813 416 VHGANRLGGNAIADCIVFGRIAG 438
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
498-924 |
2.40e-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: 2.40e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGiQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:COG1053 20 LEAAEAGLKVLVLEKVPPRGGHTAAAQGGINAAGTNVQKAAG-EDSPEEHFYDTVKGGDGLADQDLVEALAEEAPEAIDW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGIMLN-----DITTTGGMSIDRTHRPKDGSavGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEE 652
Cdd:COG1053 99 LEAQGVPFSrtpdgRLPQFGGHSVGRTCYAGDGT--GHALLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVVARDRT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 653 NETVIVATKSVIVATGGFSANSQMVVKYRPDLEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISE 732
Cdd:COG1053 177 GEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEGALSTNAPGNTGDGIAMALRAGAALADMEFVQFHPTGLPGDGGLISE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 733 SIRGG-GAILVNQKGERFYNEMSTRDKVSAQIIALPEKYAYIVFDEHVRaknKAADEYIAKGFVTSASSPKALAEALGMD 811
Cdd:COG1053 257 GARGKpGGILVNKEGERFMNEYAPRDVVSRAILEEIDEPAYLVLDLRHR---RRLEEYLEAGYLVKADTIEELAAKLGID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 812 HHAFLATLERYNGFVEKQHDDdfgRTTALRaPINEGPFYAIQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVV 891
Cdd:COG1053 334 AAELAATVARYNAAAKAGVDP---RGTCLG-PIKEGPFYAIPVRPGVHYTMGGLRVDADARVLDADGTPIPGLYAAGEAA 409
|
410 420 430
....*....|....*....|....*....|...
gi 504697314 892 GGIHGGNRIGGNAVADIIIFGTLAGHQAAMRAK 924
Cdd:COG1053 410 GSVHGANRLGGNSLGDALVFGRIAGRHAAEYAK 442
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
1-343 |
6.25e-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: 358.71 E-value: 6.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 1 MSTNERILSPFTLpNGTELKNRLLMAPMTTCTGYYDGTVTSELVEYYRAR-SGSIGTIIVECCFVDDLGLAFPGAIGIDN 79
Cdd:COG1902 1 MMKMPKLFSPLTL-GGLTLKNRIVMAPMTRGRADEDGVPTDLHAAYYAQRaRGGAGLIITEATAVSPEGRGYPGQPGIWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 80 DEKIAGLAKIAEAIKSKGSKALLQIYHGGRMVDPKLIGGRTPVGPSAVAAPRDGAaTPVALTAEEVEGMIGKFGEAVRRA 159
Cdd:COG1902 80 DEQIAGLRRVTDAVHAAGGKIFIQLWHAGRKAHPDLPGGWPPVAPSAIPAPGGPP-TPRALTTEEIERIIEDFAAAARRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 160 IQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDIthkmVRQYADDAFIIGYRFSPEELEVPGIR 239
Cdd:COG1902 159 KEAGFDGVEIHGAHGYLLDQFLSPLTNQRTDEYGGSLENRARFLLEVVEA----VRAAVGPDFPVGVRLSPTDFVEGGLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 240 FEDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTQDP----------------TPLIekyCAMRSETLAQvpvmgvggvv 303
Cdd:COG1902 235 LEESVELAKALEEAGVDYLHVSSGGYEPDAMIPTIVPegyqlpfaarirkavgIPVI---AVGGITTPEQ---------- 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 504697314 304 nasdVNDALDHGY-DLIAVGRATIAYPDWTDRIAAGESLEL 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 |
6.58e-98 |
|
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: 310.27 E-value: 6.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 8 LSPFTLpNGTELKNRLLMAPMTTCTGYYDGTVTSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIAGL 86
Cdd:cd02803 1 FSPIKI-GGLTLKNRIVMAPMTENMATEDGTPTDELIEYYEERAkGGVGLIITEAAYVDPEGKGYPGQLGIYDDEQIPGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 87 AKIAEAIKSKGSKALLQIYHGGRMVDPKLIGGrTPVGPSAVAAPRDGAaTPVALTAEEVEGMIGKFGEAVRRAIQAGFDG 166
Cdd:cd02803 80 RKLTEAVHAHGAKIFAQLAHAGRQAQPNLTGG-PPPAPSAIPSPGGGE-PPREMTKEEIEQIIEDFAAAARRAKEAGFDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 167 VEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLdithKMVRQYADDAFIIGYRFSPEELEVPGIRFEDTMYL 246
Cdd:cd02803 158 VEIHGAHGYLLSQFLSPYTNKRTDEYGGSLENRARFLLEIV----AAVREAVGPDFPVGVRLSADDFVPGGLTLEEAIEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 247 LEKLAARGVDYLHFSVGATLRP-SIVDTQDPTPLIEKYCAMRSETLAQVPVMGVGGVVNASDVNDALDHGY-DLIAVGRA 324
Cdd:cd02803 234 AKALEEAGVDALHVSGGSYESPpPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKaDLVALGRA 313
|
330
....*....|....
gi 504697314 325 TIAYPDWTDRIAAG 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 |
2.13e-78 |
|
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: 258.56 E-value: 2.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLPNgTELKNRLLMAPMTTCTGYYDGTVTSELVEYYRARSgSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIAGL 86
Cdd:cd02933 2 LFSPLKLGN-LTLKNRIVMAPLTRSRADPDGVPTDLMAEYYAQRA-SAGLIITEATQISPQGQGYPNTPGIYTDEQVEGW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 87 AKIAEAIKSKGSKALLQIYHGGRMVDPKLI-GGRTPVGPSAVAAP--------RDGAATPVALTAEEVEGMIGKFGEAVR 157
Cdd:cd02933 80 KKVTDAVHAKGGKIFLQLWHVGRVSHPSLLpGGAPPVAPSAIAAEgkvftpagKVPYPTPRALTTEEIPGIVADFRQAAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 158 RAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLdithkmvrqyadDAFI-------IGYRFSp 230
Cdd:cd02933 160 NAIEAGFDGVEIHGANGYLIDQFLRDGSNKRTDEYGGSIENRARFLLEVV------------DAVAeaigadrVGIRLS- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 231 eelevPGIRF--------EDTM-YLLEKLAARGVDYLHFSVGATLRPSIVDTQDPTPLIEKY------CAMRsetlaqvp 295
Cdd:cd02933 227 -----PFGTFndmgdsdpEATFsYLAKELNKRGLAYLHLVEPRVAGNPEDQPPDFLDFLRKAfkgpliAAGG-------- 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504697314 296 vmgvggvVNASDVNDALDHGY-DLIAVGRATIAYPDWTDRIAAGESL 341
Cdd:cd02933 294 -------YDAESAEAALADGKaDLVAFGRPFIANPDLVERLKNGAPL 333
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
496-920 |
2.73e-73 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 262.79 E-value: 2.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 496 AAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQESLKGG-GNKNNPELLRRFVENAPEA 574
Cdd:PTZ00306 424 AAIEAASCGAQVILLEKEAKLGGNSAKATSGINGWGTRAQAKQDVLDGGKFFERDTHLSGkGGHCDPGLVKTLSVKSADA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 575 IEWLATRGIMLNDITTTGGMSIDRTHRP---KDGSAVG-GYLI----SGLVRNVNKRNIEVMLDTSVSDIIFENGE---- 642
Cdd:PTZ00306 504 ISWLSSLGVPLTVLSQLGGASRKRCHRApdkKDGTPVPiGFTImrtlEDHIRTKLSGRVTIMTETTVTSLLSESSArpdg 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 643 -----VTGVRLT--TEENETVIVAT-KSVIVATGGFS----ANSqMVVKYRPDLEGFVTTNHKGATGGGIALLERIGAGT 710
Cdd:PTZ00306 584 vreirVTGVRYKqaSDASGQVMDLLaDAVILATGGFSndhtPNS-LLREYAPQLSGFPTTNGPWATGDGVKLARKLGATL 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 711 VDMGEIQIHPT--VEQK-----TSYLISESIRGGGAILVNQKGERFYNEMSTRDKVSAQIIA----LP----EKYAYIVF 775
Cdd:PTZ00306 663 VDMDKVQLHPTglIDPKdpsnrTKYLGPEALRGSGGVLLNKNGERFVNELDLRSVVSQAIIAqgneYPgsggSKFAYCVL 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 776 -DEHVRAKNKAADEYIAK--GFVTSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGRTTALRAPI-NEGPFYA 851
Cdd:PTZ00306 743 nEAAAKLFGKNSLGFYWKrlGLFQRVDDVKGLAKLIGCPVENLHRTLETYERLSTKKVACPLTGKVVFPCVVgTQGPYYV 822
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504697314 852 IQIAPGVHHTMGGVTINTETCVLDSNH--NVLP------GAFAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAA 920
Cdd:PTZ00306 823 AFVTPSIHYTMGGCLISPSAEMQMEDNsvNIFEdrrpilGLFGAGEVTGGVHGGNRLGGNSLLECVVFGKIAGDRAA 899
|
|
| Oxidored_FMN |
pfam00724 |
NADH:flavin oxidoreductase / NADH oxidase family; |
7-342 |
8.39e-71 |
|
NADH:flavin oxidoreductase / NADH oxidase family;
Pssm-ID: 395587 [Multi-domain] Cd Length: 341 Bit Score: 238.12 E-value: 8.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLPNgTELKNRLLMAPMTTCTGYYDGTV-TSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIA 84
Cdd:pfam00724 2 LFEPIKIGN-TTLKNRIVMAPMTRLRSLDDGTKaTGLLAEYYSQRSrGPGTLIITEGAFVNPQSGGFDNGPRIWDDEQIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 85 GLAKIAEAIKSKGSKALLQIYHGGR------MVDPKLIGgrtPVGPSAVAAPRDGAATPV-ALTAEEVEGMIGKFGEAVR 157
Cdd:pfam00724 81 GWRKLTEAVHKNGSKAGVQLWHLGReapmeyRPDLEVDG---PSDPFALGAQEFEIASPRyEMSKEEIKQHIQDFVDAAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 158 RAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDithkMVRQYADDAFIIGYRFSPEELEVPG 237
Cdd:pfam00724 158 RAREAGFDGVEIHGANGYLINQFLSPGTNQRTDEYGGSLENRARFPLEVVD----AVKEAVGQERIVGYRLSPFDVVGPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 238 IRFEDTMYLLEKLAARGVDYLHFSVGAtlrpsIVDTQDPTPL----IEKYCAMRSETLAQVPVMGVGGVVN---ASDVND 310
Cdd:pfam00724 234 LDFAETAQFIYLLAELGVRLPDGWHLA-----YIHAIEPRPRgagpVRTRQQHNTLFVKGVWKGPLITVGRiddPSVAAE 308
|
330 340 350
....*....|....*....|....*....|...
gi 504697314 311 ALDHGY-DLIAVGRATIAYPDWTDRIAAGESLE 342
Cdd:pfam00724 309 IVSKGRaDLVAMGRPFLADPDLPFKAKKGRPLN 341
|
|
| OYE_YqiM_FMN |
cd02932 |
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ... |
7-337 |
1.04e-59 |
|
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: 207.35 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLpNGTELKNRLLMAPMttCTgyY---DGTVTS-ELVEY-YRARSGsIGTIIVECCFVDDLGLAFPGAIGIDNDE 81
Cdd:cd02932 1 LFTPLTL-RGVTLKNRIVVSPM--CQ--YsaeDGVATDwHLVHYgSRALGG-AGLVIVEATAVSPEGRITPGDLGLWNDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 82 KIAGLAKIAEAIKSKGSKALLQIYHGGR------------MVDPKLIGGRTPVGPSAVAApRDGAATPVALTAEEVEGMI 149
Cdd:cd02932 75 QIEALKRIVDFIHSQGAKIGIQLAHAGRkastappwegggPLLPPGGGGWQVVAPSAIPF-DEGWPTPRELTREEIAEVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 150 GKFGEAVRRAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDIthkmVRQYADDAFIIGYRFS 229
Cdd:cd02932 154 DAFVAAARRAVEAGFDVIEIHAAHGYLLHQFLSPLSNKRTDEYGGSLENRMRFLLEVVDA----VRAVWPEDKPLFVRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 230 PEELEVPGIRFEDTMYLLEKLAARGVDYLHFSVGATLrPSIVDTQDP---TPLIEkycAMRSEtlAQVPVMGVGGVVNAS 306
Cdd:cd02932 230 ATDWVEGGWDLEDSVELAKALKELGVDLIDVSSGGNS-PAQKIPVGPgyqVPFAE---RIRQE--AGIPVIAVGLITDPE 303
|
330 340 350
....*....|....*....|....*....|..
