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Conserved domains on  [gi|11024672|ref|NP_067604|]
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kynurenine 3-monooxygenase [Rattus norvegicus]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 11428987)

FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-364 4.32e-30

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: 119.66  E-value: 4.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654  19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654  93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654 167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKF-- 334
Cdd:COG0654 188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAAlr 263

                       330       340       350
                ....*....|....*....|....*....|
gi 11024672 335 NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 364
Cdd:COG0654 264 GRDDEAALARYERERRPRAARVQRAADALG 293
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-364 4.32e-30

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: 119.66  E-value: 4.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654  19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654  93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654 167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKF-- 334
Cdd:COG0654 188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAAlr 263

                       330       340       350
                ....*....|....*....|....*....|
gi 11024672 335 NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 364
Cdd:COG0654 264 GRDDEAALARYERERRPRAARVQRAADALG 293
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 24-356 1.13e-09

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: 59.91  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    24 ACFLAKRNFQVDVYEAREDIRVAN-FMRGRSInlALSYRGRQALKAVGLEDQIVskgvPMKARMIHSL----SGKKSAIP 98
Cdd:TIGR01988  15 ALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRDIhvsdGGSFGALR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    99 YgNKSQYILS-----ISREKLNKDLLTAVESYPNAKVHFGHKLS--KCCPEEGILTmLGPNKVprdITCDLIVGCDGAYS 171
Cdd:TIGR01988  89 F-DADEIGLEalgyvVENRVLQQALWERLQELPNVTLLCPARVVelPRHSDHVELT-LDDGQQ---LRARLLVGADGANS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   172 TVRAHL-MKKPRFDYSQQYI--------PHGY--MELTIPpkNGEYAM----EPNCLHIW---PRNAFMMIALPnmdksf 233
Cdd:TIGR01988 164 KVRQLAgIPTTGWDYGQSAVvanvkherPHQGtaWERFTP--TGPLALlplpDNRSSLVWtlpPEEAERLLALS------ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   234 tctlfmsFEEFeklpthsdvLDFFQKNFPdaiPLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFF 313
Cdd:TIGR01988 236 -------DEEF---------LAELQRAFG---SRLGAITLVGERHAFPLSLTHAKR----YVAPRLALIGDAAHTIHPLA 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 11024672   314 GQGMNAGFED------CLVFDELMDKFNNDLSVcLPEFSRFRIPDDHAI 356
Cdd:TIGR01988 293 GQGLNLGLRDvaalaeVLEDARRRGEDIGSLRV-LQRYERRRRFDNAAM 340
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 66-323 1.43e-09

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: 59.65  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    66 LKAVGLEDQIVSKGVPmKARMIHSLSGKKSAIPYGNKS--QYILSISREKLNKDLLTAVESYPnAKVHFGHKL-SKCCPE 142
Cdd:pfam01494  53 LRQAGLEDRILAEGVP-HEGMGLAFYNTRRRADLDFLTspPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVlSLEQDG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   143 EGILTML--GPNKVPRDITCDLIVGCDGAYSTVRAHLmkkpRFDY-SQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRN 219
Cdd:pfam01494 131 DGVTAVVrdRRDGEEYTVRAKYLVGCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   220 A----FMMIALPNMDKS---FTCTLFMSFEEFEKLPTHSDVldffqknFPDAIPLMGEQALMRDFFLLPAQPMISVKCSP 292
Cdd:pfam01494 207 PhsrgFMVGPWRSAGREryyVQVPWDEEVEERPEEFTDEEL-------KQRLRSIVGIDLALVEILWKSIWGVASRVATR 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 11024672   293 FHlKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:pfam01494 280 YR-KGRVFLAGDAAHIHPPTGGQGLNTAIQD 309
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
118-323 1.36e-08

