|
Name |
Accession |
Description |
Interval |
E-value |
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
1-544 |
0e+00 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 708.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 1 MAIQHPDiqpavNHCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHT 80
Cdd:PRK06183 1 MAAQHPD-----AHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAVGIDDEALRVLQAIGLADEVLPHT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 81 TPWHAMRFLTPKGRCFADIQ-PMTDEFGWPRRNAFIQPQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAE 159
Cdd:PRK06183 76 TPNHGMRFLDAKGRCLAEIArPSTGEFGWPRRNAFHQPLLEAVLRAGLARFPHVRVRFGHEVTALTQDDDGVTVTLTDAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 160 GQRETVKAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVD--IANDPLSTPHIYLCCDPVRPYVSAALPHAVRRFEFM 237
Cdd:PRK06183 156 GQRETVRARYVVGCDGANSFVRRTLGVPFEDLTFPERWLVVDvlIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRWEFM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 238 VMPGETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFN 317
Cdd:PRK06183 236 LLPGETEEQLASPENVWRLLAPWGPTPDDAELIRHAVYTFHARVADRWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 318 LAWKLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVswllnylppvkryflemrfkpmp 397
Cdd:PRK06183 316 LAWKLAAVLRGRAGDALLDTYEQERRPHARAMIDLAVRLGRVICPTDRLAAALRDAV----------------------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 398 qyyagalvregeakhSPVGKMFIQPKVTLENGDVTLLDNAIGANFAVIGWGCNPLWGMSDEQIQQWRALGTRFIQVVPDV 477
Cdd:PRK06183 373 ---------------LPVGTLFPQPRVELGGGDRGLLDDVLGPGFAVLGWGCDPLAGLSDEQRARWRALGARFVQVVPAV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608030184 478 QIHTaqdnyDGVLRVGDTQGRLRSWFAQHNASLVVMRPDRFVAAIAIPQTLGNTLNKLASVMTLNRP 544
Cdd:PRK06183 438 QAHT-----AQDDHDSDVDGALRAWLARHGASAVLLRPDRYVAAAADAQTLGALLAALAALLHLTRA 499
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
16-353 |
6.40e-89 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 277.67 E-value: 6.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLTPKGRC 95
Cdd:pfam01494 2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYNTRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 96 FADIQPmtdEFGWPRRNAFIQPQVDAVMLEGLSRFPnVRCLFSRELEAFSQQDDEVTLYLK-TAEGQRETVKAQWLVACD 174
Cdd:pfam01494 82 RADLDF---LTSPPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRdRRDGEEYTVRAKYLVGCD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 175 GGASFVRRTLNVPFEGkTAPNQWIVVDIAND--PLSTP------HIYLCCDP-----VRPYVSAALPHAVRRFEFMVMPG 241
Cdd:pfam01494 158 GGRSPVRKTLGIEFEG-FEGVPFGSLDVLFDapDLSDPverafvHYLIYAPHsrgfmVGPWRSAGRERYYVQVPWDEEVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 242 ETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWK 321
Cdd:pfam01494 237 ERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWK 316
|
330 340 350
....*....|....*....|....*....|..
gi 1608030184 322 LALVIQGKARDALLDTYQQERRDHAKAMIDLS 353
Cdd:pfam01494 317 LAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
16-386 |
2.56e-70 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 228.67 E-value: 2.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLT-PKGR 94
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVRDgSDGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 95 CFADIQpmTDEFGWPRRNAFIQPQVDAVMLEGLSRFpNVRCLFSRELEAFSQQDDEVTLYLktAEGqrETVKAQWLVACD 174
Cdd:COG0654 84 VLARFD--AAETGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTL--ADG--RTLRADLVVGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 175 GGASFVRRTLNVPFEGKTAPNQWIVVDiandplstphiylccdpVRPYVSAALPHAVRRFefmvmpgeteeqlrepqnmr 254
Cdd:COG0654 157 GARSAVRRLLGIGFTGRDYPQRALWAG-----------------VRTELRARLAAAGPRL-------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 255 kllskvlpnPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKARDAL 334
Cdd:COG0654 200 ---------GELLELSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAA 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1608030184 335 LDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVSWLLNYLPPVKR 386
Cdd:COG0654 271 LARYERERRPRAARVQRAADALGRLFHPDSPPLRLLRNAGLRLLDRLPPLKG 322
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
18-389 |
2.83e-24 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 104.59 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEK------LDKLIDyPRAIGIDDEALRTMQSVGLVDNVLP-HTTPWHAMRfLT 90
Cdd:TIGR01988 2 IVIVGGGMVGLALALALARSGLKVALIEAtplpapADPGFD-NRVSALSAASIRLLEKLGVWDKIEPaRAQPIRDIH-VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 91 PKGR----CFADIQPMTDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAegqrETVK 166
Cdd:TIGR01988 80 DGGSfgalRFDADEIGLEALGYVVENRVLQ----QALWERLQELPNVTLLCPARVVELPRHSDHVELTLDDG----QQLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 167 AQWLVACDGGASFVRRTLNVPFEGKtAPNQWIVVdiANDPLSTPHIYL---CCDPVRPYvsAALPhavrrfefmvMPG-- 241
Cdd:TIGR01988 152 ARLLVGADGANSKVRQLAGIPTTGW-DYGQSAVV--ANVKHERPHQGTaweRFTPTGPL--ALLP----------LPDnr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 242 ------ETEEQLREPQNM-----RKLLSKVLPNPDNVELI--RQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGY 308
Cdd:TIGR01988 217 sslvwtLPPEEAERLLALsdeefLAELQRAFGSRLGAITLvgERHAFPLSLTHAKRYVAPRLALIGDAAHTIHPLAGQGL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 309 NSGMRDAFNLAwklALVIQGKARD------ALLDTYQQERRDHAKAMI---DLSVTAGNVLAPPKRWqgtLRDGVSWLLN 379
Cdd:TIGR01988 297 NLGLRDVAALA---EVLEDARRRGedigslRVLQRYERRRRFDNAAMLgatDGLNRLFSNDFPPLRL---LRNLGLRLLN 370
|
410
....*....|
gi 1608030184 380 YLPPVKRYFL 389
Cdd:TIGR01988 371 NLPPLKNFIA 380
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
18-95 |
8.68e-04 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 41.54 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVV----EKLDKLIDYPRAIGID-----DEALRTMQSVGLVD---NVLPHTTPW-H 84
Cdd:cd05188 138 VLVLGAGGVGLLAAQLAKAAGARVIVTdrsdEKLELAKELGADHVIDykeedLEEELRLTGGGGADvviDAVGGPETLaQ 217
|
90
....*....|.