gi 504697314 307 DVNDALDHG-YDLIAVGRATIAYPDWTDRIAA 337
Cdd:cd02932 304 QAEAILESGrADLVALGRELLRNPYWPLHAAA 335
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
498-905 |
6.91e-57 |
|
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: 201.36 E-value: 6.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:pfam00890 16 LAAAEAGLKVAVVEKGQPFGGATAWSSGGIDAL---GNPPQGGIDSPELHPTDTLKGLDELADHPYVEAFVEAAPEAVDW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGIMLN-------DITTTGGMSIDRTH-----RPKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTG 645
Cdd:pfam00890 93 LEALGVPFSrtedghlDLRPLGGLSATWRTphdaaDRRRGLGTGHALLARLLEGLRKAGVDFQPRTAADDLIVEDGRVTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 646 VRLT--TEENETVIVATKSVIVATGGFSANSQMvvkYRPDLEGFVTTNHKGATGGGIALLERIGAGTVD--MGEIQIHPT 721
Cdd:pfam00890 173 AVVEnrRNGREVRIRAIAAVLLATGGFGRLAEL---LLPAAGYADTTNPPANTGDGLALALRAGAALTDdlMEFVQFHPT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 722 VEQKT---SYLISESIRGGGAILVNQKGERFYNEMSTRDKVSAQIIalpekyayivfdEHVRAKNKAADEY-IAKGfvts 797
Cdd:pfam00890 250 SLVGIrlgSGLLIEALRGEGGILVNKDGRRFMNELASRDVVSRAIT------------RNEIDEGRGANVYlDASG---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 798 asspkalaealGMDHHAFLATLERYNGFVEKQHDDDfgrttalrapINEGPfyaIQIAPGVHHTMGGVTINTETCVLDSN 877
Cdd:pfam00890 314 -----------SLDAEGLEATLPAINEEAIFGLDVD----------PYDRP---IPVFPAQHYTMGGVRTDENGRVLDAD 369
|
410 420
....*....|....*....|....*....
gi 504697314 878 HNVLPGAFAAGEVV-GGIHGGNRIGGNAV 905
Cdd:pfam00890 370 GQPIPGLYAAGEVAcGGVHGANRLGGNSL 398
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
7-263 |
4.10e-54 |
|
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: 191.64 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLPNGTELKNRLLMAPMTTCTGYYDGTVTSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIG---IDNDEK 82
Cdd:cd04733 1 LGQPLTLPNGATLPNRLAKAAMSERLADGRGLPTPELIRLYRRWAeGGIGLIITGNVMVDPRHLEEPGIIGnvvLESGED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 83 IAGLAKIAEAIKSKGSKALLQIYHGGRMVdPKLIGgRTPVGPSAVA---APRDGAATPVALTAEEVEGMIGKFGEAVRRA 159
Cdd:cd04733 81 LEAFREWAAAAKANGALIWAQLNHPGRQS-PAGLN-QNPVAPSVALdpgGLGKLFGKPRAMTEEEIEDVIDRFAHAARLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 160 IQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFplaVLDITHKmVRQYADDAFIIGYRFSPEELEVPGIR 239
Cdd:cd04733 159 QEAGFDGVQIHAAHGYLLSQFLSPLTNKRTDEYGGSLENRARL---LLEIYDA-IRAAVGPGFPVGIKLNSADFQRGGFT 234
|
250 260
....*....|....*....|....
gi 504697314 240 FEDTMYLLEKLAARGVDYLHFSVG 263
Cdd:cd04733 235 EEDALEVVEALEEAGVDLVELSGG 258
|
|
| PRK10605 |
PRK10605 |
N-ethylmaleimide reductase; Provisional |
5-341 |
5.08e-54 |
|
N-ethylmaleimide reductase; Provisional
Pssm-ID: 182584 [Multi-domain] Cd Length: 362 Bit Score: 192.25 E-value: 5.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 5 ERILSPFTLPNGTeLKNRLLMAPMTTCTGYYDGTVTSELV-EYYRARSGSiGTIIVECCFVDDLGLAFPGAIGIDNDEKI 83
Cdd:PRK10605 1 EKLFSPLKVGAIT-APNRVFMAPLTRLRSIEPGDIPTPLMaEYYRQRASA-GLIISEATQISAQAKGYAGAPGLHSPEQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 84 AGLAKIAEAIKSKGSKALLQIYHGGRMVDPKL-IGGRTPVGPSAVAAP-------------RDGAATPVALTAEEVEGMI 149
Cdd:PRK10605 79 AAWKKITAGVHAEGGHIAVQLWHTGRISHASLqPGGQAPVAPSAINAGtrtslrdengqaiRVETSTPRALELEEIPGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 150 GKFGEAVRRAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDIThkmVRQYADDAfiIGYRFS 229
Cdd:PRK10605 159 NDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAG---IAEWGADR--IGIRIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 230 P----EELEVPGIRFEDTMYLLEKLAARGVDYLHFSvgatlRPsivDTQDPTPLIEkycAMRSETLAQ-VPVMGVGGVVN 304
Cdd:PRK10605 234 PlgtfNNVDNGPNEEADALYLIEQLGKRGIAYLHMS-----EP---DWAGGEPYSD---AFREKVRARfHGVIIGAGAYT 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 504697314 305 ASDVNDALDHGY-DLIAVGRATIAYPDWTDRIAAGESL 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 |
3.44e-53 |
|
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: 188.98 E-value: 3.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLpNGTELKNRLLMAPMTTctGY-YDGTVTSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIA 84
Cdd:cd04734 1 LLSPLQL-GHLTLRNRIVSTAHAT--NYaEDGLPSERYIAYHEERArGGAGLIITEGSSVHPSDSPAFGNLNASDDEIIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 85 GLAKIAEAIKSKGSKALLQIYHGGRMVDPKlIGGRTPVGPSAVAAPRDgAATPVALTAEEVEGMIGKFGEAVRRAIQAGF 164
Cdd:cd04734 78 GFRRLAEAVHAHGAVIMIQLTHLGRRGDGD-GSWLPPLAPSAVPEPRH-RAVPKAMEEEDIEEIIAAFADAARRCQAGGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 165 DGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDithkMVRQYADDAFIIGYRFSPEELEVPGIRFEDTM 244
Cdd:cd04734 156 DGVELQAAHGHLIDQFLSPLTNRRTDEYGGSLENRMRFLLEVLA----AVRAAVGPDFIVGIRISGDEDTEGGLSPDEAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 245 YLLEKLAARG-VDYLHFSVG--ATLRPSiVDTQDPTPLIEKYCAMRSETLAQVPVMGVGGVVNASDVNDA---LDHGY-D 317
Cdd:cd04734 232 EIAARLAAEGlIDYVNVSAGsyYTLLGL-AHVVPSMGMPPGPFLPLAARIKQAVDLPVFHAGRIRDPAEAeqaLAAGHaD 310
|
330 340
....*....|....*....|...
gi 504697314 318 LIAVGRATIAYPDWTDRIAAGES 340
Cdd:cd04734 311 MVGMTRAHIADPHLVAKAREGRE 333
|
|
| OYE_like_5_FMN |
cd04747 |
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN ... |
7-343 |
1.27e-51 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 5. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240095 [Multi-domain] Cd Length: 361 Bit Score: 185.21 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLpNGTELKNRLLMAPMTTctGYYDGTV-TSELVEYYRARS-GSIGTIIVECCFVDD-LGLAFPGAIGIDNDEKI 83
Cdd:cd04747 1 LFTPFTL-KGLTLPNRIVMAPMTR--SFSPGGVpGQDVAAYYRRRAaGGVGLIITEGTAVDHpAASGDPNVPRFHGEDAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 84 AGLAKIAEAIKSKGSKALLQIYHGG--RMVDPKLIGGRTPVGPSAVAAPRDGAATPvaLTAEEVEGMIGKFGEAVRRAIQ 161
Cdd:cd04747 78 AGWKKVVDEVHAAGGKIAPQLWHVGamRKLGTPPFPDVPPLSPSGLVGPGKPVGRE--MTEADIDDVIAAFARAAADARR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 162 AGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLdithKMVRQYADDAFIIGYRFS------------ 229
Cdd:cd04747 156 LGFDGIELHGAHGYLIDQFFWAGTNRRADGYGGSLAARSRFAAEVV----KAIRAAVGPDFPIILRFSqwkqqdytarla 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 230 --PEELEVpgirfedtmyLLEKLAARGVDYLHFSV---------GATL-----------RPSI------VDTQDptplie 281
Cdd:cd04747 232 dtPDELEA----------LLAPLVDAGVDIFHCSTrrfwepefeGSELnlagwtkkltgLPTItvgsvgLDGDF------ 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504697314 282 kYCAMRSETLAQvpvmgvggVVNASDVNDALDHG-YDLIAVGRATIAYPDWTDRIAAGESLEL 343
Cdd:cd04747 296 -IGAFAGDEGAS--------PASLDRLLERLERGeFDLVAVGRALLSDPAWVAKVREGRLDEL 349
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
498-923 |
2.11e-49 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 182.78 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNA-AETRFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIE 576
Cdd:PRK07121 37 IEAAAAGARVLVLERAAGAGGATALSGGVIYLgGGTAVQKAAGFEDSPENMYAYLRVAVGPGVDEEKLRRYCEGSVEHFD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 577 WLATRGI-----------------------------MLNDITTtggmSIDRTHRPK--DGSAVGGYLISGLVRNVNKRNI 625
Cdd:PRK07121 117 WLEGLGVpfersffpektsyppndeglyysgnekawPFAEIAK----PAPRGHRVQgpGDSGGGAMLMDPLAKRAAALGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 626 EVMLDTSVSDIIFE-NGEVTGVRLTTEENETVIVATKSVIVATGGFSANSQMVVKYRPDLEGFV---TTNHKGAtggGIA 701
Cdd:PRK07121 193 QIRYDTRATRLIVDdDGRVVGVEARRYGETVAIRARKGVVLAAGGFAMNREMVARYAPAYAGGLplgTTGDDGS---GIR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 702 LLERIGAGTVDMGEIQIhptveqkTSYLISESIRGGGaILVNQKGERFYNEMSTRDKVSAQIIALPEKYAYIVFDEHVRA 781
Cdd:PRK07121 270 LGQSAGGATAHMDQVFA-------WRFIYPPSALLRG-ILVNARGQRFVNEDTYGARIGQFILEQPGGTAYLIVDEALFE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 782 KNKAADEYIAKGFVT---SASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGRTTALRAPINEGPFYAIQIAPGV 858
Cdd:PRK07121 342 EARAQLRPQIDGRTPgawKAETVEELARKLGIPPGGLQATVDAYNRAAAGGEDPPFHKQPEWLRPLDTGPFAAIDLSLGK 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 859 ----HHTMGGVTINTETC-VLDSNHNVLPGAFAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAMRA 923
Cdd:PRK07121 422 aptpGFTLGGLRVDEDTGeVLRADGAPIPGLYAAGRCASGIASNGYVSGLSLADCSFFGRRAGRHAAARA 491
|
|
| PRK13523 |
PRK13523 |
NADPH dehydrogenase NamA; Provisional |
6-264 |
6.14e-47 |
|
NADPH dehydrogenase NamA; Provisional
Pssm-ID: 184110 [Multi-domain] Cd Length: 337 Bit Score: 171.04 E-value: 6.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 6 RILSPFTLPNGTeLKNRLLMAPMTTCTGY-YDGTVTSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIGIDNDEKI 83
Cdd:PRK13523 2 KLFSPYTIKDVT-LKNRIVMSPMCMYSSEnKDGKVTNFHLIHYGTRAaGQVGLVIVEATAVLPEGRISDKDLGIWDDEHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 84 AGLAKIAEAIKSKGSKALLQIYHGGR--MVDPkliggrTPVGPSAVAApRDGAATPVALTAEEVEGMIGKFGEAVRRAIQ 161
Cdd:PRK13523 81 EGLHKLVTFIHDHGAKAAIQLAHAGRkaELEG------DIVAPSAIPF-DEKSKTPVEMTKEQIKETVLAFKQAAVRAKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 162 AGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDithkMVRQYADDAFIIgyRFSPEELEVPGIRFE 241
Cdd:PRK13523 154 AGFDVIEIHGAHGYLINEFLSPLSNKRTDEYGGSPENRYRFLREIID----AVKEVWDGPLFV--RISASDYHPGGLTVQ 227
|
250 260
....*....|....*....|...