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 56.84  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  118 LLTAVESYPNAKVHFGHKLSKCCPEEG--ILTMLGPNKVPRDITCDLIVGCDGAYSTVRaHLMKKPRFDYSQqyiPHGYM 195
Cdd:PRK06183 119 LRAGLARFPHVRVRFGHEVTALTQDDDgvTVTLTDADGQRETVRARYVVGCDGANSFVR-RTLGVPFEDLTF---PERWL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  196 ELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFtctlfmsfeEFEKLP--THSDVLDffqknfPDAIplmgeQAL 273
Cdd:PRK06183 195 VVDVLIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRW---------EFMLLPgeTEEQLAS------PENV-----WRL 254

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11024672  274 MRDFFLLPAQP-MISVKCSPFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06183 255 LAPWGPTPDDAeLIRHAVYTFHArvadrwrSGRVLLAGDAAHLMPPFAGQGMNSGIRD 312
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-364 4.32e-30

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: 119.66  E-value: 4.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654  19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654  93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654 167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKF-- 334
Cdd:COG0654 188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAAlr 263

                       330       340       350
                ....*....|....*....|....*....|
gi 11024672 335 NNDLSVCLPEFSRFRIPDDHAISDLSMYNY 364
Cdd:COG0654 264 GRDDEAALARYERERRPRAARVQRAADALG 293
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
24-216 1.69e-13

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 70.77  E-value: 1.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  24 ACFLAKRNFQVDVYEAREDIRVANfMRGrsinlALSYRGRQALKAVGLEDQIVSkgvPMKARMIHSLSGKKSAIPYGNKS 103
Cdd:COG0644   9 ARRLARAGLSVLLLEKGSFPGDKI-CGG-----GLLPRALEELEPLGLDEPLER---PVRGARFYSPGGKSVELPPGRGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672 104 QYIlsISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTMLGPNkvPRDITCDLIVGCDGAYSTVRAHLMKKPRF 183
Cdd:COG0644  80 GYV--VDRARFDRWLAEQAEEA-GAEVRTGTRVTDVLRDDGRVVVRTGD--GEEIRADYVVDADGARSLLARKLGLKRRS 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 11024672 184 DYSQQYIpHGYMELTIPPKNGEYamEPNCLHIW 216
Cdd:COG0644 155 DEPQDYA-LAIKEHWELPPLEGV--DPGAVEFF 184
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 24-356 1.13e-09

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: 59.91  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    24 ACFLAKRNFQVDVYEAREDIRVAN-FMRGRSInlALSYRGRQALKAVGLEDQIVskgvPMKARMIHSL----SGKKSAIP 98
Cdd:TIGR01988  15 ALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRDIhvsdGGSFGALR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    99 YgNKSQYILS-----ISREKLNKDLLTAVESYPNAKVHFGHKLS--KCCPEEGILTmLGPNKVprdITCDLIVGCDGAYS 171
Cdd:TIGR01988  89 F-DADEIGLEalgyvVENRVLQQALWERLQELPNVTLLCPARVVelPRHSDHVELT-LDDGQQ---LRARLLVGADGANS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   172 TVRAHL-MKKPRFDYSQQYI--------PHGY--MELTIPpkNGEYAM----EPNCLHIW---PRNAFMMIALPnmdksf 233
Cdd:TIGR01988 164 KVRQLAgIPTTGWDYGQSAVvanvkherPHQGtaWERFTP--TGPLALlplpDNRSSLVWtlpPEEAERLLALS------ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   234 tctlfmsFEEFeklpthsdvLDFFQKNFPdaiPLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFF 313
Cdd:TIGR01988 236 -------DEEF---------LAELQRAFG---SRLGAITLVGERHAFPLSLTHAKR----YVAPRLALIGDAAHTIHPLA 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 11024672   314 GQGMNAGFED------CLVFDELMDKFNNDLSVcLPEFSRFRIPDDHAI 356
Cdd:TIGR01988 293 GQGLNLGLRDvaalaeVLEDARRRGEDIGSLRV-LQRYERRRRFDNAAM 340
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 66-323 1.43e-09