gi 1608030184 85 AMRFLTPKGRC 95
Cdd:cd05188 218 ALRLLRPGGRI 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
1-544 |
0e+00 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 708.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 1 MAIQHPDiqpavNHCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHT 80
Cdd:PRK06183 1 MAAQHPD-----AHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAVGIDDEALRVLQAIGLADEVLPHT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 81 TPWHAMRFLTPKGRCFADIQ-PMTDEFGWPRRNAFIQPQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAE 159
Cdd:PRK06183 76 TPNHGMRFLDAKGRCLAEIArPSTGEFGWPRRNAFHQPLLEAVLRAGLARFPHVRVRFGHEVTALTQDDDGVTVTLTDAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 160 GQRETVKAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVD--IANDPLSTPHIYLCCDPVRPYVSAALPHAVRRFEFM 237
Cdd:PRK06183 156 GQRETVRARYVVGCDGANSFVRRTLGVPFEDLTFPERWLVVDvlIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRWEFM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 238 VMPGETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFN 317
Cdd:PRK06183 236 LLPGETEEQLASPENVWRLLAPWGPTPDDAELIRHAVYTFHARVADRWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 318 LAWKLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVswllnylppvkryflemrfkpmp 397
Cdd:PRK06183 316 LAWKLAAVLRGRAGDALLDTYEQERRPHARAMIDLAVRLGRVICPTDRLAAALRDAV----------------------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 398 qyyagalvregeakhSPVGKMFIQPKVTLENGDVTLLDNAIGANFAVIGWGCNPLWGMSDEQIQQWRALGTRFIQVVPDV 477
Cdd:PRK06183 373 ---------------LPVGTLFPQPRVELGGGDRGLLDDVLGPGFAVLGWGCDPLAGLSDEQRARWRALGARFVQVVPAV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608030184 478 QIHTaqdnyDGVLRVGDTQGRLRSWFAQHNASLVVMRPDRFVAAIAIPQTLGNTLNKLASVMTLNRP 544
Cdd:PRK06183 438 QAHT-----AQDDHDSDVDGALRAWLARHGASAVLLRPDRYVAAAADAQTLGALLAALAALLHLTRA 499
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
16-353 |
6.40e-89 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 277.67 E-value: 6.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLTPKGRC 95
Cdd:pfam01494 2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYNTRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 96 FADIQPmtdEFGWPRRNAFIQPQVDAVMLEGLSRFPnVRCLFSRELEAFSQQDDEVTLYLK-TAEGQRETVKAQWLVACD 174
Cdd:pfam01494 82 RADLDF---LTSPPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVLSLEQDGDGVTAVVRdRRDGEEYTVRAKYLVGCD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 175 GGASFVRRTLNVPFEGkTAPNQWIVVDIAND--PLSTP------HIYLCCDP-----VRPYVSAALPHAVRRFEFMVMPG 241
Cdd:pfam01494 158 GGRSPVRKTLGIEFEG-FEGVPFGSLDVLFDapDLSDPverafvHYLIYAPHsrgfmVGPWRSAGRERYYVQVPWDEEVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 242 ETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWK 321
Cdd:pfam01494 237 ERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWK 316
|
330 340 350
....*....|....*....|....*....|..
gi 1608030184 322 LALVIQGKARDALLDTYQQERRDHAKAMIDLS 353
Cdd:pfam01494 317 LAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
16-386 |
2.56e-70 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 228.67 E-value: 2.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLT-PKGR 94
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVRDgSDGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 95 CFADIQpmTDEFGWPRRNAFIQPQVDAVMLEGLSRFpNVRCLFSRELEAFSQQDDEVTLYLktAEGqrETVKAQWLVACD 174
Cdd:COG0654 84 VLARFD--AAETGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTL--ADG--RTLRADLVVGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 175 GGASFVRRTLNVPFEGKTAPNQWIVVDiandplstphiylccdpVRPYVSAALPHAVRRFefmvmpgeteeqlrepqnmr 254
Cdd:COG0654 157 GARSAVRRLLGIGFTGRDYPQRALWAG-----------------VRTELRARLAAAGPRL-------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 255 kllskvlpnPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKARDAL 334
Cdd:COG0654 200 ---------GELLELSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAA 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1608030184 335 LDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVSWLLNYLPPVKR 386
Cdd:COG0654 271 LARYERERRPRAARVQRAADALGRLFHPDSPPLRLLRNAGLRLLDRLPPLKG 322
|
|
| PRK06184 |
PRK06184 |
hypothetical protein; Provisional |
13-538 |
1.37e-65 |
|
hypothetical protein; Provisional
Pssm-ID: 235728 [Multi-domain] Cd Length: 502 Bit Score: 221.78 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 13 NHCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLTPK 92
Cdd:PRK06184 1 YTTTDVLIVGAGPTGLTLAIELARRGVSFRLIEKAPEPFPGSRGKGIQPRTQEVFDDLGVLDRVVAAGGLYPPMRIYRDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 93 GRC-----FADIQPMTDEfgwPRRNAFIQPQ--VDAVMLEGLSRFpNVRCLFSRELEAFSQQDDEVTLYLKTAEGQrETV 165
Cdd:PRK06184 81 GSVaesdmFAHLEPTPDE---PYPLPLMVPQwrTERILRERLAEL-GHRVEFGCELVGFEQDADGVTARVAGPAGE-ETV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 166 KAQWLVACDGGASFVRRTLNVPFEGKT-APNQWIVVDIANDPLSTPHIYLCCDPVRPYVSAA-LPHAvRRFEFMVMPGET 243
Cdd:PRK06184 156 RARYLVGADGGRSFVRKALGIGFPGETlGIDRMLVADVSLTGLDRDAWHQWPDGDMGMIALCpLPGT-DLFQIQAPLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 244 EEQLREPQNMRKLLSKVLPNPDnvelIRQR------VYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFN 317
Cdd:PRK06184 235 GEPDLSADGLTALLAERTGRTD----IRLHsvtwasAFRMNARLADRYRVGRVFLAGDAAHVHPPAGGQGLNTSVQDAYN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 318 LAWKLALVIQGkARDALLDTYQQERRDHAKAMIDLSVtagnvlappKRWQGTLRDGVSwllnylppvkryflemRFKPMP 397
Cdd:PRK06184 311 LGWKLAAVLAG-APEALLDTYEEERRPVAAAVLGLST---------ELLDAIKRGDMR----------------RGRDVQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 398 Q----YYAGALVREGEAK--------HSPVGkmfiqPKVTLENGDVTLLDNAIGANFAVIGWGCNPLWGMSDeqiqqwra 465
Cdd:PRK06184 365 QldlgYRGSSLAVDGPERtgglragdRAPDA-----PLLGAAGQPTRLFDLFRGPHWTLLAFGAGAAAILAR-------- 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608030184 466 lgtrfiqvvPDVQIHTAQDNYDGVlRVGDTQGRLRSWFAQHNASLVVMRPDRFVAAIAIPQTLGNTLNKLASV 538
Cdd:PRK06184 432 ---------RGLRIHRVGDAAEGG-DLVDDAGHFRDAYGLTGGTLVLVRPDGYVGLIAAGDDAAALEAYLARV 494
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
17-357 |
5.92e-55 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 194.06 E-value: 5.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDdeaLRTMQ---SVGLVDNV----LPHTTP------- 82
Cdd:PRK06126 9 PVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFNPKANTTS---ARSMEhfrRLGIADEVrsagLPVDYPtdiayft 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 83 ----WHAMRFLTPKGRcfaDIQPMTDEFG--WP---RRNAFIQPQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTL 153
Cdd:PRK06126 86 rltgYELARFRLPSAR---EAITPVGGPDgsWPspeLPHRIPQKYLEPILLEHAAAQPGVTLRYGHRLTDFEQDADGVTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 154 YLK-TAEGQRETVKAQWLVACDGGASFVRRTLNVPFEGKTA--PNQWIVVDIANDPLSTPH----IYLCCDPVRPYVSAA 226
Cdd:PRK06126 163 TVEdLDGGESLTIRADYLVGCDGARSAVRRSLGISYEGTSGlqRDLSIYIRAPGLAALVGHdpawMYWLFNPDRRGVLVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 227 LpHAVRRFEFMVMPGETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQ 306
Cdd:PRK06126 243 I-DGRDEWLFHQLRGGEDEFTIDDVDARAFVRRGVGEDIDYEVLSVVPWTGRRLVADSYRRGRVFLAGDAAHLFTPTGGY 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608030184 307 GYNSGMRDAFNLAWKLALVIQGKARDALLDTYQQERR-----------DHAKAMIDLSVTAG 357
Cdd:PRK06126 322 GMNTGIGDAVNLAWKLAAVLNGWAGPALLDSYEAERRpiaarntdyarRNADALGSFPVPPE 383
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
5-521 |
9.88e-55 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 193.55 E-value: 9.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 5 HPDIQPAVNHCVqvAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWH 84