gi 504697314 242 DTMYLLEKLAARGVDYLHFSVGA 264
Cdd:PRK13523 228 DYVQYAKWMKEQGVDLIDVSSGA 250
|
|
| DCR_FMN |
cd02930 |
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ... |
7-263 |
4.12e-46 |
|
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: 169.39 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 7 ILSPFTLpNGTELKNRLLMAPMTTCTGYYDGTVtSELVEYYRARS-GSIGTIIVECCFVDDLGLAFPGAIGIDNDEKIAG 85
Cdd:cd02930 1 LLSPLDL-GFTTLRNRVLMGSMHTGLEELDDGI-DRLAAFYAERArGGVGLIVTGGFAPNEAGKLGPGGPVLNSPRQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 86 LAKIAEAIKSKGSKALLQIYHGGRMVDPKLIggrtpVGPSAVAAPRDgAATPVALTAEEVEGMIGKFGEAVRRAIQAGFD 165
Cdd:cd02930 79 HRLITDAVHAEGGKIALQILHAGRYAYHPLC-----VAPSAIRAPIN-PFTPRELSEEEIEQTIEDFARCAALAREAGYD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 166 GVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLdithKMVRQYADDAFIIGYRFSPEELEVPGIRFEDTMY 245
Cdd:cd02930 153 GVEIMGSEGYLINQFLAPRTNKRTDEWGGSFENRMRFPVEIV----RAVRAAVGEDFIIIYRLSMLDLVEGGSTWEEVVA 228
|
250
....*....|....*...
gi 504697314 246 LLEKLAARGVDYLHFSVG 263
Cdd:cd02930 229 LAKALEAAGADILNTGIG 246
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
498-926 |
5.07e-46 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 172.37 E-value: 5.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPtiggntiKASAGMNAAETRFQRV--KGIQD------SKELFYQESLKGGGNKNNPELLRRFVE 569
Cdd:PRK08274 21 LAAREAGASVLLLEAAP-------REWRGGNSRHTRNLRCmhDAPQDvlvgayPEEEFWQDLLRVTGGRTDEALARLLIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 570 NAPEAIEWLATRGIMLNDItttggmsIDRTHRPKDGSAV----GGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTG 645
Cdd:PRK08274 94 ESSDCRDWMRKHGVRFQPP-------LSGALHVARTNAFfwggGKALVNALYRSAERLGVEIRYDAPVTALELDDGRFVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 646 VRLTTEENETVIVATKSVIVATGGFSANSQMVVKY-RPDLEGFVTTNHKGATGGGIALLERIGAGTV-DMGEIQIHPT-- 721
Cdd:PRK08274 167 ARAGSAAGGAERIRAKAVVLAAGGFESNREWLREAwGQPADNFLVRGTPYNQGDLLKALLDAGADRIgDPSQCHAVAIda 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 722 ---------VEQKTSYLIsesirgggAILVNQKGERFYNE-----MSTRDKVSAQIIALPEKYAYIVFDEhvraknKAAD 787
Cdd:PRK08274 247 raplydggiCTRIDCVPL--------GIVVNRDGERFYDEgedfwPKRYAIWGRLVAQQPGQIAYQIFDA------KAIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 788 EYIAKGFV-TSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDD----DFGRTTALR-------APINEGPFYAIQIA 855
Cdd:PRK08274 313 RFMPPVFPpIQADTLEELAEKLGLDPAAFLRTVAAFNAAVRPGPFDptvlDDCGTEGLTppkshwaRPIDTPPFYAYPVR 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504697314 856 PGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGG-IHGGNRIGGNAVADIIIFGTLAGHQAAMRAKMA 926
Cdd:PRK08274 393 PGITFTYLGLKVDEDARVRFADGRPSPNLFAAGEMMAGnVLGKGYPAGVGLTIGAVFGRIAGEEAARHAQHE 464
|
|
| sdhA |
PRK06263 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
503-923 |
2.86e-45 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 235758 [Multi-domain] Cd Length: 543 Bit Score: 171.70 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 503 EGASVLIVEKmpTI---GGNTIKASAGMNAaetrfqrVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLA 579
Cdd:PRK06263 28 RGKNVVIVSK--GLfgkSGCTVMAEGGYNA-------VLNPEDSFEKHFEDTMKGGAYLNDPKLVEILVKEAPKRLKDLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 580 TRGiMLNDITTT--------GGMSIDRTHRPKDGSavGGYLISGLVRNVNKRNIEVMLDTSVSDIIF-ENGEVTG-VRLT 649
Cdd:PRK06263 99 KFG-ALFDRTEDgeiaqrpfGGQSFNRTCYAGDRT--GHEMMMGLMEYLIKERIKILEEVMAIKLIVdENREVIGaIFLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 650 TEENETVIVATKSVIVATGGfsaNSQMvvkYRpdlegfVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPT----VEQK 725
Cdd:PRK06263 176 LRNGEIFPIYAKATILATGG---AGQL---YP------ITSNPIQKTGDGFAIAYRAGAELIDMEMVQFHPTgmvyPYSG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 726 TSYLISESIRGGGAILVNQKGERF---YN----EMSTRDKVSAQIialpekYAYIvfdehvraknkaadeyiakgfvtsa 798
Cdd:PRK06263 244 RGILVTEAVRGEGGILYNKNGERFmkrYDpermELSTRDVVARAI------YTEI------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 799 sspkalAEALGMDHHA-FLATLERYNGFVEKQHDDDFGRTTALRAPINEGPfyaIQIAPGVHHTMGGVTINtETCvlDSN 877
Cdd:PRK06263 293 ------QEGRGTNHGGvYLDVTHLPDEVIEEKLETMLEQFLDVGVDIRKEP---MEVAPTAHHFMGGIRIN-EDC--ETN 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 504697314 878 hnvLPGAFAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAMRA 923
Cdd:PRK06263 361 ---IPGLFACGEVAGGVHGANRLGGNALADTQVFGAIAGKSAAKNA 403
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
500-924 |
1.43e-43 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 166.85 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 500 AHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKE--LFYQESLKGG-GNKNNPELLRRFVENAPEAIE 576
Cdd:PRK12844 25 AADSGLEPLIVEKQDKVGGSTAMSGGVLWLPNNPLMKAAGVPDSHEdaLAYLDAVVGDqGPASSPERREAYLRAGPAMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 577 WLATRG----------------------------------------------------IMLNDITTTGGMSIDRTHRPKD 604
Cdd:PRK12844 105 FLEHQGmrfarcegwsdyypdlpggeargrsleakpfdarklgpwfdrlnppmatppgTVVMTDEYKWLQLIKRTPRGMR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 605 GSA------------------VGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVA 666
Cdd:PRK12844 185 TAArvgartlaarirgqklltNGAALIGRMLEAALAAGVPLWTNTPLTELIVEDGRVVGVVVVRDGREVLIRARRGVLLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 667 TGGFSANSQMVVKYRPD-LEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIRGG----GAIL 741
Cdd:PRK12844 265 SGGFGHNAEMRKRYQPQpNSGDWTNANPGDTGEVIEAAMRLGAALDLMDEAWWVPGAPLPNGGPRPYMHNSErskpGSII 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 742 VNQKGERFYNEMSTRDKVSAQIIALPEKYAYIVFDEHVRAK--------NKAADEYIAKGFVTSASSPKALAEALGMDHH 813
Cdd:PRK12844 345 VDRAGRRFVNEAGSYMEVGRAMYAQDAVPAWMIMDSRYRKRylfgtippGPTPQEWLDSGYMKRADTIEELAGKTGIDPA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 814 AFLATLERYNGFVEKQHDDDFGR---------------TTALRAPINEGPFYAIQIAPGVHHTMGGVTINTETCVLDSNH 878
Cdd:PRK12844 425 GLAATVERFNGFAATGTDPDFHRgesaydryygdptnkPNPSLGPLDKPPFYAVRMVPGDVGTSGGLLTDEHARVLREDG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 504697314 879 NVLPGAFAAGEVVGGIHGGNRIG-GNAVADIIIFGTLAGHQAAMRAK 924
Cdd:PRK12844 505 SVIPGLYATGNCTASVMGRTYPGaGASIGNSFVFGYIAALHAAGARS 551
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
498-920 |
5.47e-42 |
|
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: 161.43 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGaSVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:COG0029 21 LKLAERG-RVTLLTKGELGESNTRWAQGGIAA-------VLDPGDSPELHIADTLAAGAGLCDPEAVRVLVEEGPERIRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGImlnDITTT----------GGMSIDRTHRPKDgsAVGGYLISGLVRNVNKR-NIEVMLDTSVSDIIFE-NGEVTG 645
Cdd:COG0029 93 LIELGV---PFDRDedgelaltreGGHSRRRILHAGD--ATGREIERALLEAVRAHpNITVLENHFAVDLITDaDGRCVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 646 VR-LTTEENETVIVATKSVIVATGGFSansQMvvkYRpdlegfVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV-- 722
Cdd:COG0029 168 AYvLDEKTGEVETIRAKAVVLATGGAG---QL---YA------YTTNPDVATGDGIAMAYRAGARLADMEFVQFHPTAly 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 723 -EQKTSYLISESIRGGGAILVNQKGERF---YN---EMSTRDKVS----AQIIALPEKYAYIvfDehVRAKNKaadEYIA 791
Cdd:COG0029 236 hPGAPSFLISEAVRGEGAVLRNADGERFmpdYHpraELAPRDVVAraidAEMKKTGGDCVYL--D--ISHLDA---EFIR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 792 KGFvtsassPK--ALAEALGMDhhaflatleryngfvekqhdddfgrttalrapINEGPfyaIQIAPGVHHTMGGVTINT 869
Cdd:COG0029 309 ERF------PTiyARCLELGID--------------------------------ITKEP---IPVAPAAHYTMGGVATDL 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 504697314 870 --ETCVldsnhnvlPGAFAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAGHQAA 920
Cdd:COG0029 348 dgRTSI--------PGLYAVGEVAcTGVHGANRLASNSLLEGLVFGRRAAEDIA 393
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
607-923 |
8.91e-36 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 143.64 E-value: 8.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 607 AVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVATGGFSANSQMVVKYRPDLEG 686
Cdd:PRK07843 205 GMGQALAAGLRIGLQRAGVPVLLNTPLTDLYVEDGRVTGVHAAESGEPQLIRARRGVILASGGFEHNEQMRAKYQRAPIG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 687 FV-TTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV--EQKTSYLISESIRGGGaILVNQKGERFYNE-MSTRDKVSAQ 762
Cdd:PRK07843 285 TEwTVGAKANTGDGILAGEKLGAALDLMDDAWWGPTIplPGGPWFALSERNLPGS-IIVNMSGKRFMNEsAPYVEAVHHM 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 763 IIALPEKY--------AYIVFDEHVRAKNKAAD---------EYIAKGFVTSASSPKALAEALGMDHHAFLATLERYNGF 825
Cdd:PRK07843 364 YGGEYGQGpgpgenipAWLVFDQRYRDRYLFAGlqprqpipsRWLESGVIVKADTLAELAAKIGVPADALTATVQRFNGF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 826 VEKQHDDDFGRTTALR---------------APINEGPFYAIQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEV 890
Cdd:PRK07843 444 ARSGVDEDFHRGESAYdryygdptnkpnpnlGELSHAPFYAAKMVPGDLGTKGGLRTDVRGRVLRDDGSVIEGLYAAGNV 523
|
330 340 350
....*....|....*....|....*....|....
