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Database: UniProt
Entry: K5WMD1_PHACS
LinkDB: K5WMD1_PHACS
Original site: K5WMD1_PHACS 
ID   K5WMD1_PHACS            Unreviewed;       496 AA.
AC   K5WMD1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHACADRAFT_152212 {ECO:0000313|EMBL:EKM51452.1};
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:EKM51452.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM51452.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51452.1,
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         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; JH930477; EKM51452.1; -; Genomic_DNA.
DR   RefSeq; XP_007400592.1; XM_007400530.1.
DR   AlphaFoldDB; K5WMD1; -.
DR   STRING; 650164.K5WMD1; -.
DR   GeneID; 18908899; -.
DR   KEGG; pco:PHACADRAFT_152212; -.
DR   HOGENOM; CLU_001570_5_1_1; -.
DR   InParanoid; K5WMD1; -.
DR   OrthoDB; 1611592at2759; -.
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; 2.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
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; PR00465; EP450IV.
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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         443
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   496 AA;  56467 MW;  5C767B3A325A11A2 CRC64;
     MSGTIVNLGL DLREWLSPAR VVLCASALLI ARVVLFVYAY IKARRQFPGP PVTNIWKGNL
     DETMTEDVHD KWRRWHRQYG PIYQTVRWNG LFSRVIYVGD PRLIRKIANE NWPKFPAQYA
     GFRPLSGSAL FAQMDQARWK TQRRGLAPAF QPRTVHAQYP ALHKYLLQFA DTIDRSAAAR
     GRAVDLAQLH VLLTLDFVGE VAFGAELRAV RDGAACRILQ IFHAVLPELM KCGLFPLRAK
     VPVFESTRAM HRAIAELRGM ARAAVEDARR AHEDSQEKDC GAEKGKKIFE ILAHHVPRRR
     RRSHGTHDDF CRGHRQLRNP AIHRKLRDEL DALLPADCVV PSIEQVSRLP YLRLVIKETL
     RYNGPGFGTF RYTPADVEIE GVVLPANTTL ALWNPQVHRC PNVWGADADT FRPERWMSTQ
     GEGNEKAALP GSYFPFSYGP RKCMGEGLAM LEMSLTLATL FKRYDLELEP GFEMDFQPSF
     TLCSRNGLPV YARLRK
//
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