Cdd:PRK08132 15 DQDADDPARHPV--VVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLSTGSRAICFAKRSLEIFDRLGCGERMVDKGVSWN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 85 AmrfltpkGRCFA--------DIQPMTDEfgwpRRNAFI---QPQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTL 153
Cdd:PRK08132 93 V-------GKVFLrdeevyrfDLLPEPGH----RRPAFInlqQYYVEGYLVERAQALPNIDLRWKNKVTGLEQHDDGVTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 154 YLKTAEGQrETVKAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVDIAN------------DPLSTPHiylccdpvrp 221
Cdd:PRK08132 162 TVETPDGP-YTLEADWVIACDGARSPLREMLGLEFEGRTFEDRFLIADVKMkadfpterwfwfDPPFHPG---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 222 yvSAALPHA----VRRFEFMVMPGETEEQLREPQNMRKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAA 297
Cdd:PRK08132 231 --QSVLLHRqpdnVWRIDFQLGWDADPEAEKKPENVIPRVRALLGEDVPFELEWVSVYTFQCRRMDRFRHGRVLFAGDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 298 HIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQGTLRDGVSWL 377
Cdd:PRK08132 309 HQVSPFGARGANSGIQDADNLAWKLALVLRGRAPDSLLDSYASEREFAADENIRNSTRSTDFITPKSPVSRLFRDAVLRL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 378 LNYLPPVKRYFLEMRFK------------PMPQYYAGALVregeakhspVGKMFIQPKVTLENGDVTLLDnAIGANFAVI 445
Cdd:PRK08132 389 ARDHPFARRLVNSGRLSvpavyadsplntPDGDAFAGGPV---------PGAPAPDAPVRADGEPGWLLD-LLGGGFTLL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608030184 446 GWGCNPLWGMSDEQIQQwRALGTRFIQVVPDVQIHTaqdnydGVLRVGDTQGRLRSWFAQHNASLVVMRPDRFVAA 521
Cdd:PRK08132 459 LFGDDAAAAALLQALAA-AALPVRVVAVVPAGAAQA------AAGVLEDADGLAAERYDARPGTVYLIRPDQHVAA 527
|
|
| PRK06834 |
PRK06834 |
hypothetical protein; Provisional |
17-391 |
1.85e-40 |
|
hypothetical protein; Provisional
Pssm-ID: 235870 [Multi-domain] Cd Length: 488 Bit Score: 153.25 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVEK-LDKLIDYPRAIGIDDEALRTMQSVGLVDnvlphttpwhamRFLtPKGRC 95
Cdd:PRK06834 5 AVVIAGGGPTGLMLAGELALAGVDVAIVERrPNQELVGSRAGGLHARTLEVLDQRGIAD------------RFL-AQGQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 96 -----FADIQPMTDEFgwPRRN----AFIQPQVDAVMLEGLSRFPnVRCLFSRELEAFSQQDDEVTLYLktAEGQreTVK 166
Cdd:PRK06834 72 aqvtgFAATRLDISDF--PTRHnyglALWQNHIERILAEWVGELG-VPIYRGREVTGFAQDDTGVDVEL--SDGR--TLR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 167 AQWLVACDGGASFVRRTLNVPFEGKTAPNQWIV--VDIANDPLSTPHiylccdpvrpyVSAALPHAVRRFEF------MV 238
Cdd:PRK06834 145 AQYLVGCDGGRSLVRKAAGIDFPGWDPTTSYLIaeVEMTEEPEWGVH-----------RDALGIHAFGRLEDegpvrvMV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 239 mpgeTEEQLR---EP--QNMRKLLSKV------LPNPDNVelirQRvYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQG 307
Cdd:PRK06834 214 ----TEKQVGatgEPtlDDLREALIAVygtdygIHSPTWI----SR-FTDMARQAASYRDGRVLLAGDAAHVHSPVGGQG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 308 YNSGMRDAFNLAWKLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPPKRWQgTLRDGVSWLLNYLPPVKRY 387
Cdd:PRK06834 285 LNTGVQDAVNLGWKLAQVVKGTSPESLLDTYHAERHPVAARVLRNTMAQVALLRPDDRTE-ALRDIVAELLGMDEPRKRI 363
|
....
gi 1608030184 388 FLEM 391
Cdd:PRK06834 364 AAMM 367
|
|
| PRK08244 |
PRK08244 |
monooxygenase; |
16-432 |
2.10e-40 |
|
monooxygenase;
Pssm-ID: 236199 [Multi-domain] Cd Length: 493 Bit Score: 152.98 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTP---WHamrfltpk 92
Cdd:PRK08244 3 YEVIIIGGGPVGLMLASELALAGVKTCVIERLKETVPYSKALTLHPRTLEILDMRGLLERFLEKGRKlpsGH-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 93 grcFADIQPMTDEFGWPRRNAF--IQPQVDA-VMLEGLSRfpNVRCLFSRELEAFS--QQDDEVTLYLKTAEGQReTVKA 167
Cdd:PRK08244 75 ---FAGLDTRLDFSALDTSSNYtlFLPQAETeKVLEEHAR--SLGVEIFRGAEVLAvrQDGDGVEVVVRGPDGLR-TLTS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 168 QWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVDIANDPLSTPHIYLCCDPVRPYVSAALPHAVRRFeFMVMPGETEEQL 247
Cdd:PRK08244 149 SYVVGADGAGSIVRKQAGIAFPGTDATFTAMLGDVVLKDPPPSSVLSLCTREGGVMIVPLSGGIYRV-LIIDPERPQVPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 248 REP---QNMRKLLSKVLPN----PDNVELIRqrvYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAW 320
Cdd:PRK08244 228 DEPvtlEELKTSLIRICGTdfglNDPVWMSR---FGNATRQAERYRSGRIFLAGDAAHIHFPAGGQGLNVGLQDAMNLGW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 321 KLALVIQGKARDALLDTYQQERRDHAKAMIDlSVTAGNVLAPPKRWQGTLRDGVSWLLNYlPPVKRYF------LEMRFK 394
Cdd:PRK08244 305 KLAAAIKGWAPDWLLDSYHAERHPVGTALLR-NTEVQTKLFDFTRPGLALRSMLSDLLGF-PEVNRYLagqisaLDVHYE 382
|
410 420 430
....*....|....*....|....*....|....*...
gi 1608030184 395 PMPQYyagalvregeAKHSPVGKMFIQPKVTLENGDVT 432
Cdd:PRK08244 383 PDAEM----------PPHPLNGKRLPDLELTLSDGESE 410
|
|
| PRK07190 |
PRK07190 |
FAD-binding protein; |
16-353 |
1.64e-28 |
|
FAD-binding protein;
Pssm-ID: 235955 [Multi-domain] Cd Length: 487 Bit Score: 118.76 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMAnYLGQM-GIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTP------WHAMRF 88
Cdd:PRK07190 6 TDVVIIGAGPVGLMCA-YLGQLcGLNTVIVDKSDGPLEVGRADALNARTLQLLELVDLFDELYPLGKPcntssvWANGKF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 89 LTPKGRCFADIQPMTDEFGWPRRNAFIQPQVDAVMLEGLSRFPNVRCLFSRELEafsqqDDEVTLYLKTAEgqreTVKAQ 168
Cdd:PRK07190 85 ISRQSSWWEELEGCLHKHFLMLGQSYVEKLLDDKLKEAGAAVKRNTSVVNIELN-----QAGCLTTLSNGE----RIQSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 169 WLVACDGGASFVRRTLNVPFEGKTAPNQWIVVD--IANDPLSTPHIYLccdpVRPYVS--AALPHA--VRRFeFMVMpgE 242
Cdd:PRK07190 156 YVIGADGSRSFVRNHFNVPFEIIRPQIIWAVIDgvIDTDFPKVPEIIV----FQAETSdvAWIPREgeIDRF-YVRM--D 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 243 TEEQLREpQNMRKLLSKVLP---NPDNVELIRQrvYTHNARLAQRFRI-DRVLLAGDAAHIMPVWQGQGYNSGMRDAFNL 318
Cdd:PRK07190 229 TKDFTLE-QAIAKINHAMQPhrlGFKEIVWFSQ--FSVKESVAEHFFIqDRIFLAGDACHIHSVNGGQGLNTGLADAFNL 305
|
330 340 350
....*....|....*....|....*....|....*
gi 1608030184 319 AWKLALVIQGKARDALLDTYQQERRDHAKAMIDLS 353
Cdd:PRK07190 306 IWKLNMVIHHGASPELLQSYEAERKPVAQGVIETS 340
|
|
| PRK08294 |
PRK08294 |
phenol 2-monooxygenase; Provisional |
6-419 |
1.61e-26 |
|
phenol 2-monooxygenase; Provisional
Pssm-ID: 236223 [Multi-domain] Cd Length: 634 Bit Score: 113.93 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 6 PDIQPAVNHC----------VQVAIAGAGPVGLMMANYLGQM-GIDVLVVEKLDKLIDYPRAIGIddeALRTM---QSVG 71
Cdd:PRK08294 13 PRIQPAAGRGinrpadlpdeVDVLIVGCGPAGLTLAAQLSAFpDITTRIVERKPGRLELGQADGI---ACRTMemfQAFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 72 LVDNVLPHTTPWHAMRFLTPkgrcfADIQPMTdefgwPRRNAFIQPQVDavmleGLSRFPNV-----RCL---------- 136
Cdd:PRK08294 90 FAERILKEAYWINETAFWKP-----DPADPST-----IVRTGRVQDTED-----GLSEFPHVivnqaRVHdyfldvmrns 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 137 -------FSRELEAFSQQDDE---VTLYLK----TAEGQRETVKAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVDI 202
Cdd:PRK08294 155 ptrlepdYGREFVDLEVDEEGeypVTVTLRrtdgEHEGEEETVRAKYVVGCDGARSRVRKAIGRELRGDSANHAWGVMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 203 andpLST---PHIYLCCdpvrpyvsaaLPHAVRRFEFMVMPgeteeqlREPQNMRKL---LSKVLPNpDNV--------E 268
Cdd:PRK08294 235 ----LAVtdfPDIRLKC----------AIQSASEGSILLIP-------REGGYLVRLyvdLGEVPPD-ERVavrnttveE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 269 LIR--QR----------------VYTHNARLAQRF----------RIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAW 320
Cdd:PRK08294 293 VIAkaQRilhpytldvkevawwsVYEVGQRLTDRFddvpaeeagtRLPRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 321 KLALVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLA-PPKRwqgtlRDGVSwllnylPP-VKRYFLEM-RFKP-- 395
Cdd:PRK08294 373 KLAAVLSGRSPPELLHTYSAERQAIAQELIDFDREWSTMMAaPPKE-----GGGVD------PAeLQDYFVKHgRFTAgt 441
|
490 500
....*....|....*....|....*...
