ID G5EJQ6_PHACH Unreviewed; 504 AA.
AC G5EJQ6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:BAL05118.1};
GN Name=PcCYP_24g {ECO:0000313|EMBL:BAL05118.1};
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231 {ECO:0000313|EMBL:BAL05118.1};
RN [1] {ECO:0000313|EMBL:BAL05118.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 34541 {ECO:0000313|EMBL:BAL05118.1};
RA Hirosue S., Hiratsuka N., Ichinose H., Wariishi H.;
RT "Phanerochaete chrysosporium cytochrome P450.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; AB597831; BAL05118.1; -; mRNA.
DR AlphaFoldDB; G5EJQ6; -.
DR VEuPathDB; FungiDB:AGR57_1148; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd11065; CYP64-like; 1.
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:SF7; P450, PUTATIVE (EUROFUNG)-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 2: Evidence at transcript level;
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 Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003476193"
SQ SEQUENCE 504 AA; 56907 MW; 98129A313FCB53D9 CRC64;
MLTALSCVFA GVLAVWAVSS WTRPRHYYPP GPKGLPLLGN MFDIPMRYGW ETFANWSRLY
GSEIVHVQAL GKHICVINSA KVAKDLFDGR PHIYSDKEQS VMTQELSGWK RAWALSPYDD
EWREYRKLFH QHFRPSAVPQ YHHKQTKAVR RLLQLLLDTP ENFLAHLRYA AGSSLLDVVY
SFDALPGDSR ITLVEKAVHT FARLLETGVY LVDVAPILKH IPAWFPGANF KRQAAEYKQL
VDDMFKVPYQ QFKDAWRRGT AQPCFAASLL ADSDPYDASE HEELFINLTG TTYAAGSDTT
VAAMGTFMLA MALHPEVQRW VQEELDRVVG RERLPEMADQ PALPRVMATV HEVLRWHPPL
PLATPHRAMA DDVYAGFTIP AGSIVLGNSW AILHDDKTYT NPQTFDPRRF VGPNAQPFPE
VVFGHGRREC PGRHFALDIL FLAVAHVLSV FTIERVDNSD RVIGDTQGLF TPHVLSYPKP
FEASFVPRFS GVESLVRTAA LSEI
//