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: 59.65  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672    66 LKAVGLEDQIVSKGVPmKARMIHSLSGKKSAIPYGNKS--QYILSISREKLNKDLLTAVESYPnAKVHFGHKL-SKCCPE 142
Cdd:pfam01494  53 LRQAGLEDRILAEGVP-HEGMGLAFYNTRRRADLDFLTspPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVlSLEQDG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   143 EGILTML--GPNKVPRDITCDLIVGCDGAYSTVRAHLmkkpRFDY-SQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRN 219
Cdd:pfam01494 131 DGVTAVVrdRRDGEEYTVRAKYLVGCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   220 A----FMMIALPNMDKS---FTCTLFMSFEEFEKLPTHSDVldffqknFPDAIPLMGEQALMRDFFLLPAQPMISVKCSP 292
Cdd:pfam01494 207 PhsrgFMVGPWRSAGREryyVQVPWDEEVEERPEEFTDEEL-------KQRLRSIVGIDLALVEILWKSIWGVASRVATR 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 11024672   293 FHlKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:pfam01494 280 YR-KGRVFLAGDAAHIHPPTGGQGLNTAIQD 309
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
118-323 1.36e-08

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 56.84  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  118 LLTAVESYPNAKVHFGHKLSKCCPEEG--ILTMLGPNKVPRDITCDLIVGCDGAYSTVRaHLMKKPRFDYSQqyiPHGYM 195
Cdd:PRK06183 119 LRAGLARFPHVRVRFGHEVTALTQDDDgvTVTLTDADGQRETVRARYVVGCDGANSFVR-RTLGVPFEDLTF---PERWL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  196 ELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFtctlfmsfeEFEKLP--THSDVLDffqknfPDAIplmgeQAL 273
Cdd:PRK06183 195 VVDVLIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRW---------EFMLLPgeTEEQLAS------PENV-----WRL 254

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11024672  274 MRDFFLLPAQP-MISVKCSPFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06183 255 LAPWGPTPDDAeLIRHAVYTFHArvadrwrSGRVLLAGDAAHLMPPFAGQGMNSGIRD 312
PRK06753 PRK06753
hypothetical protein; Provisional
 24-351 3.00e-08

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 55.47  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   24 ACFLAKRNFQVDVYEAREDIRVAnfmrGRSINLALSyrGRQALKAVGLEDQIVSKGVPMKARMIHSLSGK---KSAIPYG 100
Cdd:PRK06753  16 AALLQEQGHEVKVFEKNESVKEV----GAGIGIGDN--VIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTllnKVKLKSN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  101 NKSqyiLSISReklnKDLLTAVESY-PNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDItcDLIVGCDGAYSTVRAHLMK 179
Cdd:PRK06753  90 TLN---VTLHR----QTLIDIIKSYvKEDAIFTGKEVTKIENETDKVTIHFADGESEAF--DLCIGADGIHSKVRQSVNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  180 KPRFDYSqqyiphGY-----MELTIPPKNGEYAMEpnclhIW-PRNAFMMIALPNMDKSFtctlFMSFEEFEKLPTHSDV 253
Cdd:PRK06753 161 DSKVRYQ------GYtcfrgLIDDIDLKLPDCAKE-----YWgTKGRFGIVPLLNNQAYW----FITINAKERDPKYSSF 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  254 ----LDFFQKNFPDAIPLMGEQA-----LMRDFFLLpaQPMISvkcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDC 324
Cdd:PRK06753 226 gkphLQAYFNHYPNEVREILDKQsetgiLHHDIYDL--KPLKS------FVYGRIVLLGDAAHATTPNMGQGAGQAMEDA 297

                        330       340
                 ....*....|....*....|....*...
gi 11024672  325 LVfdeLMDKFNN-DLSVCLPEFSRFRIP 351
Cdd:PRK06753 298 IV---LANCLNAyDFEKALQRYDKIRVK 322
PRK07364 PRK07364
FAD-dependent hydroxylase;
118-323 4.41e-08