gi 1608030184 396 MPQYYAGALVREGE----AKHSPVGKMF 419
Cdd:PRK08294 442 ATHYAPSLLTGEAThqdlATGFPIGKRF 469
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
18-389 |
2.83e-24 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 104.59 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEK------LDKLIDyPRAIGIDDEALRTMQSVGLVDNVLP-HTTPWHAMRfLT 90
Cdd:TIGR01988 2 IVIVGGGMVGLALALALARSGLKVALIEAtplpapADPGFD-NRVSALSAASIRLLEKLGVWDKIEPaRAQPIRDIH-VS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 91 PKGR----CFADIQPMTDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAegqrETVK 166
Cdd:TIGR01988 80 DGGSfgalRFDADEIGLEALGYVVENRVLQ----QALWERLQELPNVTLLCPARVVELPRHSDHVELTLDDG----QQLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 167 AQWLVACDGGASFVRRTLNVPFEGKtAPNQWIVVdiANDPLSTPHIYL---CCDPVRPYvsAALPhavrrfefmvMPG-- 241
Cdd:TIGR01988 152 ARLLVGADGANSKVRQLAGIPTTGW-DYGQSAVV--ANVKHERPHQGTaweRFTPTGPL--ALLP----------LPDnr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 242 ------ETEEQLREPQNM-----RKLLSKVLPNPDNVELI--RQRVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGY 308
Cdd:TIGR01988 217 sslvwtLPPEEAERLLALsdeefLAELQRAFGSRLGAITLvgERHAFPLSLTHAKRYVAPRLALIGDAAHTIHPLAGQGL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 309 NSGMRDAFNLAwklALVIQGKARD------ALLDTYQQERRDHAKAMI---DLSVTAGNVLAPPKRWqgtLRDGVSWLLN 379
Cdd:TIGR01988 297 NLGLRDVAALA---EVLEDARRRGedigslRVLQRYERRRRFDNAAMLgatDGLNRLFSNDFPPLRL---LRNLGLRLLN 370
|
410
....*....|
gi 1608030184 380 YLPPVKRYFL 389
Cdd:TIGR01988 371 NLPPLKNFIA 380
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
18-343 |
4.71e-18 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 86.61 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEK--LDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRfLT----P 91
Cdd:PRK07364 21 VAIVGGGIVGLTLAAALKDSGLRIALIEAqpAEAAAAKGQAYALSLLSARIFEGIGVWEKILPQIGKFRQIR-LSdadyP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 92 KGRCFADIQPMTDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTaEGQRETVKAQWLV 171
Cdd:PRK07364 100 GVVKFQPTDLGTEALGYVGEHQVLL----EALQEFLQSCPNITWLCPAEVVSVEYQQDAATVTLEI-EGKQQTLQSKLVV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 172 ACDGGASFVRRTLNVPFEGKTAPNQWIVVDIANDpLSTPHI-YLCCDPVRPYvsAALPHAVRRFEFM-VMPGETEEQLR- 248
Cdd:PRK07364 175 AADGARSPIRQAAGIKTKGWKYWQSCVTATVKHE-APHNDIaYERFWPSGPF--AILPLPGNRCQIVwTAPHAQAKALLa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 249 --EPQNMRKLLSKVLPNPDNVELIRQRvYTHNARLAQ--RFRIDRVLLAGDAAH-IMPVwQGQGYNSGMRDAFNLAWKLA 323
Cdd:PRK07364 252 lpEAEFLAELQQRYGDQLGKLELLGDR-FLFPVQLMQsdRYVQHRLALVGDAAHcCHPV-GGQGLNLGIRDAAALAQVLQ 329
|
330 340
....*....|....*....|....
gi 1608030184 324 LVIQgKARD----ALLDTYQQERR 343
Cdd:PRK07364 330 TAHQ-RGEDigslAVLKRYERWRK 352
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
17-386 |
2.38e-14 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 74.90 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVEK-LDKLIDYpRAIGIDDEALRTMQSVGLVDNVL--PHTTPwHAMRFLTPKG 93
Cdd:PRK06185 8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEKhADFLRDF-RGDTVHPSTLELMDELGLLERFLelPHQKV-RTLRFEIGGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 94 RCF-ADiqpmtdeFGW-PRRNAFI--QPQVDavMLEGL----SRFPNVRCLFSRELEAFSQQDDEVT-LYLKTAEGQREt 164
Cdd:PRK06185 86 TVTlAD-------FSRlPTPYPYIamMPQWD--FLDFLaeeaSAYPNFTLRMGAEVTGLIEEGGRVTgVRARTPDGPGE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 165 VKAQWLVACDGGASFVRRTLNVPFEGKTAPNQ--WIVVDIANDplstphiylccDPvrpyvsAALPHAVRRFEFMVM--- 239
Cdd:PRK06185 156 IRADLVVGADGRHSRVRALAGLEVREFGAPMDvlWFRLPREPD-----------DP------ESLMGRFGPGQGLIMidr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 240 ----------PGETEEQLREP--QNMRKLLSKVLPNP----------DNVELIRQRVythnARLAQRFRiDRVLLAGDAA 297
Cdd:PRK06185 219 gdywqcgyviPKGGYAALRAAglEAFRERVAELAPELadrvaelkswDDVKLLDVRV----DRLRRWHR-PGLLCIGDAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 298 HIM-PVwQGQGYNSGMRDAFNLAWKLA-LVIQGKARDALLDTYQQERRDHAKAMIDLSVTAGNVLAPP--KRWQGTLRDG 373
Cdd:PRK06185 294 HAMsPV-GGVGINLAIQDAVAAANILAePLRRGRVSDRDLAAVQRRREFPTRVTQALQRRIQRRLLAPalAGRGPLGPPL 372
|
410
....*....|...