gi 504697314 891 VGGIHGGNRIG-GNAVADIIIFGTLAGHQAAMRA 923
Cdd:PRK07843 524 SAPVMGHTYAGpGATIGPAMTFGYLAALDIAAQA 557
|
|
| sdhA |
PRK06069 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
505-924 |
7.80e-35 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 235689 [Multi-domain] Cd Length: 577 Bit Score: 140.96 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 505 ASVLIVEKMPTIGGNTIKASAGMNAA---ETrfqrvkgiQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATR 581
Cdd:PRK06069 32 LSVAVVSKTQPMRSHSVSAEGGTAAVlypEK--------GDSFDLHAYDTVKGSDFLADQDAVEVFVREAPEEIRFLDHW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 582 G----------IMLNDItttGGMSIDRTHRPKDGSavGGYLISGLVRNVNK-RNIEVMLDTSVSDIIFENGEVTGVR-LT 649
Cdd:PRK06069 104 GvpwsrrpdgrISQRPF---GGMSFPRTTFAADKT--GFYIMHTLYSRALRfDNIHFYDEHFVTSLIVENGVFKGVTaID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 650 TEENETVIVATKSVIVATGGFSAnsqmvvkyrpdLEGFVTTNHKgATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYL 729
Cdd:PRK06069 179 LKRGEFKVFQAKAGIIATGGAGR-----------LYGFTTYAHS-VTGDGLAIAYRAGIPLKDMEFVQFHPTGLVPSGIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 730 ISESIRGGGAILVNQKGERFYN-------EMSTRDKVSAQIIAlpekyayivfdehvraknkaadEYIA-KGFVTSASSP 801
Cdd:PRK06069 247 ITEAARGEGGYLINKEGERFMKryapqkmELAPRDVVSRAIMT----------------------EIMEgRGFKHESGLC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 802 KALaeaLGMDHHAFLATLERYNGFVEKQHdddfgrTTALRAPINEgpfyAIQIAPGVHHTMGGVTINTETCVLDSNHNVL 881
Cdd:PRK06069 305 YVG---LDLRHLGEEKINERLPLIREIAK------KYAGIDPVTE----PIPVRPAAHYTMGGIHTDVYGRVLTADGEWV 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 504697314 882 PGAFAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAMRAK 924
Cdd:PRK06069 372 RGLWAAGEAAAvSVHGANRLGSNSTAECLVWGRIAGEQAAEYAL 415
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
503-924 |
1.65e-34 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 140.26 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 503 EGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKE---LFYQESLkggGNKNNPELLRRFVENAPEAIEWL- 578
Cdd:PRK12843 38 AGLKVLLVERTEYVGGTTATSAGTTWIPGTRHGLAVGPDDSLEaarTYLDALV---GDRSPEELRDAFLASGPRAIAFLe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 579 -----------------------ATRGIMLN---------------------DITTTGGMSIDRT--------------- 599
Cdd:PRK12843 115 ansevkfrayashpdyesdlpgaTLRGRALEplpfdgrklgadfalirppipEFTVLGGMMVDRTdvghllaltkswraf 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 600 ----------------HRPKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSV 663
Cdd:PRK12843 195 rhavrllaryardrisYARGTRLVMGNALIGRLLYSLRARGVRILTQTDVESLETDHGRVIGATVVQGGVRRRIRARGGV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 664 IVATGGFSANSQMVVKYRPDLEGFVTTNHKGATGGGIALLERIGA----GTVDMG---EIQIHPTVEQKTS---YLISEs 733
Cdd:PRK12843 275 VLATGGFNRHPQLRRELLPAAVARYSPGAPGHTGAAIDLALDAGArygrGLLSNAfwaPVSVRRRADGSTAvfpHFYLD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 734 iRGG-GAILVNQKGERFYNEMSTRDKVSAQIIA----LPEKYAYIVFDEH---------VRAKNKAADEYIAKGFVTSAS 799
Cdd:PRK12843 354 -RGKpGTIAVNQQGRRFVNESTSYHLFGTAMFAagktSPGIPAYLITDAEflrkyglgmVRPGGRGLAPFLRDGYLTVAS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 800 SPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGR-TTALR--------------APINEGPFYAIQIAPGVHHTMGG 864
Cdd:PRK12843 433 TLDELAPKLGIDPAALAATVQRHNQYARTGIDPDFGRgATAYQrmngdamigpnpnlGPIETAPFYAVRLYPGDIGAATG 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504697314 865 VTINTETCVLDSNHNVLPGAFAAGEVVGGIHGGNRIG-GNAVADIIIFGTLAGHQAAMRAK 924
Cdd:PRK12843 513 LVTDASARVLNADGQPISGLYACGNDMASIMGGTYPGpGITLGPAIVFAYLAARHAAKRTL 573
|
|
| PRK06175 |
PRK06175 |
L-aspartate oxidase; Provisional |
502-911 |
1.84e-34 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 180442 [Multi-domain] Cd Length: 433 Bit Score: 137.51 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 502 DEGASVLIVEKMPTIGGNTIKASAGMNAAetrfqrvKGIQDsKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATR 581
Cdd:PRK06175 24 RKDLKILMVSKGKLNECNTYLAQGGISVA-------RNKDD-ITSFVEDTLKAGQYENNLEAVKILANESIENINKLIDM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 582 GIMLN------DITTTGGMSIDRTHRPKDgsAVGGYLISGLVRNVNKR-NIEVMLDTSVSDIIFENGEVTGVRLTTEeNE 654
Cdd:PRK06175 96 GLNFDkdekelSYTKEGAHSVNRIVHFKD--NTGKKVEKILLKKVKKRkNITIIENCYLVDIIENDNTCIGAICLKD-NK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 655 TVIVATKSVIVATGGFSA---NSqmvvkyrpdlegfvtTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV-----EQKT 726
Cdd:PRK06175 173 QINIYSKVTILATGGIGGlfkNS---------------TNQRIITGDGIAIAIRNNIKIKDLDYIQIHPTAfyeetIEGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 727 SYLISESIRGGGAILVNQKGERFYNEMSTRDKVSAQIIALPEK--YAYIVFDehVRAKNKaadEYIAKGFVTSasspkal 804
Cdd:PRK06175 238 KFLISESVRGEGGKLLNSKGERFVDELLPRDVVTKAILEEMKKtgSNYVYLD--ITFLDK---DFLKNRFPTI------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 805 aealgmdhhaflatlerYNGFVEKQHDddfgrttalraPINEgpfyAIQIAPGVHHTMGG--VTINTETcvldSNHNVlp 882
Cdd:PRK06175 306 -----------------YEECLKRGID-----------ITKD----AIPVSPAQHYFMGGikVDLNSKT----SMKNL-- 347
|
410 420 430
....*....|....*....|....*....|
gi 504697314 883 gaFAAGEV-VGGIHGGNRIGGNAVADIIIF 911
Cdd:PRK06175 348 --YAFGEVsCTGVHGANRLASNSLLEGLVF 375
|
|
| PLN02411 |
PLN02411 |
12-oxophytodienoate reductase |
4-230 |
3.23e-34 |
|
12-oxophytodienoate reductase
Pssm-ID: 178033 [Multi-domain] Cd Length: 391 Bit Score: 135.75 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 4 NERILSPFTLPNgTELKNRLLMAPMTTCTGYyDGTVTSELVEYYRARSGSIGTIIVECCFVDDLGLAFPGAIGIDNDEKI 83
Cdd:PLN02411 9 NETLFSPYKMGR-FDLSHRVVLAPMTRCRAL-NGIPNAALAEYYAQRSTPGGFLISEGTLISPTAPGFPHVPGIYSDEQV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 84 AGLAKIAEAIKSKGSKALLQIYHGGR----MVDPkliGGRTPVGPSA--------VAAPrDGA----ATPVALTAEEVEG 147
Cdd:PLN02411 87 EAWKKVVDAVHAKGSIIFCQLWHVGRashqVYQP---GGAAPISSTNkpiserwrILMP-DGSygkyPKPRALETSEIPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 148 MIGKFGEAVRRAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFplaVLDITHKMVRQYADDAfiIGYR 227
Cdd:PLN02411 163 VVEHYRQAALNAIRAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSIENRCRF---LMQVVQAVVSAIGADR--VGVR 237
|
...
gi 504697314 228 FSP 230
Cdd:PLN02411 238 VSP 240
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
498-923 |
1.59e-31 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 131.08 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKE--LFYQESLKGGgnKNNPELLRRFVENAPEAI 575
Cdd:PRK12835 28 LTAAARGLDTLVVEKSAHFGGSTALSGGGIWVPGAPAQRREGYVPDPEdvRRYLKQITGG--LVSAARLRAYVDAAPQMM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 576 EWLATRGIMLNDITTTG--------------GMSID-------------RTHR-------------PKD----------- 604
Cdd:PRK12835 106 EFLENLSPWLEFVWKPGyadyypelpggsplGSTINvppidlrklgedeQHLLpplalapkgiwftPKDlrlfymvrqtw 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 605 -GSAVGGYLISGLVRNVNKR---------------------NIEVMLDTSVSDIIF-ENGEVTGVRLTTEENETVIVATK 661
Cdd:PRK12835 186 aGKAVLLKLIWRMVRARVFGrrmaaigqslvarlrlalkdaGVPLWLDSPMTELITdPDGAVVGAVVEREGRTLRIGARR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 662 SVIVATGGFSANSQMVVKYRPDLEGF-VTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV---EQKTSYLISESIRGG 737
Cdd:PRK12835 266 GVILATGGFDHDMDWRKEYLPELERKdWSFGNPANTGDGIRAGEKVGAATDLLDEAWWFPAIcwpDGRMQFMLNERMMPA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 738 GAIlVNQKGERFYNEMS-----TRDKVSAQIIALPEKYAYIVFDehVRAKN----------------------KAADEYI 790
Cdd:PRK12835 346 QFI-VNGAGKRFINEAApymdfVHAMIAGQRSGVGHIPCWLVTD--IRSFSryvfgghlpipkipfapvptgrKFPQAWL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 791 AKGFVTSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGRTTALR--------------APINEGPFYAIQIAP 856
Cdd:PRK12835 423 ESGVVKKADTWDELAAKIGVPAENLRATAERFNGLARKGHDDDFNRGDSAYdnyygdptlpnpnlDPLGKPPYYAFRIEL 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504697314 857 GVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGGIHGGNRIGGNA-VADIIIFGTLAGHQAAMRA 923
Cdd:PRK12835 503 GDLGTSGGLRTDEHARVLREDDSVIPGLYAVGNTSASVMGRSYAGAGAtIGPAMTFGYVAARHAAAVV 570
|
|
| ER_like_FMN |
cd02931 |
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ... |
18-343 |
3.47e-31 |
|
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: 126.47 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 18 ELKNRLLMAPMTT---CTgyYDGTVTSELVEYYRARS-GSIGTIIVECCFVDDLGLAFP-GAIGIDNDEK---IAGLAKI 89
Cdd:cd02931 11 EIKNRFAMAPMGPlglAD--NDGAFNQRGIDYYVERAkGGTGLIITGVTMVDNEIEQFPmPSLPCPTYNPtafIRTAKEM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 90 AEAIKSKGSKALLQIYHG-GRMVDPKLIGGRTPVGPSAVAAPRDGAATPVALTAEEVEGMIGKFGEAVRRAIQAGFDGVE 168
Cdd:cd02931 89 TERVHAYGTKIFLQLTAGfGRVCIPGFLGEDKPVAPSPIPNRWLPEITCRELTTEEVETFVGKFGESAVIAKEAGFDGVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 169 IHGANT-YLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLdithKMVRQYADDAFIIGYRFSPEEL-------EVPGIRF 240
Cdd:cd02931 169 IHAVHEgYLLDQFTISLFNKRTDKYGGSLENRLRFAIEIV----EEIKARCGEDFPVSLRYSVKSYikdlrqgALPGEEF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 241 EDTMYLLEK-LAA----RGVDYLHFSVGATLRPSIVDTQDPT----PLIEKYCAMRSETLaQVPVMGVGGVVNASDVNDA 311
Cdd:cd02931 245 QEKGRDLEEgLKAakilEEAGYDALDVDAGSYDAWYWNHPPMyqkkGMYLPYCKALKEVV-DVPVIMAGRMEDPELASEA 323
|
330 340 350
....*....|....*....|....*....|...