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 55.03  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  118 LLTAVESYPNakvhfghkLSKCCPEEGILTMLGPNKV---------PRDITCDLIVGCDGAYSTVRAHLMKKPR-FDYSQ 187
Cdd:PRK07364 127 LQEFLQSCPN--------ITWLCPAEVVSVEYQQDAAtvtleiegkQQTLQSKLVVAADGARSPIRQAAGIKTKgWKYWQ 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  188 QYI--------PHGYMeltippkngeyAMEpnclHIWPRNAFMMIALPNMDKSFTCTlfMSFEEFEKLPT--HSDVLDFF 257
Cdd:PRK07364 199 SCVtatvkheaPHNDI-----------AYE----RFWPSGPFAILPLPGNRCQIVWT--APHAQAKALLAlpEAEFLAEL 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11024672  258 QKNFPDaipLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07364 262 QQRYGD---QLGKLELLGDRFLFPVQLMQSDR----YVQHRLALVGDAAHCCHPVGGQGLNLGIRD 320
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 156-323 1.88e-07

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: 53.22  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   156 RDITCDLIVGCDGAYSTVR-AHLMKKPRFDYSQQYIPhGYMELTIPPKN----------GEYAMEP----NCLHIW---P 217
Cdd:TIGR01989 168 QVLYTKLLIGADGSNSNVRkAANIDTTGWNYNQHAVV-ATLKLEEATENdvawqrflptGPIALLPlpdnNSTLVWstsP 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   218 RNAFMMIALPnmDKSFTCTLFMSFE-EFEKLPtHSDVLDFFQKNFPDAIPLMGEQAlMRDFFLLPAqpMISVKCS----- 291
Cdd:TIGR01989 247 EEALRLLSLP--PEDFVDALNAAFDlGYSDHP-YSYLLDYAMEKLNEDIGFRTEGS-KSCFQVPPR--VIGVVDKsraaf 320

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 11024672   292 PFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:TIGR01989 321 PLGLghadeyvTKRVALVGDAAHRVHPLAGQGVNLGFGD 359
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 296-353 2.68e-07

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 52.47  E-value: 2.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 11024672  296 KSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKfNNDLSVCLPE-FSRFRIPDD 353
Cdd:PRK08849 278 KNNCVLLGDAAHTINPLAGQGVNLGFKDVDVLLAETEK-QGVLNDASFArYERRRRPDN 335
PRK06847 PRK06847
hypothetical protein; Provisional
 27-351 2.91e-07

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 52.57  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   27 LAKRNFQVDVYEAREDIRVAnfmrGRSINL---ALsyrgrQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSA------- 96
Cdd:PRK06847  23 LRRAGIAVDLVEIDPEWRVY----GAGITLqgnAL-----RALRELGVLDECLEAGFGFDGVDLFDPDGTLLAelptprl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   97 ----IPYGNksqyilSISREKLNKDLLTAVESyPNAKVHFGHKLSKCCP-EEGIltmlgpnkvprDITC--------DLI 163
Cdd:PRK06847  94 agddLPGGG------GIMRPALARILADAARA-AGADVRLGTTVTAIEQdDDGV-----------TVTFsdgttgryDLV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  164 VGCDGAYSTVRAHLM---KKPRF----------------DYSQQYIP-------------HGYMELTIPPKNGEYaMEPn 211
Cdd:PRK06847 156 VGADGLYSKVRSLVFpdePEPEYtgqgvwravlprpaevDRSLMYLGpttkagvvplsedLMYLFVTEPRPDNPR-IEP- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  212 clHIWPRnafmmiALPNMDKSFTctlfmsfeefeklpthSDVLDFFQKNFPDAiplmgEQALMRDF--FLLPAqpmisvk 289
Cdd:PRK06847 234 --DTLAA------LLRELLAPFG----------------GPVLQELREQITDD-----AQVVYRPLetLLVPA------- 277

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11024672  290 csPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKfNNDLSVCLPEFSRFRIP 351
Cdd:PRK06847 278 --PWH-RGRVVLIGDAAHATTPHLAQGAGMAIEDAIVLAEELAR-HDSLEAALQAYYARRWE 335
PRK06126 PRK06126
hypothetical protein; Provisional
 118-323 1.08e-06