gi 1608030184 374 VSWLLNYLPPVKR 386
Cdd:PRK06185 373 LLRLLNRLPWLRR 385
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
18-343 |
1.35e-13 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 72.63 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVeklDKLIDYP--RAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLTPKGRC 95
Cdd:PRK07494 10 IAVIGGGPAGLAAAIALARAGASVALV---APEPPYAdlRTTALLGPSIRFLERLGLWARLAPHAAPLQSMRIVDATGRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 96 F---------ADIQpmTDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRcLFSRELEAFSQQDDEVTlyLKTAEGqrETVK 166
Cdd:PRK07494 87 IrapevrfraAEIG--EDAFGYNIPNWLLN----RALEARVAELPNIT-RFGDEAESVRPREDEVT--VTLADG--TTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 167 AQWLVACDGGASFVRRTLNVPFeGKTAPNQWIVV-----DIANDPLST----PHiylccdpvRPYVSAALPHAVRRFEFM 237
Cdd:PRK07494 156 ARLVVGADGRNSPVREAAGIGV-RTWSYPQKALVlnfthSRPHQNVSTefhtEG--------GPFTQVPLPGRRSSLVWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 238 VMPGETEEQLREP---------QNMRKLLSKVlpnpdNVELIRQrVYTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGY 308
Cdd:PRK07494 227 VRPAEAERLLALSdaalsaaieERMQSMLGKL-----TLEPGRQ-AWPLSGQVAHRFAAGRTALVGEAAHVFPPIGAQGL 300
|
330 340 350
....*....|....*....|....*....|....*
gi 1608030184 309 NSGMRDAFNLAWKLALVIQGKARDALLDTYQQERR 343
Cdd:PRK07494 301 NLGLRDVATLVEIVEDRPEDPGSAAVLAAYDRARR 335
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
14-386 |
9.77e-13 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 69.97 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 14 HCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEK--LDKLIDYP---RAIGIDDEALRTMQSVGLVDNVLPH-TTPWHAMR 87
Cdd:PRK09126 2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERqpLAALADPAfdgREIALTHASREILQRLGAWDRIPEDeISPLRDAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 88 FLT---PKGRCFADIQPMTDEFGW------PRRNAFiqpqvDAVmleglSRFPNVRCLFSRELEAFSQQDDEVTLYLktA 158
Cdd:PRK09126 82 VLNgrsPFALTFDARGRGADALGYlvpnhlIRRAAY-----EAV-----SQQDGIELLTGTRVTAVRTDDDGAQVTL--A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 159 EGQRetVKAQWLVACDGGASFVRRTLNVP-----FeGKTApnqwIVVDIANdPLSTPHI-YLCCD--------PVRPYVS 224
Cdd:PRK09126 150 NGRR--LTARLLVAADSRFSATRRQLGIGadmhdF-GRTM----LVCRMRH-ELPHHHTaWEWFGygqtlallPLNGHLS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 225 AA---LPhAVRRFEFMVMPGE--TEEQLREPQN----MRkllskvlpnpdnveLIRQR-VYTHNARLAQRFRIDRVLLAG 294
Cdd:PRK09126 222 SLvltLP-PDQIEALLALDPEafAAEVTARFKGrlgaMR--------------LVSSRhAYPLVAVYAHRFVAKRFALIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 295 DAAHIM-PVwQGQGYNSGMRDAFNLAwklALVIQGKARDA------LLDTYQQERRDHAKAMIdlsvTAGNVLA------ 361
Cdd:PRK09126 287 DAAVGMhPV-TAHGFNLGLKGQDILA---RLILAAARRGQdigaasLLERYERKHRLATRPLY----HATNAIAalytdd 358
|
410 420
....*....|....*....|....*.
gi 1608030184 362 -PPKRwqgTLRDGVSWLLNYLPPVKR 386
Cdd:PRK09126 359 rPPAR---LLRRAVLRAANRFPPLKQ 381
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
13-350 |
1.63e-11 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 66.08 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 13 NHCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKlidyPRAIGIDD----EALRTMQSVGLVDNVLPH-TTPWHAMR 87
Cdd:PRK07045 3 NNPVDVLINGSGIAGVALAHLLGARGHSVTVVERAAR----NRAQNGADllkpSGIGVVRAMGLLDDVFAAgGLRRDAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 88 FltpkgrcFADIQPMT--DEFGWPRRNAFIQ---PQVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAEGqr 162
Cdd:PRK07045 79 L-------YHDKELIAslDYRSASALGYFILipcEQLRRLLLAKLDGLPNVRLRFETSIERIERDADGTVTSVTLSDG-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 163 ETVKAQWLVACDGGASFVRR-TLNVPFEGKTAPNQWIVVDIAndplSTPHIYLCCdpvRPYVSAA------LPHAVRRFE 235
Cdd:PRK07045 150 ERVAPTVLVGADGARSMIRDdVLRMPAERVPYATPMAFGTIA----LTDSVRECN---RLYVDSNqglayfYPIGDQATR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 236 FMV-MPGETEEQLREPQNMRKLLSKV--LPNPDNVELIRQRVYTHNARLA-------QRFRIDRVLLAGDAAH-IMPVwQ 304
Cdd:PRK07045 223 LVVsFPADEMQGYLADTTRTKLLARLneFVGDESADAMAAIGAGTAFPLIplgrmnlDRYHKRNVVLLGDAAHsIHPI-T 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1608030184 305 GQGYNSGMRDAFNLAWKLALVIQGK-ARDALLDTYQQERRDHAKAMI 350
Cdd:PRK07045 302 GQGMNLAIEDAGELGACLDLHLSGQiALADALERFERIRRPVNEAVI 348
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
18-389 |
1.72e-10 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 63.07 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMG--IDVLVVEKLDKLI--DYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAM------- 86
Cdd:PRK07333 4 VVIAGGGYVGLALAVALKQAAphLPVTVVDAAPAGAwsRDPRASAIAAAARRMLEALGVWDEIAPEAQPITDMvitdsrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 87 ------RFLTPKGrcfaDIQPmtdefGWPRrnAFIQPQVDAV-MLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLktae 159
Cdd:PRK07333 84 sdpvrpVFLTFEG----EVEP-----GEPF--AHMVENRVLInALRKRAEALGIDLREATSVTDFETRDEGVTVTL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 160 GQRETVKAQWLVACDGGASFVR-----RTLNVPFeGKTApnqwIVVDIANDplsTPHI------YLccdPVRPYvsAALP 228
Cdd:PRK07333 149 SDGSVLEARLLVAADGARSKLRelagiKTVGWDY-GQSG----IVCTVEHE---RPHGgraeehFL---PAGPF--AILP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 229 HAVRR--------------------FEFmvmpgETEEQLREPQNMRKLlsKVLPNPdnvelirqRVYTHNARLAQRFRID 288
Cdd:PRK07333 216 LKGNRsslvwtertadaerlvalddLVF-----EAELEQRFGHRLGEL--KVLGKR--------RAFPLGLTLARSFVAP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 289 RVLLAGDAAH-IMPVwQGQGYNSGMRDAFnlawKLALVIQGKARDAL-------LDTYQQERRDHAKAMiDLSVTAGNVL 360
Cdd:PRK07333 281 RFALVGDAAHgIHPI-AGQGLNLGLKDVA----ALAEVVVEAARLGLdigsldvLERYQRWRRFDTVRM-GVTTDVLNRL 354
|
410 420 430
....*....|....*....|....*....|...