gi 504697314 312 LDHGY-DLIAVGRATIAYPDWTDRIAAGESLEL 343
Cdd:cd02931 324 INEGIaDMISLGRPLLADPDVVNKIRRGRFKNI 356
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
498-920 |
1.77e-29 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 124.81 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:PRK12842 26 ITARKLGLDVVVLEKEPVFGGTTAFSGGVLWIPGNPHAREAGVADSREAARTYLKHETGAFFDAAAVEAFLDNGPEMVEF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LAT-------------------------RGIM-------------------LNDITTTGGMS----------IDRTHRPK 603
Cdd:PRK12842 106 FERetevkfvptlypdyhpdapggvdigRSILaapydirglgkdmarlrppLKTITFIGMMFnssnadlkhfFNATRSLT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 604 DGSAV----------------------GGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATK 661
Cdd:PRK12842 186 SFIYVakrlathlkdlalyrrgtqvtsGNALAARLAKSALDLGIPILTGTPARELLTEGGRVVGARVIDAGGERRITARR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 662 SVIVATGGFSANSQMVVKYRPDLEgfVTTNH-----KGATGGGIALLERIGA---------------GTVDM--GEIQIH 719
Cdd:PRK12842 266 GVVLACGGFSHDLARIARAYPHLA--RGGEHlspvpAGNTGDGIRLAEAVGGavdirfpdaaawmpvSKVPLggGRTGVF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 720 PTVEQKTSylisesirgGGAILVNQKGERFYNEM-STRDKVSAQIIA---LPEKYAYIVFDEHVRAK-----NKAA---- 786
Cdd:PRK12842 344 PHLLDRYK---------PGVIGVLRNGKRFTNESnSYHDVGAAMIRAcegQKETAMWLICDRATLRKyglgyAKPApmpv 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 787 DEYIAKGFVTSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGR-TTALR--------------APINEGPFYA 851
Cdd:PRK12842 415 GPLLRNGYLIKGDTLAELAGKAGIDAAGLEATVRRYNEGAVKGIDPAFGRgSTSFNrylgdpdhkpnpcvAPIGSGPFYA 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 852 IQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGGIHGGNRIG-GNAVADIIIFGTLAGHQAA 920
Cdd:PRK12842 495 VKVIMGDLGTFDGLRTDVTGEVLDADGTPIAGLYAVGNDRASIMGGNYPGaGITLGPIMTFGYITGRHLA 564
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
504-920 |
3.28e-29 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 123.68 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 504 GASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELfYQESLKGG-GNKNNPELLRRFVENAPEAIEWL---- 578
Cdd:PRK06134 35 GLKVIVVEKDPVFGGTTAWSGGWMWIPRNPLARRAGIVEDIEQ-PRTYLRHElGARYDAARIDAFLEAGPHMVAFFerht 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 579 ATRGIMLNDIT---------TTGGMS---------------------IDRT----------------------------- 599
Cdd:PRK06134 114 ALRFADGNAIPdyhgdtpgaATGGRSliaapfdgrelgallerlrkpLRETsfmgmpimagadlaaflnptrsfraflhv 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 600 ---------HRPKDGSAV----GGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVA 666
Cdd:PRK06134 194 arrfarhliDLARHGRGMhlvnGNALVARLLKSAEDLGVRIWESAPARELLREDGRVAGAVVETPGGLQEIRARKGVVLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 667 TGGFSANSQMvvkyRPDLEGFVTTNH-------KGATGGGIALLERIGaGTVDM------------------GEIQIHPt 721
Cdd:PRK06134 274 AGGFPHDPAR----RAALFPRAPTGHehlslppPGNSGDGLRLGESAG-GVVATdlaspvawapvslvphadGSVGHFP- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 722 veqktsYLISesiRGG-GAILVNQKGERFYNEM-STRDKVSAQIIALPEK---YAYIVFDE---------HVRAKNKAAD 787
Cdd:PRK06134 348 ------HIIE---RGKpGLIGVLANGKRFVNEAdSYHDYVAAMFAATPPGqpvRSWLICDHrflrryglgHIRPAPLPLG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 788 EYIAKGFVTSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGR-TTALR---------------APINEGPFYA 851
Cdd:PRK06134 419 PYVRSGYLKRGASLEELARACGIDPDGLEATVARYNRHARNGQDPDFGRgSTPYNrkqgdpahggpnpcvAPIEHGPFYA 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504697314 852 IQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAG----EVVGGIHGGnriGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK06134 499 VKVLPGCLGTFAGLKTDADARVLDQAGQPIPGLYAAGndmaSVMGGFYPS---GGITLGPALTFGYIAGRHIA 568
|
|
| PRK08071 |
PRK08071 |
L-aspartate oxidase; Provisional |
519-917 |
1.99e-28 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236147 [Multi-domain] Cd Length: 510 Bit Score: 120.48 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 519 NTIKASAGMNAAETRfqrvkgiQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGiMLNDITTTGGMSIDR 598
Cdd:PRK08071 40 NSHLAQGGIAAAVAT-------YDSPNDHFEDTLVAGCHHNNERAVRYLVEEGPKEIQELIENG-MPFDGDETGPLHLGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 599 --THRPK-----DGSAVGGYLISGLVRNVNKRnIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVATGGFS 671
Cdd:PRK08071 112 egAHRKRrilhaGGDATGKNLLEHLLQELVPH-VTVVEQEMVIDLIIENGRCIGVLTKDSEGKLKRYYADYVVLASGGCG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 672 ANSQmvvkyrpdlegfVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPT---VEQKTSYLISESIRGGGAILVNQKGER 748
Cdd:PRK08071 191 GLYA------------FTSNDKTITGDGLAMAYRAGAELVDLEFIQFHPTmlyANGRCVGLVSEAVRGEGAVLINEDGRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 749 FYN------EMSTRDKVSAQIialpekYAYIVFDEHVRAkNKAADEYIAKGFVTSAsspkALAEALGMDhhaflatlery 822
Cdd:PRK08071 259 FMMgihplaDLAPRDVVARAI------HEELLSGEKVYL-NISSIQNFEERFPTIS----ALCEKNGVD----------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 823 ngfvekqhdddfgrttalrapINEGpfyAIQIAPGVHHTMGGVTINT--ETCVldsnhnvlPGAFAAGEVV-GGIHGGNR 899
Cdd:PRK08071 317 ---------------------IETK---RIPVVPGAHFLMGGVKTNLdgETSI--------PGLYAIGEVAcTGVHGANR 364
|
410
....*....|....*...
gi 504697314 900 IGGNAVADIIIFGTLAGH 917
Cdd:PRK08071 365 LASNSLLEGLVFGKRAAE 382
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
529-926 |
2.50e-28 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 121.28 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 529 AAETRFQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLN-------DITTTGGMSIDRTHR 601
Cdd:PRK09231 47 AAEGGSAAVAQDHDSFDYHFHDTVAGGDWLCEQDVVEYFVHHCPTEMTQLEQWGCPWSrkpdgsvNVRRFGGMKIERTWF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 602 PKDGSavGGYLISGLVRNVNK-RNIEVMLDTSVSDIIFENGEVTG-VRLTTEENETVIVATKSVIVATGGfsanSQMVVK 679
Cdd:PRK09231 127 AADKT--GFHMLHTLFQTSLKyPQIQRFDEHFVLDILVDDGHVRGlVAMNMMEGTLVQIRANAVVMATGG----AGRVYR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 680 YrpdlegfvTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIRGGGAILVNQKGERF---------- 749
Cdd:PRK09231 201 Y--------NTNGGIVTGDGMGMAYRHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKDGYRYlqdyglgpet 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 750 --------YNEMSTRDKVSAqiialpekyayiVFDEHVRAKNkaadeyiakgfvtSASSPKALAEALGMDH--HAFLatL 819
Cdd:PRK09231 273 plgepknkYMELGPRDKVSQ------------AFWHEWRKGN-------------TISTPRGDVVYLDLRHlgEKKL--H 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 820 ERYngfvekqhddDFGRTTAlRAPINEGPFYA-IQIAPGVHHTMGG--VTINTETCvldsnhnvLPGAFAAGEVVG-GIH 895
Cdd:PRK09231 326 ERL----------PFICELA-KAYVGVDPVKEpIPVRPTAHYTMGGieTDQNCETR--------IKGLFAVGECSSvGLH 386
|
410 420 430
....*....|....*....|....*....|.
gi 504697314 896 GGNRIGGNAVADIIIFGTLAGHQAAMRAKMA 926
Cdd:PRK09231 387 GANRLGSNSLAELVVFGRVAGEQAAERAATA 417
|
|
| PRK12837 |
PRK12837 |
FAD-binding protein; |
592-915 |
7.29e-28 |
|
FAD-binding protein;
Pssm-ID: 237222 [Multi-domain] Cd Length: 513 Bit Score: 118.78 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 592 GGMSIDRTHRPKDGSAVGGY-LISGLVRNVNK-RNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVATGG 669
Cdd:PRK12837 154 GPLDTERLGAPPPDYLVGGRaLIGRFLAALARfPNARLRLNTPLVELVVEDGRVVGAVVERGGERRRVRARRGVLLAAGG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 670 FSANSQMVVKYRPDLEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHP--TVEQKTSYLiseSIRGGGAILVNQKGE 747
Cdd:PRK12837 234 FEQNDDMRARYGVPGSARDTMGGPGNTGLAHQAAIAVGADTDLMDQAWWSPglTHPDGRSAF---ALWFTGGIFVDQHGE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 748 RFYNEMSTRDKVSAQIIALPEKYA-----YIVFDEH------VRAKNKA---ADEYIAKGFVTSASSPKALAEALGMDHH 813
Cdd:PRK12837 311 RFVNESAPYDRLGRAVIAEMDSGGmtlpfWMIYDDRegevppVKATNVSmveTAQYVAAGLWRTADTLEELAAKIGVPAD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 814 AFLATLERYNGFVEKQHDDDFGR--TTALRA---------PINEGPFYAiqIAPGVHH--TMGGVTINTETCVLDSNHNV 880
Cdd:PRK12837 391 ALTATVARFNGFAAAGVDEDFGRgdEAYDRAfsggasplvPIDTPPFHA--AAFGVSDlgTKGGLRTDTAARVLDTDGRP 468
|
330 340 350
....*....|....*....|....*....|....*.
gi 504697314 881 LPGAFAAGEVVGGIHGGNRI-GGNAVADIIIFGTLA 915
Cdd:PRK12837 469 IPGLYAAGNTMAAVSGTTYPgGGNPIGASMLFSHLA 504
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
498-920 |
8.55e-28 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 119.55 E-value: 8.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFyQESLKG--GGNKNNPELlRRFVENAPEAI 575
Cdd:PRK12839 25 VAAAYGGAKVLVVEKASTCGGATAWSGGWMWTPGNSLARADGVVEDKEEP-RTYLEHrlGENYDADKV-DALLDGAPEMV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 576 EWLATR-------GIMLNDI--------------------------------------TTTGGMSIDR------------ 598
Cdd:PRK12839 103 DFFEKKtalqfvpGAKIADIygdlpgagtghrsvgpkpvnlrklgpdvaallrhqlyeTSFLGMGIMAgpdlqaflhatq 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 599 --------------------THRPKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDI-IFENGEVTGVRLTTEENETVI 657
Cdd:PRK12839 183 dpkgfvhaarrvivhmwdlaTHRRGMQLVNGTALTGRLLRSADDLGVDLRVSTSATSLtTDKNGRVTGVRVQGPDGAVTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 658 VATKSVIVATGGFSANSQM---VVKYRPDLEGFVTTNHKGATGGGIALLERIGAG-------TVDMGEIQIHPTVEQKTS 727
Cdd:PRK12839 263 EATRGVVLATGGFPNDVDRrkeLFPRTPTGREHWTLAPAETTGDGISLAESVGARldrdlasPAAWCPVSLVPYRNGKVG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 728 YLISESIRGG-GAILVNQKGERFYNE-MSTRDKVSAQIIALPEK---YAYIVFDE-HVR------AKNKAAD--EYIAKG 793
Cdd:PRK12839 343 TFPHIMDRGKpGSIGVLATGKRFVNEaNGYYDYTLAMVKAAPEGepvCSWLIADSrFVRkyplgmAKPLPVPltPYLRSG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 794 FVTSASSPKALAEALGMDHHAFLATLERYNGFVEKQHDDDFGR-TTALR--------------APINEGPFYAIQIAPGV 858
Cdd:PRK12839 423 YLTRGRTIEELAEKCGIDPAGLEATVAEFNENARDGEDPEFGRgTTPFNrgsgdpdngpnpslAPLEKGPFYAVKVVPGS 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504697314 859 HHTMGGVTINTETCVLDSNHNVLPGAFAAGEVVGGIHGGNR-IGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK12839 503 FGTFAGLVADGKSRVLRDDDTPIDGLYAAGNDQASVMGGHYpSGGINLGPAMTFGYIAGRELA 565
|
|
| PRK08255 |
PRK08255 |
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase; |
8-337 |
2.11e-27 |
|
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
Pssm-ID: 236203 [Multi-domain] Cd Length: 765 Bit Score: 119.27 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 8 LSPFTLpNGTELKNRLLMAPMT--TCTgyyDGTVTS-ELVEY-YRARSGSiGTIIVECCFVDDLGLAFPGAIGIDNDEKI 83
Cdd:PRK08255 400 FTPFRL-RGLTLKNRVVVSPMAmySAV---DGVPGDfHLVHLgARALGGA-GLVMTEMTCVSPEGRITPGCPGLYNDEQE 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 84 AGLAKIAEAIKSKGS-KALLQIYHGGRM---------VDPKLIGGRTP-VGPSAVAApRDGAATPVALTAEEVEGMIGKF 152
Cdd:PRK08255 475 AAWKRIVDFVHANSDaKIGIQLGHSGRKgstrlgwegIDEPLEEGNWPlISASPLPY-LPGSQVPREMTRADMDRVRDDF 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 153 GEAVRRAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDithkMVRQYADDAFIIGYRFSPEE 232
Cdd:PRK08255 554 VAAARRAAEAGFDWLELHCAHGYLLSSFISPLTNQRTDEYGGSLENRLRYPLEVFR----AVRAVWPAEKPMSVRISAHD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 233 LEVPGIRFEDTMYLLEKLAARGVDYLHFSVGATLRpsivdTQDP-------TPLIEKycaMRSE----TLAqvpvmgVGG 301
Cdd:PRK08255 630 WVEGGNTPDDAVEIARAFKAAGADLIDVSSGQVSK-----DEKPvygrmyqTPFADR---IRNEagiaTIA------VGA 695
|
330 340 350
....*....|....*....|....*....|....*..