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 51.15  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  118 LLTAVESYPNAKVHFGHKLSKCCP-EEGILTM---LGPNKvPRDITCDLIVGCDGAYSTVRAHL---------------- 177
Cdd:PRK06126 132 LLEHAAAQPGVTLRYGHRLTDFEQdADGVTATvedLDGGE-SLTIRADYLVGCDGARSAVRRSLgisyegtsglqrdlsi 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  178 -MKKPRFdysQQYIPH--GYMELTI-PPKNGEYAmepnclHIWPRNAFMMIALPnmdksftctlfmsFEEFEKLPTHSDV 253
Cdd:PRK06126 211 yIRAPGL---AALVGHdpAWMYWLFnPDRRGVLV------AIDGRDEWLFHQLR-------------GGEDEFTIDDVDA 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11024672  254 LDFFQKnfpdaipLMGEQAlmrDFFLLPAQPMISVK-CSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06126 269 RAFVRR-------GVGEDI---DYEVLSVVPWTGRRlVADSYRRGRVFLAGDAAHLFTPTGGYGMNTGIGD 329
PRK07538 PRK07538
hypothetical protein; Provisional
 24-177 2.72e-06

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 49.51  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   24 ACFLAKRNFQVDVYEAREDIRVAnfmrGRSINLaLSYRGRQaLKAVGLEDQIVSKGVPMKARMIHSLSGKKsaI---PYG 100
Cdd:PRK07538  16 ALTLHQRGIEVVVFEAAPELRPL----GVGINL-LPHAVRE-LAELGLLDALDAIGIRTRELAYFNRHGQR--IwsePRG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  101 NKSQYI---LSISREKLNKDLLTAV-ESYPNAKVHFGHKLSKCCP-EEGILTMLGPN--KVPRDITCDLIVGCDGAYSTV 173
Cdd:PRK07538  88 LAAGYDwpqYSIHRGELQMLLLDAVrERLGPDAVRTGHRVVGFEQdADVTVVFLGDRagGDLVSVRGDVLIGADGIHSAV 167


                 ....
gi 11024672  174 RAHL 177
Cdd:PRK07538 168 RAQL 171
PRK07045 PRK07045
putative monooxygenase; Reviewed
 50-356 4.14e-06

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 48.75  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672   50 RGRSINLA--LSYRGRQALKAVGLEDQIVSKGVPMKARMihSLSGKKSAIPYGNKSQ-----YILSISREKLNKDLLTAV 122
Cdd:PRK07045  39 RNRAQNGAdlLKPSGIGVVRAMGLLDDVFAAGGLRRDAM--RLYHDKELIASLDYRSasalgYFILIPCEQLRRLLLAKL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  123 ESYPNAKVHFGHKLSKCCPEE-GILTML----GPNKVPRditcdLIVGCDGAYSTVRAHLMKKP--RFDYSQqyiPHGYM 195
Cdd:PRK07045 117 DGLPNVRLRFETSIERIERDAdGTVTSVtlsdGERVAPT-----VLVGADGARSMIRDDVLRMPaeRVPYAT---PMAFG 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  196 ELTIPPKngeyAMEPNCLHIwPRNAFMMIALPNMDKSftCTLFMSFEEFEKLPTHSDVL---------DFFQKNFPDAIP 266
Cdd:PRK07045 189 TIALTDS----VRECNRLYV-DSNQGLAYFYPIGDQA--TRLVVSFPADEMQGYLADTTrtkllarlnEFVGDESADAMA 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  267 LMGEQALmrdfflLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNND---LSVCLP 343
Cdd:PRK07045 262 AIGAGTA------FPLIPLGRMNLDRYH-KRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGqiaLADALE 334

                        330
                 ....*....|...
gi 11024672  344 EFSRFRIPDDHAI 356
Cdd:PRK07045 335 RFERIRRPVNEAV 347
PRK06185 PRK06185
FAD-dependent oxidoreductase;
118-318 1.28e-05