gi 1608030184 361 ----APPKRwqgTLRDGVSWLLNYLPPVKRYFL 389
Cdd:PRK07333 355 fsndSTLLR---SVRDIGLGLVDRLPKLKSFFI 384
|
|
| PRK08013 |
PRK08013 |
oxidoreductase; Provisional |
16-399 |
7.02e-10 |
|
oxidoreductase; Provisional
Pssm-ID: 236139 [Multi-domain] Cd Length: 400 Bit Score: 61.21 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKldkliDYPRAIGIDDE-ALRT----------MQSVGLVDNVLP-HTTPW 83
Cdd:PRK08013 4 VDVVIAGGGMVGLAVACGLQGSGLRVAVLEQ-----RVPEPLAADAPpALRVsainaaseklLTRLGVWQDILArRASCY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 84 HAMRFLTPKGrcFADIQPMTDEFGWPRRNAFIQPQV-DAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAEgqr 162
Cdd:PRK08013 79 HGMEVWDKDS--FGRIAFDDQSMGYSHLGHIIENSViHYALWQKAQQSSDITLLAPAELQQVAWGENEAFLTLKDGS--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 163 eTVKAQWLVACDGGASFVRRTLNVPFEG------------KTA-PNQWIVVDI-------ANDPLSTPHiyLCcdpvrPY 222
Cdd:PRK08013 154 -MLTARLVVGADGANSWLRNKADIPLTFwdyqhhalvatiRTEePHDAVARQVfhgdgilAFLPLSDPH--LC-----SI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 223 VSAALPHAVRRFEfmVMPGET-EEQLREPQNMRKLLskvlpnpdnVELIRQR-VYTHNARLAQRFRIDRVLLAGDAAHIM 300
Cdd:PRK08013 226 VWSLSPEEAQRMQ--QAPEEEfNRALAIAFDNRLGL---------CELESERqVFPLTGRYARQFAAHRLALVGDAAHTI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 301 PVWQGQGYNSGMRDAFNLAWKLA-LVIQGK--ARDALLDTYQQeRRDHAKAMIDLSVT------AGNvlAPPKRWqgtLR 371
Cdd:PRK08013 295 HPLAGQGVNLGFMDAAELIAELRrLHRQGKdiGQHLYLRRYER-SRKHSAALMLAGMQgfrdlfAGN--NPAKKL---LR 368
|
410 420 430
....*....|....*....|....*....|.
gi 1608030184 372 D-GVSwLLNYLPPVKRYFLE--MRFKPMPQY 399
Cdd:PRK08013 369 DiGLK-LADTLPGVKPQLIRqaMGLNDLPEW 398
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
16-350 |
5.41e-09 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 58.24 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVE------KLDKLIDYpRAIGIDDEALRTMQSVGLVDNVLP-HTTPWHAMRF 88
Cdd:PRK08850 5 VDVAIIGGGMVGLALAAALKESDLRIAVIEgqlpeeALNELPDV-RVSALSRSSEHILRNLGAWQGIEArRAAPYIAMEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 89 LTPKGrcFADIQPMTDEFGWPRRNAFIQPQV-DAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKTAEGqretVKA 167
Cdd:PRK08850 84 WEQDS--FARIEFDAESMAQPDLGHIVENRViQLALLEQVQKQDNVTLLMPARCQSIAVGESEAWLTLDNGQA----LTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 168 QWLVACDGGASFVRRTLNVPFEGKTAPNQWIVvdiANDPLSTPHIYLCCDPVRP-----YVSAALPH---------AVRR 233
Cdd:PRK08850 158 KLVVGADGANSWLRRQMDIPLTHWDYGHSALV---ANVRTVDPHNSVARQIFTPqgplaFLPMSEPNmssivwstePLRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 234 FEFMVMPGET-EEQLREPQNMRKLLSKVLPNPDNVELirqrvythNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGM 312
Cdd:PRK08850 235 EALLAMSDEQfNKALTAEFDNRLGLCEVVGERQAFPL--------KMRYARDFVRERVALVGDAAHTIHPLAGQGVNLGL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1608030184 313 RDAFNLAWK-LALVIQGK--ARDALLDTYQQERRDHAKAMI 350
Cdd:PRK08850 307 LDAASLAQEiLALWQQGRdiGLKRNLRGYERWRKAEAAKMI 347
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
18-343 |
2.37e-08 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 56.20 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDnvlphttpwhAMRfltpkGRC-F 96
Cdd:PRK08163 7 VLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGEIGAGIQLGPNAFSALDALGVGE----------AAR-----QRAvF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 97 ADIQPMTD----------EFGWPRRNAFIQP-------QVDAVMLEGLSRFPNVRCLFSRELEAFSQQDDEVTLYLKtae 159
Cdd:PRK08163 72 TDHLTMMDavdaeevvriPTGQAFRARFGNPyavihraDIHLSLLEAVLDHPLVEFRTSTHVVGIEQDGDGVTVFDQ--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 160 gQRETVKAQWLVACDGGASFVRRTLN---------------VPFEGKTAPNQWivvdiaNDPL--STPHIYLCCDPVR-- 220
Cdd:PRK08163 149 -QGNRWTGDALIGCDGVKSVVRQSLVgdaprvtghvvyravIDVDDMPEDLRI------NAPVlwAGPHCHLVHYPLRgg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 221 -PYVSAALPHAVRRFEFMVMPGETEEQLREPQNM----RKLLSK-------VLPNPDNVElirqrvythnarlaqRFRID 288
Cdd:PRK08163 222 eQYNLVVTFHSREQEEWGVKDGSKEEVLSYFEGIhprpRQMLDKptswkrwATADREPVA---------------KWSTG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1608030184 289 RVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAwkLALVIQGKARDALLDTYQQERR 343
Cdd:PRK08163 287 RVTLLGDAAHPMTQYMAQGACMALEDAVTLG--KALEGCDGDAEAAFALYESVRI 339
|
|
| PRK08773 |
PRK08773 |
UbiH/UbiF family hydroxylase; |
18-333 |
3.52e-08 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181552 [Multi-domain] Cd Length: 392 Bit Score: 55.64 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL---IDYPR----AIGIDDEALrtMQSVGLVDNVL-PHTTPWHAMRFL 89
Cdd:PRK08773 9 AVIVGGGVVGAACALALADAGLSVALVEGREPPrwqADQPDlrvyAFAADNAAL--LDRLGVWPAVRaARAQPYRRMRVW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 90 TPKG---RCFADIQPMTDEFGWPRRNAFIQPQV-DAVMLEGLSrfpnVRClfSRELEAFSQQDDEVTLYLKtaEGQRetV 165
Cdd:PRK08773 87 DAGGggeLGFDADTLGREQLGWIVENDLLVDRLwAALHAAGVQ----LHC--PARVVALEQDADRVRLRLD--DGRR--L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 166 KAQWLVACDGGASFVRRTLNVPFEGKTAPNQWIVVDIANDPLSTPHIYLCCDPVRPYvsAALPHAVRRFEFMVMPGETEE 245
Cdd:PRK08773 157 EAALAIAADGAASTLRELAGLPVSRHDYAQRGVVAFVDTEHPHQATAWQRFLPTGPL--ALLPFADGRSSIVWTLPDAEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 246 Q----LREPQNMRKLLSKVLPNPDNVELIRQRV-YTHNARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAw 320
Cdd:PRK08773 235 ErvlaLDEAAFSRELTQAFAARLGEVRVASPRTaFPLRRQLVQQYVSGRVLTLGDAAHVVHPLAGQGVNLGLRDVAALQ- 313
|
330
....*....|...
gi 1608030184 321 klALVIQGKARDA 333
Cdd:PRK08773 314 --QLVRQAHARRA 324
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
17-390 |
1.20e-07 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 54.19 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVE----KLDKLIDY-PRAIGIDDEALRTMQSVGlVDNVLPHT--TPWHAMR-F 88
Cdd:PRK07608 7 DVVVVGGGLVGASLALALAQSGLRVALLAprapPRPADDAWdSRVYAISPSSQAFLERLG-VWQALDAArlAPVYDMRvF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 89 LTPKGRC-FADIQPMTDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRcLFSRELEAFSQQDDEVTLylKTAEGQRetVKA 167
Cdd:PRK07608 86 GDAHARLhFSAYQAGVPQLAWIVESSLIE----RALWAALRFQPNLT-WFPARAQGLEVDPDAATL--TLADGQV--LRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 168 QWLVACDGGASFVR-----RTLNVPFE--------------GKTApNQWIVVD--IANDPLSTPHIYLccdpvrpyV-SA 225
Cdd:PRK07608 157 DLVVGADGAHSWVRsqagiKAERRPYRqtgvvanfkaerphRGTA-YQWFRDDgiLALLPLPDGHVSM--------VwSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 226 ALPHAVrrfEFMVMPGETE-EQLREPQNMR----KLLSKVLPNPdnveLIRQRVythnARLAQrfriDRVLLAGDAAHIM 300
Cdd:PRK07608 228 RTAHAD---ELLALSPEALaARVERASGGRlgrlECVTPAAGFP----LRLQRV----DRLVA----PRVALVGDAAHLI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 301 PVWQGQGYNSGMRDAFnlawKLALVIQGKA--RDA----LLDTYQQERRDHAKAMidLSVTAG-----NVLAPPKRWqgt 369
Cdd:PRK07608 293 HPLAGQGMNLGLRDVA----ALADVLAGREpfRDLgdlrLLRRYERARREDILAL--QVATDGlqrlfALPGPLARW--- 363
|
410 420
....*....|....*....|..