gi 504697314 302 VVNASDVNDALDHGY-DLIAVGRATIAYPDWTDRIAA 337
Cdd:PRK08255 696 ISEADHVNSIIAAGRaDLCALARPHLADPAWTLHEAA 732
|
|
| PRK07395 |
PRK07395 |
L-aspartate oxidase; Provisional |
542-912 |
5.75e-26 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236010 [Multi-domain] Cd Length: 553 Bit Score: 113.60 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 542 DSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLNDITTTGGMSIDRTH-RPK---DGSAVGGYLISGLV 617
Cdd:PRK07395 62 DSPKLHYEDTLKAGAGLCDPEAVRFLVEQAPEAIASLVEMGVAFDRHGQHLALTLEAAHsRPRvlhAADTTGRAIVTTLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 618 RNVNKR-NIEVMLDTSVSD--IIFENGEVTGVRLTTEENETVIVAtKSVIVATGG----FSAnsqmvvkyrpdlegfvTT 690
Cdd:PRK07395 142 EQVLQRpNIEIISQALALSlwLEPETGRCQGISLLYQGQITWLRA-GAVILATGGggqvFAQ----------------TT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 691 NHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQK---TSYLISESIRGGGAILVNQKGERF---YN---EMSTRDKVSA 761
Cdd:PRK07395 205 NPAVSTGDGVALAWRAGAQLRDLEFFQFHPTALTKpgaPRFLISEAVRGEGAHLVDAQGRRFafdYHpagELAPRDVVSR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 762 QIIALPEKYAYIVFDEHV----RAknkAADEYIAKGFvtsassPKALA--EALGMDhhaflatleryngfVEKQhdddfg 835
Cdd:PRK07395 285 AIFSHLQKTATDPATAHVwldlRP---IPAERIRRRF------PNIIRvcQKWGID--------------VFQE------ 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504697314 836 rttalrapinegpfyAIQIAPGVHHTMGGVTINTEtcvldsNHNVLPGAFAAGEVVG-GIHGGNRIGGNAVADIIIFG 912
Cdd:PRK07395 336 ---------------PIPVAPAAHYWMGGVVTDLN------NQTSIPGLYAVGETAStGVHGANRLASNSLLECLVFA 392
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
498-920 |
1.45e-25 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 112.82 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrfQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:PRK07803 25 IEARERGLRVAVVCKSLFGKAHTVMAEGGCAAA----MGNVNPKDNWQVHFRDTMRGGKFLNNWRMAELHAKEAPDRVWE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGiMLNDITTTG----------------------GMSIDRTHRPK-------DGSAVGGYlisglvrnvnKRNIEVM 628
Cdd:PRK07803 101 LETYG-ALFDRTKDGrisqrnfgghtyprlahvgdrtGLELIRTLQQKivslqqeDHAELGDY----------EARIKVF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 629 LDTSVSDIIFENGEVTGV-RLTTEENETVIVATKSVIVATGGFSANSQmvvkyrpdlegfVTTNHKGATGGGIALLERIG 707
Cdd:PRK07803 170 AECTITELLKDGGRIAGAfGYWRESGRFVLFEAPAVVLATGGIGKSFK------------VTSNSWEYTGDGHALALRAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 708 AGTVDMGEIQIHPT-------VEqktSYLISESIRGGGAILVNQKGERF------------YNEMS------TRDKVSAQ 762
Cdd:PRK07803 238 ATLINMEFVQFHPTgmvwppsVK---GILVTEGVRGDGGVLKNSEGKRFmfdyipdvfkgqYAETEeeadrwYKDNDNNR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 763 IIA--LPEkyayivfDEHVRAKNKAADEyiAKG------FVTSAS--SPKALAEALGMDHHAF--LATLEryngfvekqh 830
Cdd:PRK07803 315 RPPelLPR-------DEVARAINSEVKA--GRGsphggvYLDIASrlPAEEIKRRLPSMYHQFkeLADVD---------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 831 dddfgrttalrapINEGPfyaIQIAPGVHHTMGGVTINTETCVLDsnhnvLPGAFAAGEVVGGIHGGNRIGGNAVADIII 910
Cdd:PRK07803 376 -------------ITKEP---MEVGPTCHYVMGGVEVDPDTGAAT-----VPGLFAAGECAGGMHGSNRLGGNSLSDLLV 434
|
490
....*....|
gi 504697314 911 FGTLAGHQAA 920
Cdd:PRK07803 435 FGRRAGLGAA 444
|
|
| 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 504697314 592 GGMSIDRTHrpkdgSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVIVATKSVIVATGGFS 671
Cdd:PRK12845 204 GGLALGRRY-----AAGGQALAAGLFAGVLRAGIPIWTETSLVRLTDDGGRVTGAVVDHRGREVTVTARRGVVLAAGGFD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 672 ANSQMVVKYR-PDLEGFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV-----EQKTSYLISESIrgGGAILVNQK 745
Cdd:PRK12845 279 HDMEMRWKFQsESLGEHASLGAEGNTGDAIRIAQDLGAAIGLMDQAWWFPAVaplpgGAPAVMLAERSL--PGSLIVDQT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 746 GERFYNEMSTRDKVSAQIIAL-----PEKYAYIVFDEHVRAKNKAADEYIAK----------GFVTSASSPKALAEALGM 810
Cdd:PRK12845 357 GRRFVNEATDYMSFGQRVLEReragdPVESMWIVFDQQYRNSYVFAAELFPRmpipqawydaGIAHRADSLADLARKIGV 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 811 DHHAFLATLERYNGFVEKQHDDDFGRTTA----------------LRaPINEGPFYAIQIAPGVHHTMGGVTINTETCVL 874
Cdd:PRK12845 437 PVDTFVATMRRFNEMAAAGVDSDFGRGRSaydryygdptvtpnpnLR-PLDKGPFYAVKMVLSDLGTCGGLRADERARVL 515
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 504697314 875 DSNHNVLPGAFAAGEVVGGIHGGNRIGGNA-VADIIIFGTLAGHQAAMR 922
Cdd:PRK12845 516 REDGSVIDGLYAIGNTAANAFGATYPGAGAtIGQGLVYGYIAAQDAAAR 564
|
|
| TMADH_HD_FMN |
cd02929 |
Trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD) FMN-binding domain. ... |
79-237 |
2.09e-23 |
|
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: 103.20 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 79 NDEKIAGLAKIAEAIKSKGSKALLQIYHGGrMVDPKLIGGRTPVGPS--AVAAPRDGAATPVALTAEEVEGMIGKFGEAV 156
Cdd:cd02929 78 DDGDIRNLAAMTDAVHKHGALAGIELWHGG-AHAPNRESRETPLGPSqlPSEFPTGGPVQAREMDKDDIKRVRRWYVDAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 157 RRAIQAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRAKFPLAVLDITHKMVrqyADDAfIIGYRFSPEELEVP 236
Cdd:cd02929 157 LRARDAGFDIVYVYAAHGYLPLQFLLPRYNKRTDEYGGSLENRARFWRETLEDTKDAV---GDDC-AVATRFSVDELIGP 232
|
.
gi 504697314 237 G 237
Cdd:cd02929 233 G 233
|
|
| PRK07512 |
PRK07512 |
L-aspartate oxidase; Provisional |
539-920 |
4.71e-23 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236036 [Multi-domain] Cd Length: 513 Bit Score: 104.22 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 539 GIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLnDITTTGGMSIDR---------THRPKDGSavG 609
Cdd:PRK07512 59 GPDDSPALHAADTLAAGAGLCDPAVAALITAEAPAAIEDLLRLGVPF-DRDADGRLALGLeaahsrrriVHVGGDGA--G 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 610 GYLISGLVRNV-NKRNIEVMLDTSVSDIIFENGEVTGVRLTTEeNETVIVATKSVIVATGGfsansqmvvkyrpdLEG-- 686
Cdd:PRK07512 136 AAIMRALIAAVrATPSITVLEGAEARRLLVDDGAVAGVLAATA-GGPVVLPARAVVLATGG--------------IGGly 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 687 FVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPT---VEQKTSYLISESIRGGGAILVNQKGERF---YN---EMSTRD 757
Cdd:PRK07512 201 AVTTNPAGAFGQGLALAARAGAVIADPEFVQFHPTaidIGRDPAPLATEALRGEGAILINEDGERFmadIHpgaELAPRD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 758 KVSAQIIAlpekyayivfdeHVRAKNKA---ADEYIAKGFVTSASSPKALAEALGMDhhaflatleryngfvekqhdddf 834
Cdd:PRK07512 281 VVARAVFA------------EIAAGRGAfldARAALGAHFATRFPTVYAACRSAGID----------------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 835 grttALRAPInegPfyaiqIAPGVHHTMGGVTINTEtcvldsNHNVLPGAFAAGEVVG-GIHGGNRIGGNAVADIIIFGT 913
Cdd:PRK07512 326 ----PARQPI---P-----VAPAAHYHMGGIAVDAD------GRSSLPGLWAAGEVAStGLHGANRLASNSLLEAVVFAA 387
|
....*..
