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LOCUS WP_003113854 425 aa linear BCT 27-FEB-2025 ACCESSION WP_003113854 VERSION WP_003113854.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 425) AUTHORS Werck-Reichhart,D. and Feyereisen,R. TITLE Cytochromes P450: a success story JOURNAL Genome Biol 1 (6), REVIEWS3003 (2000) PUBMED 11178272 REFERENCE 2 (residues 1 to 425) AUTHORS Graham-Lorence,S., Amarneh,B., White,R.E., Peterson,J.A. and Simpson,E.R. TITLE A three-dimensional model of aromatase cytochrome P450 JOURNAL Protein Sci 4 (6), 1065-1080 (1995) PUBMED 7549871 REFERENCE 3 (residues 1 to 425) AUTHORS Degtyarenko,K.N. and Archakov,A.I. TITLE Molecular evolution of P450 superfamily and P450-containing monooxygenase systems JOURNAL FEBS Lett 332 (1-2), 1-8 (1993) PUBMED 8405421 REFERENCE 4 (residues 1 to 425) AUTHORS Nelson,D.R., Kamataki,T., Waxman,D.J., Guengerich,F.P., Estabrook,R.W., Feyereisen,R., Gonzalez,F.J., Coon,M.J., Gunsalus,I.C., Gotoh,O. et al. TITLE The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature JOURNAL DNA Cell Biol 12 (1), 1-51 (1993) PUBMED 7678494 REFERENCE 5 (residues 1 to 425) AUTHORS Guengerich,F.P. TITLE Reactions and significance of cytochrome P-450 enzymes JOURNAL J Biol Chem 266 (16), 10019-10022 (1991) PUBMED 2037557 REFERENCE 6 (residues 1 to 425) AUTHORS Nebert,D.W. and Gonzalez,F.J. TITLE P450 genes: structure, evolution, and regulation JOURNAL Annu Rev Biochem 56, 945-993 (1987) PUBMED 3304150 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF012296.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00067.27 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..425 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..425 /product="cytochrome P450" /GO_function="GO:0004497 - monooxygenase activity [Evidence IEA]" /GO_function="GO:0005506 - iron ion binding [Evidence IEA]" /GO_function="GO:0016705 - oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [Evidence IEA]" /GO_function="GO:0020037 - heme binding [Evidence IEA]" /calculated_mol_wt=48709 Region 49..415 /region_name="cytochrome_P450" /note="cytochrome P450 (CYP) superfamily; cl41757" /db_xref="CDD:477761" Site order(106,110,156,236..237,240..241,244..245,248,298,307, 310,333,367..369,373..377,380..381) /site_type="other" /note="heme binding site [chemical binding]" /db_xref="CDD:410651" Site order(179..180,236,239..240,244,305..307,309) /site_type="other" /note="chemical substrate binding pocket [chemical binding]" /db_xref="CDD:410651" ORIGIN 1 mqqtidcpir rrlahlpwan dgragvrhwl emqrdplawl qkmhvaqpdl avarmgpqrl 61 wclfhpqavq elmvdrrddl qrwqpalcml kqwngrsfmm regapaqarr kevrphlapp 121 pasevrrlaa ewgerveegr eydldlemaa fsvtlsghal fdvdlqpsay riakavrlls 181 rvallemstg lplghwfpsk lcprkrwalg qlreavgeva ersprpladl rdelctllma 241 shqstgvtlt wsllllaqrp ellarlrael agvnwtairs vadlrdcall ravlqeclrl 301 yppayglapr qvtadievfg qrlkrgdvtm vsswitqrdp rwfeaplefr perfleparw 361 prgayfpfgl gdracpgtam amidlaaala ywvehwdimh dgdlaprgwf slrpqrarvr 421 frrra