gi 1608030184 370 LRD-GVSWlLNYLPPVKRYFLE 390
Cdd:PRK07608 364 LRNaGMAL-VGALPLVKRWLVR 384
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
23-199 |
2.97e-07 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 52.28 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 23 AGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTpwhAMRFLTPKGRCFADIQPM 102
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLERPVR---GARFYSPGGKSVELPPGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 103 TDEFGWPRRNafiqpqVDAVMLEGLSRfPNVRCLFSRELEAFSQQDDEVTLYLktaeGQRETVKAQWLVACDGGASFVRR 182
Cdd:COG0644 78 GGGYVVDRAR------FDRWLAEQAEE-AGAEVRTGTRVTDVLRDDGRVVVRT----GDGEEIRADYVVDADGARSLLAR 146
|
170
....*....|....*..
gi 1608030184 183 TLNVPfEGKTAPNQWIV 199
Cdd:COG0644 147 KLGLK-RRSDEPQDYAL 162
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
10-357 |
6.00e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 51.80 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 10 PAVNHcvqVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFL 89
Cdd:PRK06847 2 AAVKK---VLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVLDECLEAGFGFDGVDLF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 90 TPKGRCFADI-QPMTDEFGWPRRNAFIQPQVDAVMLEGLsRFPNVRCLFSRELEAFSQQDDEVTLYLKTAEGQRetvkAQ 168
Cdd:PRK06847 79 DPDGTLLAELpTPRLAGDDLPGGGGIMRPALARILADAA-RAAGADVRLGTTVTAIEQDDDGVTVTFSDGTTGR----YD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 169 WLVACDGGASFVRRTL-----------------NVPF-EGKTAPNQWI-------VVdiandPLSTPHIYLCC---DPVR 220
Cdd:PRK06847 154 LVVGADGLYSKVRSLVfpdepepeytgqgvwraVLPRpAEVDRSLMYLgpttkagVV-----PLSEDLMYLFVtepRPDN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 221 PYVS-AALPHAVRRfefmVMPGETEEQLREpqnmrklLSKVLPNPDNVelirqrVYThnaRLAQRFrID------RVLLA 293
Cdd:PRK06847 229 PRIEpDTLAALLRE----LLAPFGGPVLQE-------LREQITDDAQV------VYR---PLETLL-VPapwhrgRVVLI 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608030184 294 GDAAHIMPVWQGQGYNSGMRDAFNLAWKLAlviQGKARDALLDTYQQERRDHAKAMIDLSVTAG 357
Cdd:PRK06847 288 GDAAHATTPHLAQGAGMAIEDAIVLAEELA---RHDSLEAALQAYYARRWERCRMVVEASARIG 348
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
17-399 |
9.44e-07 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 51.27 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL------IDYpraIGIDDEALRTMqsvGLVDNVLPHTTPWHAMRFLT 90
Cdd:PRK07588 2 KVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtggymVDF---WGVGYEVAKRM---GITDQLREAGYQIEHVRSVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 91 PKGRCFAD------IQPMTDEFGWPRRNAFIQPQVDAvmLEGlsrfpNVRCLFSRELEAFSQQDDEVTLYLktAEGQRET 164
Cdd:PRK07588 76 PTGRRKADlnvdsfRRMVGDDFTSLPRGDLAAAIYTA--IDG-----QVETIFDDSIATIDEHRDGVRVTF--ERGTPRD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 165 VkaQWLVACDGGASFVRRtlnvpfegktapnqwivvdIANDPLSTPHIYLCC-------DPVRP-----YVSAALP-HAV 231
Cdd:PRK07588 147 F--DLVIGADGLHSHVRR-------------------LVFGPERDFEHYLGCkvaacvvDGYRPrdertYVLYNEVgRQV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 232 RRF-----EFMVM-------PGETEEQLREPQNMRKLLS----------KVLPNP-----DNVELIRQrvythnarlaQR 284
Cdd:PRK07588 206 ARValrgdRTLFLfifraehDNPPLTPAEEKQLLRDQFGdvgwetpdilAALDDVedlyfDVVSQIRM----------DR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 285 FRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALViQGKARDAlLDTYQQERRDHAKAMIDLSVTAGNVLAPPK 364
Cdd:PRK07588 276 WSRGRVALVGDAAACPSLLGGEGSGLAITEAYVLAGELARA-GGDHRRA-FDAYEKRLRPFIAGKQAAAAKFLSVFAPKT 353
|
410 420 430
....*....|....*....|....*....|....*...
gi 1608030184 365 RWQGTLRDGVSWLLNyLPPVKRYFLEMRFK---PMPQY 399
Cdd:PRK07588 354 RFGLYVRNIAMKIMN-LPPVADFVGAGSFRddfELPEY 390
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
18-357 |
5.03e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 48.92 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGIDDEALRTMQSVGLVDNVLPHTTPWHAMRFLTPKGRCF- 96
Cdd:PRK06753 3 IAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTLLn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 97 -ADIQPMTDEFGWPRRN--AFIQPQVDAvmleglsrfpnvRCLFSRElEAFSQQDDEVTLYLKTAEGQREtvKAQWLVAC 173
Cdd:PRK06753 83 kVKLKSNTLNVTLHRQTliDIIKSYVKE------------DAIFTGK-EVTKIENETDKVTIHFADGESE--AFDLCIGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 174 DGGASFVRRTLN----------VPFEGKTAPNQWIVVDIAND-----------PLSTPHIY--LCC-----DPvrPYVSA 225
Cdd:PRK06753 148 DGIHSKVRQSVNadskvryqgyTCFRGLIDDIDLKLPDCAKEywgtkgrfgivPLLNNQAYwfITInakerDP--KYSSF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 226 ALPHAVRRFEFMvmpgeteeqlrePQNMRKLLSkvlpNPDNVELIRQRVYthNARLAQRFRIDRVLLAGDAAHIMPVWQG 305
Cdd:PRK06753 226 GKPHLQAYFNHY------------PNEVREILD----KQSETGILHHDIY--DLKPLKSFVYGRIVLLGDAAHATTPNMG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1608030184 306 QGYNSGMRDAFNLAWKLAlviQGKARDALLDtYQQERRDHAKAMIDLSVTAG 357
Cdd:PRK06753 288 QGAGQAMEDAIVLANCLN---AYDFEKALQR-YDKIRVKHTAKVIKRSRKIG 335
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
16-338 |
1.04e-04 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 44.79 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 16 VQVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKliDY----PRAiGIDDE-ALRTMQSVGLVDNV----LPHTTPWhaM 86
Cdd:PRK08243 3 TQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSR--EYvegrIRA-GVLEQgTVDLLREAGVGERMdregLVHDGIE--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 87 RFltpKGRCF-ADIQPMTDefGwprRNAFIQPQ---------------------VDAVMLEGL-SRFPNVRClfsrelea 143
Cdd:PRK08243 78 RF---DGRRHrIDLTELTG--G---RAVTVYGQtevtrdlmaarlaaggpirfeASDVALHDFdSDRPYVTY-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 144 fsqqddevtlylkTAEGQRETVKAQWLVACDG--GASfvRRTlnVP------FEgKTAPNQW--IVVDIAndPLSTPHIY 213
Cdd:PRK08243 142 -------------EKDGEEHRLDCDFIAGCDGfhGVS--RAS--IPagalrtFE-RVYPFGWlgILAEAP--PVSDELIY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 214 --------LCcdpvrpyvSAALPHaVRRFEFMVMPGETEEQ---------LREpqnmRkllskvLPNPDNVELIRQRVYT 276
Cdd:PRK08243 202 anhergfaLC--------SMRSPT-RSRYYLQCPLDDKVEDwsderfwdeLRR----R------LPPEDAERLVTGPSIE 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608030184 277 HN-ARL----AQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKaRDALLDTY 338
Cdd:PRK08243 263 KSiAPLrsfvAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG-DTALLDAY 328
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
18-343 |
1.60e-04 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 43.99 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVE-KLDKLIDYPRAIGIDDEALrTMQSVGLVDNVlphtTPWH---AMRfLTP-- 91
Cdd:PRK08849 6 IAVVGGGMVGAATALGFAKQGRSVAVIEgGEPKAFEPSQPMDIRVSAI-SQTSVDLLESL----GAWSsivAMR-VCPyk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 92 ----------KGRCFADIQPMtDEFGWPRRNAFIQpqvdAVMLEGLSRFPNVRCLFSRELE--AFSQQDDEVTLylktaE 159
Cdd:PRK08849 80 rletwehpecRTRFHSDELNL-DQLGYIVENRLIQ----LGLWQQFAQYPNLTLMCPEKLAdlEFSAEGNRVTL-----E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 160 GQREtVKAQWLVACDGGASFVRRTLNVpfeGKTApnqW------IVVDIAND------------PlSTPHIYL-CCDPVR 220
