ID   K5W9U3_PHACS            Unreviewed;       582 AA.
AC   K5W9U3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHACADRAFT_209483 {ECO:0000313|EMBL:EKM55975.1};
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:EKM55975.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM55975.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM55975.1,
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}.
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DR   EMBL; JH930472; EKM55975.1; -; Genomic_DNA.
DR   RefSeq; XP_007396279.1; XM_007396217.1.
DR   AlphaFoldDB; K5W9U3; -.
DR   STRING; 650164.K5W9U3; -.
DR   GeneID; 18912851; -.
DR   KEGG; pco:PHACADRAFT_209483; -.
DR   HOGENOM; CLU_001570_14_10_1; -.
DR   InParanoid; K5W9U3; -.
DR   OrthoDB; 2117278at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
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:InterPro.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
SQ   SEQUENCE   582 AA;  65641 MW;  91448924A7664A5D CRC64;
     MRFGFGVEVG VGVGEQLKGF FPIILLTALW TLPSFRKVQI AASERVQRCT RARRRSSRVD
     SACAKMARYV TNLASMFIRR LHTIPQRCRL KHLVSDTPKA LSRGPMPSGT RSLTTNQWML
     AVAACALVTH WIFNRWEPTD IPTLFILLLL APAAASTLLI QHHGVTYGVA LTFFTYHASL
     LSSITVYRIS PFHPLARYPG PLLAKVTRWY LTFIAVGGRQ HVVTRRLFEQ YGDAVRIQFR
     DASVLQTMMG PKGMPKGLMW QVRSLEAASP ALIGLRDNAE HARRQRPWNR AFSTAALKNY
     EPALIKRVSQ FVRLLEEQKH VDFAHCAHLF TFDFMSDALF GGGSEVMQDD DKDGEVHLTH
     RDFTSLNTFP RSDVSQVIFR SNRGVARLMK ASSTKDLFYW LNNEDGSEEE DLPKGLVAAD
     SGLAMIAGSD TTARTLSTIV YCLLAHPETY VRLQTEVDQF YPPEGDSLDP KHHTSMPYLE
     AVIFIPEWTS VRAPTWSLHR DARNFAQPDA FLSERWLAPE DRDTTAPAGP EGVHNTRAFV
     PFSCGPWNCV GKNLAMVEMK VVLTHMLQRL RLRFEEGFDC VA
//