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 47.55  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  118 LLTAVESYPNAKVHFGHKLSKCCPEEGI---LTMLGPNKvPRDITCDLIVGCDGAYSTVR--AHLmkKPR-----FDYSq 187
Cdd:PRK06185 114 LAEEASAYPNFTLRMGAEVTGLIEEGGRvtgVRARTPDG-PGEIRADLVVGADGRHSRVRalAGL--EVRefgapMDVL- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  188 qyiphgYMELTIPPKNGEYAMEpnclHIWPRNafMMIALPNMDKsFTCTLFMSFEEFEKLptHSDVLDFFQKNFPDAIPL 267
Cdd:PRK06185 190 ------WFRLPREPDDPESLMG----RFGPGQ--GLIMIDRGDY-WQCGYVIPKGGYAAL--RAAGLEAFRERVAELAPE 254

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 11024672  268 MGEQAL----MRDFFLLpaqpmiSVKCSpfHLK--SR--CVLMGDAAHAIVPFFGQGMN 318
Cdd:PRK06185 255 LADRVAelksWDDVKLL------DVRVD--RLRrwHRpgLLCIGDAAHAMSPVGGVGIN 305
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 156-323 4.07e-05

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 45.92  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  156 RDITCDLIVGCDGAYSTVRaHLMKKP--RFDYSQQYI--------PHGYMELTIPPKNGEYAM----EPN-CLHIWPRNA 220
Cdd:PRK08850 153 QALTAKLVVGADGANSWLR-RQMDIPltHWDYGHSALvanvrtvdPHNSVARQIFTPQGPLAFlpmsEPNmSSIVWSTEP 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11024672  221 FMMIALPNMDKS-FTCTLFMSFEEfeKLPTHSDVLDFFqknfpdAIPLMGEQAlmRDFfllpaqpmisvkcspfhLKSRC 299
Cdd:PRK08850 232 LRAEALLAMSDEqFNKALTAEFDN--RLGLCEVVGERQ------AFPLKMRYA--RDF-----------------VRERV 284

                        170       180
                 ....*....|....*....|....
gi 11024672  300 VLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK08850 285 ALVGDAAHTIHPLAGQGVNLGLLD 308
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
296-323 4.62e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 45.72  E-value: 4.62e-05
                         10        20
                 ....*....|....*....|....*...
gi 11024672  296 KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07608 279 APRVALVGDAAHLIHPLAGQGMNLGLRD 306
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 301-356 2.07e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 43.66  E-value: 2.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11024672  301 LMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNN------DLSVcLPEFSRFRIPDDHAI 356
Cdd:PRK05714 289 LIGDAAHTIHPLAGQGVNLGFLDAAVLAEVLLHAAErgerlaDVRV-LSRFERRRMPHNLAL 349
PRK08013 PRK08013
oxidoreductase; Provisional
 298-323 2.07e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 43.50  E-value: 2.07e-04
                         10        20
                 ....*....|....*....|....*.
gi 11024672  298 RCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK08013 283 RLALVGDAAHTIHPLAGQGVNLGFMD 308
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
296-323 6.57e-04

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 41.89  E-value: 6.57e-04
                         10        20
                 ....*....|....*....|....*...
gi 11024672  296 KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07333 279 APRFALVGDAAHGIHPIAGQGLNLGLKD 306
PRK06475 PRK06475
FAD-binding protein;
284-351 1.19e-03

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 40.96  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11024672  284 PMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDkfNNDLSVCLPEFSRFRIP 351
Cdd:PRK06475 279 PLFEMADAQFVGPDRTIFLGDASHAVTPFAAQGAAMAIEDAAALAEALD--SDDQSAGLKRFDSVRKE 344
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 300-332 2.00e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 40.35  E-value: 2.00e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 11024672  300 VLMGDAAHAIVPFFGQGMNAGFEDClvfDELMD 332
Cdd:PRK08020 284 ALVGDAAHTINPLAGQGVNLGYRDV---DALLD 313
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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