gi 504697314 914 LAGHQAA 920
Cdd:PRK07512 388 RAAEDIA 394
|
|
| PRK07804 |
PRK07804 |
L-aspartate oxidase; Provisional |
500-923 |
3.46e-22 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236102 [Multi-domain] Cd Length: 541 Bit Score: 101.59 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 500 AHDEGASVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLA 579
Cdd:PRK07804 35 ARRAGRRVLVVTKAALDDGSTRWAQGGIAA-------VLDPGDSPEAHVADTLVAGAGLCDPDAVRSLVAEGPRAVRELV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 580 TRGIMLnDITTTGGMSIDRT--HRPK-----DGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIF-ENGEVTGVRL--- 648
Cdd:PRK07804 108 ALGARF-DESPDGRWALTREggHSRRrivhaGGDATGAEVQRALDAAVRADPLDIREHALALDLLTdGTGAVAGVTLhvl 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 649 -TTEENETVIVATKSVIVATGG----FSAnsqmvvkyrpdlegfvTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV- 722
Cdd:PRK07804 187 gEGSPDGVGAVHAPAVVLATGGlgqlYAA----------------TTNPAGSTGDGVALALRAGAAVSDLEFVQFHPTVl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 723 -------EQKTsyLISESIRGGGAILVNQKGERF------YNEMSTRDKVSAQIIAlpekyayivfdehvRAKnkaadey 789
Cdd:PRK07804 251 flgpaagGQRP--LISEAVRGEGAILVDAQGNRFmagvhpLADLAPRDVVAKAIDR--------------RMK------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 790 iakgfvtsasspkalaeALGMDHHaflatleryngFVEKQHDDDFGR-----TTALRA----PINEgpfyAIQIAPGVHH 860
Cdd:PRK07804 308 -----------------ATGDDHV-----------YLDARGIEGFARrfptiTASCRAagidPVRQ----PIPVAPAAHY 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504697314 861 TMGGVTINTEtcvldsNHNVLPGAFAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAGHQAAMRA 923
Cdd:PRK07804 356 SCGGVVTDVY------GRTSVPGLYAAGEVACtGVHGANRLASNSLLEGLVVGERAGAAAAAHA 413
|
|
| sdhA |
PRK05945 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
507-916 |
5.17e-22 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 180319 [Multi-domain] Cd Length: 575 Bit Score: 101.35 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 507 VLIVEKMPTIGGNTIKASAGMNAAetrFQRVKGiQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLN 586
Cdd:PRK05945 31 VAVVAKTHPIRSHSVAAQGGIAAS---LKNVDP-EDSWEAHAFDTVKGSDYLADQDAVAILTQEAPDVIIDLEHLGVLFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 587 DIT-------TTGGMSIDRTHRPKDGSavGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTG-VRLTTEENETVIV 658
Cdd:PRK05945 107 RLPdgriaqrAFGGHSHNRTCYAADKT--GHAILHELVNNLRRYGVTIYDEWYVMRLILEDNQAKGvVMYHIADGRLEVV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 659 ATKSVIVATGGFsansqmvvkyrpdleGFV---TTNHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIR 735
Cdd:PRK05945 185 RAKAVMFATGGY---------------GRVfntTSNDYASTGDGLAMTAIAGLPLEDMEFVQFHPTGLYPVGVLISEAVR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 736 GGGAILVNQKGERFYN-------EMSTRDkVSAQIIALpekyayivfdeHVRAknkaadeyiAKGfVTSASSPKALAEAL 808
Cdd:PRK05945 250 GEGAYLINSEGDRFMAdyapsrmELAPRD-ITSRAITL-----------EIRA---------GRG-INPDGSAGGPFVYL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 809 GMDHHAFLATLERYNGFVEKQHdddfgRTTALRApINEgpfyAIQIAPGVHHTMGGVTINTETCVLDSNHNVLPGAFAAG 888
Cdd:PRK05945 308 DLRHMGKEKIMSRVPFCWEEAH-----RLVGVDA-VTE----PMPVRPTVHYCMGGIPVNTDGRVRRSADGLVEGFFAAG 377
|
410 420
....*....|....*....|....*....
gi 504697314 889 EVVG-GIHGGNRIGGNAVADIIIFGTLAG 916
Cdd:PRK05945 378 ECACvSVHGANRLGSNSLLECVVYGRRTG 406
|
|
| COG3976 |
COG3976 |
Uncharacterized conserved protein, contains FMN-binding domain [General function prediction ... |
373-466 |
2.12e-21 |
|
Uncharacterized conserved protein, contains FMN-binding domain [General function prediction only];
Pssm-ID: 443175 Cd Length: 116 Bit Score: 90.35 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 373 SMAESKFKPGTFVEKVQDDANELVINVSLETDCIADIALASGPSEDVEFVTSFEEIRTRILDANTPHVDAITGATSQSEA 452
Cdd:COG3976 23 SSAAAKYKDGTYTGTAQGFNGDVTVEVTVSDGKITDIEVLEHGETPGIGDKAIEELPDEIVEAQSLDVDAVSGATLTSKA 102
|
90
....*....|....
gi 504697314 453 VKKAVSKAMLKSSK 466
Cdd:COG3976 103 IKEAVEDALEQAGG 116
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
636-916 |
1.91e-20 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 96.73 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 636 IIFENGEVTGVRLTTEENETV-IVATKSVIVATGGFSAnsqmvvKYrpdlegFVTTNHKGATGGGIALLERIGAGTVDMG 714
Cdd:PTZ00139 193 IMDEDGECRGVIAMSMEDGSIhRFRAHYTVIATGGYGR------AY------FSCTSAHTCTGDGGAMVSRAGLPLQDLE 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 715 EIQIHPTVEQKTSYLISESIRGGGAILVNQKGERFyneMstrdkvsaqiialpEKYAyivfdehvrakNKAADeyIAKGF 794
Cdd:PTZ00139 261 FVQFHPTGIYGAGCLITEGCRGEGGILRNSEGERF---M--------------ERYA-----------PTAKD--LASRD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 795 VTSASSPKALAEALGM----DH------HAFLATL-ERYNGFVEKQHDddFGRTTALRAPInegPfyaiqIAPGVHHTMG 863
Cdd:PTZ00139 311 VVSRAMTIEILEGRGCgpnkDHiyldltHLPPETLhERLPGISETAKI--FAGVDVTKEPI---P-----VLPTVHYNMG 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 504697314 864 GVTINTETCVLDSNHN----VLPGAFAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAG 916
Cdd:PTZ00139 381 GIPTNWKTQVLTQRNGdddkIVPGLLAAGEAAcASVHGANRLGANSLLDIVVFGRAAA 438
|
|
| PRK09077 |
PRK09077 |
L-aspartate oxidase; Provisional |
507-915 |
3.87e-19 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236374 [Multi-domain] Cd Length: 536 Bit Score: 91.90 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 507 VLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLN 586
Cdd:PRK09077 33 VAVLSKGPLSEGSTFYAQGGIAA-------VLDETDSIESHVEDTLIAGAGLCDEDAVRFIAENAREAVQWLIDQGVPFT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 587 D-----------ITTTGGMSIDRTHRPKDgsAVGGYLISGLVRNV-NKRNIEVMLDTSVSDIIFENG-EVTGVR------ 647
Cdd:PRK09077 106 TdeqangeegyhLTREGGHSHRRILHAAD--ATGKAVQTTLVERArNHPNITVLERHNAIDLITSDKlGLPGRRvvgayv 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 648 LTTEENETVIVATKSVIVATGGFSAnsqmVVKYrpdlegfvTTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV---EQ 724
Cdd:PRK09077 184 LNRNKERVETIRAKFVVLATGGASK----VYLY--------TTNPDIASGDGIAMAWRAGCRVANMEFNQFHPTClyhPQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 725 KTSYLISESIRGGGAILVNQKGERFY------NEMSTRDkvsaqIIAlpekyayivfdehvraknKAADEYIAKgfvtsa 798
Cdd:PRK09077 252 ARSFLITEALRGEGAYLKLPDGTRFMpdfderAELAPRD-----IVA------------------RAIDHEMKR------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 799 sspkalaeaLGMDhHAFLATLERYNGFVEKQHDDDFGRTTALRAPINEGPfyaIQIAPGVHHTMGGVtintetcVLDSN- 877
Cdd:PRK09077 303 ---------LGAD-CVYLDISHKPADFIRQHFPTIYERCLELGIDITKEP---IPVVPAAHYTCGGV-------MVDLHg 362
|
410 420 430
....*....|....*....|....*....|....*....
gi 504697314 878 HNVLPGAFAAGEVV-GGIHGGNRIGGNAVADIIIFGTLA 915
Cdd:PRK09077 363 RTDLDGLYAIGEVSyTGLHGANRMASNSLLECLVYGRSA 401
|
|
| PRK08401 |
PRK08401 |
L-aspartate oxidase; Provisional |
515-912 |
3.32e-18 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236259 [Multi-domain] Cd Length: 466 Bit Score: 88.71 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 515 TIGGNTIKASAGMNA-AETRFQRVKGiqDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRGIMLNDITTTGG 593
Cdd:PRK08401 28 TIIGPGIKKSNSYLAqAGIAFPILEG--DSIRAHVLDTIRAGKYINDEEVVWNVISKSSEAYDFLTSLGLEFEGNELEGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 594 MSIDRTHRPKdgSAVGGYLISGLVRNVNKRNIEvMLDTSVSDIIFENGEVTGVRLTTEenetvIVATKSVIVATGGFSAn 673
Cdd:PRK08401 106 HSFPRVFTIK--NETGKHIIKILYKHARELGVN-FIRGFAEELAIKNGKAYGVFLDGE-----LLKFDATVIATGGFSG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 674 sqmVVKYrpdlegfvTTNHKGATGGGIALLERIGAGTVDMGEIQIHPT--VEQKTSYLISESIRGGGAILVNQKGERFYN 751
Cdd:PRK08401 177 ---LFKF--------TAGSPLNLGTLIGDAVMKGAPARDLEFVQFHPTgfIGKRGTYLISEAVRGAGAKLVTGDGERFVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 752 EMSTRDKVSAQIIALPEKYAYIVFDEHVRAKNKAADEYIakgfvtsasspkalaealgmdhHAFLatleryngfveKQHD 831
Cdd:PRK08401 246 ELETRDIVARAIYRKMQEGKGVFLDATGIEDFKRRFPQI----------------------YAFL-----------RKEG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 832 DDFGRTTalrapinegpfyaIQIAPGVHHTMGGVTINTETcvldsnHNVLPGAFAAGEVV-GGIHGGNRIGGNAVADIII 910
Cdd:PRK08401 293 IDPSRDL-------------IPVTPIAHYTIGGISVDTFY------RTGIKNLYAIGEAAsNGFHGANRLASNSLLECIV 353
|
..
gi 504697314 911 FG 912
Cdd:PRK08401 354 SG 355
|
|
| sdhA |
PRK06452 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
542-916 |
1.29e-17 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 180567 [Multi-domain] Cd Length: 566 Bit Score: 87.25 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 542 DSKELFYQESLKGGG---NKNNPELLRrfvENAPEAIEWLATRGIMLND-------ITTTGGMSIDRTHRPkdGSAVGGY 611
Cdd:PRK06452 63 DNPDYMTYDTVKGGDylvDQDAAELLS---NKSGEIVMLLERWGALFNRqpdgrvaVRYFGGQTYPRTRFV--GDKTGMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 612 LISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTG-VRLTTEENETVIVATKSVIVATGGfsansqMVVKYRPdlegfvTT 690
Cdd:PRK06452 138 LLHTLFERTSGLNVDFYNEWFSLDLVTDNKKVVGiVAMQMKTLTPFFFKTKAVVLATGG------MGMLYRH------TT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 691 NHKGATGGGIALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIRGGGAILVNQKGERFYN-------EMSTRDKVS-AQ 762
Cdd:PRK06452 206 NSYINTGDGFGIALRAGAALKDPEFVQFHPTALYPSDVLISEAARGEGGILKNVKGERFMTkyapkklDLAPRDIVSrAI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 763 IIALPEKY----AYIVFD-EHVraknkaADEYIAKGFVTSASSPKALAealGMDhhaflATLEryngfvekqhdddfgrt 837
Cdd:PRK06452 286 ITEIREGRgfpgGYVGLDlTHL------GEEYIKERLALAVEAAKSFA---GVD-----AFTE----------------- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 838 talrapinegpfyAIQIAPGVHHTMGGVTINTETCVLDsnhnvLPGAFAAGEVVG-GIHGGNRIGGNAVADIIIFGTLAG 916
Cdd:PRK06452 335 -------------PIPVRPAQHYYMGGIDVDIDGRNPD-----IVGLFSAGEAACvSVHGANRLGSNSLLDTLVFGQVTG 396
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
622-924 |
6.15e-17 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 85.68 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 622 KRNIEVMLDTSVSDIIFEN-GEVTGVRLTTEENETV-IVATKSVIVATGGFSANSqmvvkyrpdlegFVTTNHKGATGGG 699
Cdd:PLN00128 199 KHNTQFFVEYFALDLIMDSdGACQGVIALNMEDGTLhRFRAHSTILATGGYGRAY------------FSATSAHTCTGDG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 700 IALLERIGAGTVDMGEIQIHPTVEQKTSYLISESIRGGGAILVNQKGERFYnemstrdkvsaqiialpEKYAyivfdehV 779
Cdd:PLN00128 267 NAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFM-----------------ERYA-------P 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 780 RAKNKAADEyiakgfVTSASSPKALAEALGM----DH-HAFLATL------ERYNGFVEkqhdddfgrTTALRAPIN--E 846
Cdd:PLN00128 323 TAKDLASRD------VVSRSMTMEIREGRGVgpekDHiYLHLNHLppevlkERLPGISE---------TAAIFAGVDvtK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 847 GPfyaIQIAPGVHHTMGGVTINTETCVL----DSNHNVLPGAFAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAGHQAAM 921
Cdd:PLN00128 388 EP---IPVLPTVHYNMGGIPTNYHGEVVtikgDDPDAVVPGLMAAGEAAcASVHGANRLGANSLLDIVVFGRACANRVAE 464
|
...