Cdd:PRK08849 150 SGAE-IEAKWVIGADGANSQVRQLAGI---GITA---WdyrqhcMLINVETEqpqqditwqqftP-SGPRSFLpLCGNQG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 221 PYVSAALPHAVRRFEFMvmpgeTEEQLREpqnmrKLLSKVLPNPDNVELIRQRVYTHNARLAQRFRIDRVLLAGDAAHIM 300
Cdd:PRK08849 222 SLVWYDSPKRIKQLSAM-----NPEQLRS-----EILRHFPAELGEIKVLQHGSFPLTRRHAQQYVKNNCVLLGDAAHTI 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1608030184 301 PVWQGQGYNSGMRDAFNLawkLALV-IQGKARDALLDTYQQERR 343
Cdd:PRK08849 292 NPLAGQGVNLGFKDVDVL---LAETeKQGVLNDASFARYERRRR 332
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
18-50 |
2.48e-04 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 43.26 E-value: 2.48e-04
10 20 30
....*....|....*....|....*....|...
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL 50
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
|
|
| PRK05732 |
PRK05732 |
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated |
289-353 |
2.52e-04 |
|
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
Pssm-ID: 235584 [Multi-domain] Cd Length: 395 Bit Score: 43.69 E-value: 2.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608030184 289 RVLLAGDAAH-IMPVwQGQGYNSGMRDAFNLAWKLALVIQGKA---RDALLDTYQQERRDHAKAMIDLS 353
Cdd:PRK05732 283 RLALVGNAAQtLHPI-AGQGFNLGLRDVMSLAETLTQALARGEdigDYAVLQRYQQRRQQDREATIGFT 350
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
10-46 |
5.61e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 42.54 E-value: 5.61e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1608030184 10 PAVNHCVQVAIAGAGPVGLMMANYLGQMGIDVLVVEK 46
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
18-68 |
7.10e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 38.34 E-value: 7.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDypraiGIDDEALRTMQ 68
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-----GFDPEIAKILQ 47
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
18-95 |
8.68e-04 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 41.54 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVV----EKLDKLIDYPRAIGID-----DEALRTMQSVGLVD---NVLPHTTPW-H 84
Cdd:cd05188 138 VLVLGAGGVGLLAAQLAKAAGARVIVTdrsdEKLELAKELGADHVIDykeedLEEELRLTGGGGADvviDAVGGPETLaQ 217
|
90
....*....|.
gi 1608030184 85 AMRFLTPKGRC 95
Cdd:cd05188 218 ALRLLRPGGRI 228
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
17-184 |
9.56e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 41.81 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVekldklidypraigiddEALRTMQSVGLVDNVLPhttpwHAMRFLTPKGrcf 96
Cdd:PRK07538 2 KVLIAGGGIGGLTLALTLHQRGIEVVVF-----------------EAAPELRPLGVGINLLP-----HAVRELAELG--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 97 adIQPMTDEFGWPRR-----NAFIQ---------------PQV------------DAVmlegLSRFPN--VRClfSRELE 142
Cdd:PRK07538 57 --LLDALDAIGIRTRelayfNRHGQriwseprglaagydwPQYsihrgelqmlllDAV----RERLGPdaVRT--GHRVV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1608030184 143 AFSQQDDEVTLYL-KTAEGQRETVKAQWLVACDGGASFVRRTL 184
Cdd:PRK07538 129 GFEQDADVTVVFLgDRAGGDLVSVRGDVLIGADGIHSAVRAQL 171
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
19-50 |
1.01e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 41.57 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|..
gi 1608030184 19 AIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL 50
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKV 32
|
|
| PRK06617 |
PRK06617 |
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated |
279-385 |
1.21e-03 |
|
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
Pssm-ID: 168629 [Multi-domain] Cd Length: 374 Bit Score: 41.45 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 279 ARLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDafnlAWKLALVIqgkARDALLDTYQQERRDHAKAMIDLSVTAGN 358
Cdd:PRK06617 264 ARIANRYFHNRIVLIADTAHTVHPLAGQGLNQGIKD----IEILSMIV---SNNGTLQEYQKLRQEDNFIMYKLTDELNN 336
|
90 100
....*....|....*....|....*..
gi 1608030184 359 VLAPPKRWQGTLRDGVSWLLNYLPPVK 385
Cdd:PRK06617 337 IFSNYSKNLRCLRQIGFKVINNFKPIK 363
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
18-46 |
2.05e-03 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 40.49 E-value: 2.05e-03
10 20
....*....|....*....|....*....
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEK 46
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG 31
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
282-389 |
2.57e-03 |
|
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
Pssm-ID: 273914 [Multi-domain] Cd Length: 437 Bit Score: 40.51 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 282 AQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLAWKLALVIQGKAR---DALLDTYQQERRDHAKAM---IDLSVT 355
Cdd:TIGR01989 327 ADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADigsISSLKPYERERYAKNVVLlglVDKLHK 406
|
90 100 110
....*....|....*....|....*....|....
gi 1608030184 356 AGNVLAPPKRWQGTLrdGVSwLLNYLPPVKRYFL 389
Cdd:TIGR01989 407 LYATDFPPVVALRTF--GLN-LTNYIGPLKNFIM 437
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
18-50 |
3.01e-03 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 40.12 E-value: 3.01e-03
10 20 30
....*....|....*....|....*....|...
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL 50
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKP 156
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
18-50 |
3.04e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 40.16 E-value: 3.04e-03
10 20 30
....*....|....*....|....*....|...
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL 50
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKA 175
|
|
| ubiF |
PRK08020 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed |
280-343 |
5.92e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
Pssm-ID: 181199 [Multi-domain] Cd Length: 391 Bit Score: 39.20 E-value: 5.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608030184 280 RLAQRFRIDRVLLAGDAAHIMPVWQGQGYNSGMRDAFNLawkLALVIQGKAR------DALLDTYQQERR 343
Cdd:PRK08020 273 RHALQYVQPGLALVGDAAHTINPLAGQGVNLGYRDVDAL---LDVLVNARSYgeawasEAVLKRYQRRRM 339
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
18-50 |
6.77e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 39.05 E-value: 6.77e-03
10 20 30
....*....|....*....|....*....|...
gi 1608030184 18 VAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKL 50
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRV 36
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
17-65 |
9.21e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.12 E-value: 9.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1608030184 17 QVAIAGAGPVGLMMANYLGQMGIDVLVVEKLDKLIDYPRAIGI--------DDEALR 65
Cdd:COG0569 97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVlvivgdatDEEVLE 153
|
|
| |
