ID K5UJK1_PHACS Unreviewed; 475 AA.
AC K5UJK1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_265393 {ECO:0000313|EMBL:EKM49741.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM49741.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM49741.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM49741.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; JH930480; EKM49741.1; -; Genomic_DNA.
DR RefSeq; XP_007401795.1; XM_007401733.1.
DR AlphaFoldDB; K5UJK1; -.
DR GeneID; 18919081; -.
DR KEGG; pco:PHACADRAFT_265393; -.
DR HOGENOM; CLU_001570_2_1_1; -.
DR InParanoid; K5UJK1; -.
DR OrthoDB; 5197776at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46300:SF2; CYTOCHROME P450 MONOOXYGENASE ALNH-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 475 AA; 52493 MW; 15C90B50DFC8CEB4 CRC64;
MVLGKSLPSG PAGLPILGSL LSLDRRPELT LQEWAQKFGP LYSVWLGEQL HIVVSDPQIA
KDLLVAQGNT FSSRKDTFVK SGIVFAGRGI SAVPTGENWT KNHRLISPYF SIEALKGYLP
GLEIEAVDML RDLYIRSEGG KIPVNPLPHV TRTSLNNMLT IIFGLRTDSI DHPLVGYWLK
LAQEFTTVTG PISNPVDFVP FLRRFPTLSG VNRAKQLHQS LVNIGGALVD DIDRRIKAGE
DVPDCLARHL LKLKEEENLD SQDIVLLCCE LMIASVEKTA AVMSGFVAQI GEYADVQARA
QAELDRVVGR DRLPGLELEK DLPYIGAIVK ETERLNNPRP LAIPHTSTQD VTYRGHFIPK
DTVIVLNTHA LTHDAARYAN PDKLEPERHL KDQPTNVEPG YSVFGYGPRA CPGKTLAQQE
IFLVVACLLW AFDVQKYQGA IIEAHDELST GSFAPVRVKL SPRHNRVSAV LGYRA
//