gi 504697314 922 RAK 924
Cdd:PLN00128 465 IAK 467
|
|
| PRK08626 |
PRK08626 |
fumarate reductase flavoprotein subunit; Provisional |
498-920 |
3.93e-14 |
|
fumarate reductase flavoprotein subunit; Provisional
Pssm-ID: 181507 [Multi-domain] Cd Length: 657 Bit Score: 76.55 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETrfQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:PRK08626 22 IAAAQRGLDTIVLSLVPAKRSHSAAAQGGMQASLG--NAVKGEGDNEDVHFADTVKGSDWGCDQEVARMFVHTAPKAVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGIMLNDIT------------TT----------------GGMSIDRTHRPKDGSavGGYLISGLVRNVNKRNIEVML 629
Cdd:PRK08626 100 LAAWGVPWTRVTagprtvvingekVTitekeeahglinardfGGTKKWRTCYTADGT--GHTMLYAVDNEAIKLGVPVHD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 630 DTSVSDIIFENGEVTG--VR-LTTEENETVIvaTKSVIVATGGFSAnsqmvvKYRpdlegfVTTNHKGATGGGIALLERI 706
Cdd:PRK08626 178 RKEAIALIHDGKRCYGavVRcLITGELRAYV--AKATLIATGGYGR------IYK------VTTNAVICEGIGAAIALET 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 707 GAGTV-DMGEIQIHPTVEQKTSYLISESIRGGGAILVNQKGERF---Y----NEMSTRDKVSAQIIalpekyayivfdEH 778
Cdd:PRK08626 244 GVAPLgNMEAVQFHPTAIVPSGILVTEGCRGDGGLLRDKDGYRFmpdYepekKELASRDVVSRRMT------------EH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 779 VRAknkaadeyiAKGfVTSASSPKALAEA--LGMDHhaflatleryngfVEKQHDD--DFGRTTALRAPINEgpfyAIQI 854
Cdd:PRK08626 312 IRK---------GKG-VKSPYGPHLWLDIriLGRKH-------------IETNLREvqEICENFLGIDPAKD----WIPV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504697314 855 APGVHHTMGGVTINTetcvlDSNHNVLPGAFAAGEVV-GGIHGGNRIGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK08626 365 RPTQHYSMGGIRTNP-----TGESYGLKGLFSAGEAAcWDMHGFNRLGGNSLAETVVAGMIVGKYVA 426
|
|
| PLN02815 |
PLN02815 |
L-aspartate oxidase |
503-911 |
4.36e-14 |
|
L-aspartate oxidase
Pssm-ID: 215436 [Multi-domain] Cd Length: 594 Bit Score: 76.29 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 503 EGASVLIVEKMPTIGGNTIKASAGMNAaetrfqrVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEWLATRG 582
Cdd:PLN02815 50 EYGTVAIITKDEPHESNTNYAQGGVSA-------VLDPSDSVESHMRDTIVAGAFLCDEETVRVVCTEGPERVKELIAMG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 583 IMLND-------ITTTGGMSidrTHRPKDGSAVGGYLIS-GLVRNV-NKRNIEVMLDTSVSDIIF-ENGEVT---GVR-L 648
Cdd:PLN02815 123 ASFDHgedgnlhLAREGGHS---HHRIVHAADMTGREIErALLEAVkNDPNITFFEHHFAIDLLTsQDGGSIvchGADvL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 649 TTEENETVIVATKSVIVATGGfsansqmvvkyrpdlEGFV---TTNHKGATGGGIALLERIGAGTVDMGEIQIHPTV--- 722
Cdd:PLN02815 200 DTRTGEVVRFISKVTLLASGG---------------AGHIypsTTNPLVATGDGIAMAHRAQAVVSNMEFVQFHPTAlad 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 723 ---------EQKTSYLISESIRGGGAILVNQKGERF---YN---EMSTRDKVS----AQIIALPEKYAYIvfdehvRAKN 783
Cdd:PLN02815 265 eglpikpakARENAFLITEAVRGDGGILYNLAGERFmplYDeraELAPRDVVArsidDQLKKRNEKYVLL------DISH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 784 KAADEyIAKGFvtsassPKALAEAL--GMDhhaflatleryngfvekqhdddfgrttalrapINEGPfyaIQIAPGVHHT 861
Cdd:PLN02815 339 KPREE-ILSHF------PNIAAECLkrGLD--------------------------------ITKQP---IPVVPAAHYM 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 504697314 862 MGGVTINtetcvLDSNHNVLpGAFAAGEVV-GGIHGGNRIGGNAVADIIIF 911
Cdd:PLN02815 377 CGGVRTG-----LQGETNVQ-GLYAAGEVAcTGLHGANRLASNSLLEALVF 421
|
|
| sdhA |
PRK08641 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
498-920 |
1.02e-12 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236319 [Multi-domain] Cd Length: 589 Bit Score: 71.93 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAetrfQRVKGIQDSKELFYQESLKGGGNKNNPELLRRFVENAPEAIEW 577
Cdd:PRK08641 20 IKAAEAGVHVDLFSLVPVKRSHSVCAQGGINGA----VNTKGEGDSPWIHFDDTVYGGDFLANQPPVKAMCEAAPGIIHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 578 LATRGIMLN-------DITTTGGMSIDRTHRPkdGSAVGGYLISGL---VR------NVNKR-NIEVMldtsvSDIIFEN 640
Cdd:PRK08641 96 LDRMGVMFNrtpegllDFRRFGGTLHHRTAFA--GATTGQQLLYALdeqVRryevagLVTKYeGWEFL-----GAVLDDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 641 GEVTGV---RLTTEENETVivATKSVIVATGGfsansqmvvkyrPDLEGFVTTNHKGATGGGIALLERIGAGTVDmGE-I 716
Cdd:PRK08641 169 GVCRGIvaqDLFTMEIESF--PADAVIMATGG------------PGIIFGKSTNSTINTGSAASRVYQQGAYYAN-GEfI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 717 QIHPTV---EQKTSyLISESIRG-GGAILVNQKGERFYnemstrdkvsaqiiALPEKY-AY-----------IVFDEHVR 780
Cdd:PRK08641 234 QIHPTAipgDDKLR-LMSESARGeGGRVWTYKDGKPWY--------------FLEEKYpAYgnlvprdiatrEIFDVCVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 781 AKNKAADEYIAKGFVTSASsPKALAEALGmdhhaflATLERYNGFVekqhDDDfGRTTALRapinegpfyaiqIAPGVHH 860
Cdd:PRK08641 299 QKLGINGENMVYLDLSHKD-PKELDIKLG-------GILEIYEKFT----GDD-PRKVPMK------------IFPAVHY 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 861 TMGGVTINtetcvLDSNHNVlPGAFAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAA 920
Cdd:PRK08641 354 SMGGLWVD-----YDQMTNI-PGLFAAGECDYSYHGANRLGANSLLSAIYGGMVAGPNAV 407
|
|
| sdhA |
PRK07573 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
608-904 |
2.94e-06 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 236054 [Multi-domain] Cd Length: 640 Bit Score: 50.97 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 608 VGGYliSGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGV---RLTTEENETVivATKSVIVATGGFSaNSqmvvkYrpdl 684
Cdd:PRK07573 170 LGAY--QALSRQIAAGTVKMYTRTEMLDLVVVDGRARGIvarNLVTGEIERH--TADAVVLATGGYG-NV-----F---- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 685 egFVTTNHKGATGGGIALLERIGAGTVDMGEIQIHPT-VEQKTSY-----LISESIRGGGAILVNQKGErfynemstrDK 758
Cdd:PRK07573 236 --YLSTNAMGSNATAIWRAHKKGAYFANPCFTQIHPTcIPVSGDYqskltLMSESLRNDGRIWVPKKKG---------DK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 759 VSAQIIALPEKYAYI-----VFDEHV-R-AKNKAADEYIAKGFvtsASSPKALA---------EALGMDhhaflATLERY 822
Cdd:PRK07573 305 RKPNDIPEEERDYYLerrypAFGNLVpRdVASRAAKERCDAGR---GVGPTGLGvyldfadaiKRLGKD-----VIRERY 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 823 -NGFvekqhdDDFGRTTAlrapinEGPFYA-IQIAPGVHHTMGGVTINTEtcvLDSNhnvLPGAFAAGEVVGGIHGGNRI 900
Cdd:PRK07573 377 gNLF------DMYERITG------ENPYETpMRIYPAVHYTMGGLWVDYN---LMST---IPGLFVIGEANFSDHGANRL 438
|
....
gi 504697314 901 GGNA 904
Cdd:PRK07573 439 GASA 442
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
498-683 |
3.37e-05 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 47.48 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 498 IQAHDEGASVLIVEKMP--TIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQESLKGGG-NKNNPELLRR----FVE- 569
Cdd:COG3573 22 AELADAGRRVLLLDQEPeaNLGGQAFWSFGGLFLVDSPEQRRLGIKDSPELALQDWLGSAGfDRPEDHWPRRwaeaYVEf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 570 NAPEAIEWLATRGIML---------NDITTTG-GMSIDRTHRPK-DGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIF 638
Cdd:COG3573 102 AAGEKRAWLHALGVRFfpvvgwaerGGYLAGGhGNSVPRFHITWgTGPGVVEPFIRRVRAAAAAGRVTFRFRHRVDELIV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504697314 639 ENGEVTGVRLTTEENETVIVATKS--------------VIVATGGFSANSQMVVKYRPD 683
Cdd:COG3573 182 EDGAVTGVRGEVLAPSDAERGAASsrdvvgefelraqaVIVASGGIGGNHELVRRNWPA 240
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
489-707 |
7.32e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.03 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 489 SGGAGLAAAIQAHDEGASVLIVEKMPTIGgntikasagmnaaetrfqrvkgiqdSKELfyqesLKGGG-----NKNNP-- 561
Cdd:pfam03486 8 GGAAGLMAAISAAKRGRRVLLIEKGKKLG-------------------------RKIL-----ISGGGrcnvtNLSEEpd 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 562 ELLRRFVENA-----------PEA-IEWLATRGIMLndITTTGGmsidrthR--PKDGSAvgGYLISGLVRNVNKRNIEV 627
Cdd:pfam03486 58 NFLSRYPGNPkflksalsrftPWDfIAFFESLGVPL--KEEDHG-------RlfPDSDKA--SDIVDALLNELKELGVKI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697314 628 MLDTSVSDIIFENGEVTGVRLTTEEnetviVATKSVIVATGGFSAnsqmvvkyrPDLegfvttnhkGATGGGIALLERIG 707
Cdd:pfam03486 127 RLRTRVLSVEKDDDGRFRVKTGGEE-----LEADSLVLATGGLSW---------PKT---------GSTGFGYPLAEQFG 183
|
|
| FMN_bind |
smart00900 |
This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR ... |
424-461 |
3.14e-04 |
|
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: 40.41 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 504697314 424 SFEEIRTRILDANTPH-VDAITGATSQSEAVKKAVSKAM 461
Cdd:smart00900 48 ALEKLAKEIVKKQSGGdVDAISGATITSRAVKDAVKRAL 86
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
623-694 |
6.10e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 39.61 E-value: 6.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504697314 623 RNIEVMLDTSVSDIIFENGEVTGVRLTTEENETVivATKSVIVATGGFSansqmvvkYRPDLEGFVTTNHKG 694
Cdd:pfam07992 75 NGIEVLLGTEVVSIDPGAKKVVLEELVDGDGETI--TYDRLVIATGARP--------RLPPIPGVELNVGFL 136
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
602-672 |
8.55e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.50 E-value: 8.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504697314 602 PKDGSAVGGYLISGLVRNVNKRNIEVMLDTSVSDIIFENGEVTGVRLTTEEnetviVATKSVIVATGGFSA 672
Cdd:COG0665 143 PDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERGT-----VRADAVVLAAGAWSA 208
|
|
| |
