ID Q9P8A1_AGABI Unreviewed; 366 AA.
AC Q9P8A1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:CAB85700.1};
DE Flags: Fragment;
GN Name=cyp {ECO:0000313|EMBL:CAB85700.1};
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341 {ECO:0000313|EMBL:CAB85700.1};
RN [1] {ECO:0000313|EMBL:CAB85700.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Horst U3 {ECO:0000313|EMBL:CAB85700.1};
RA Eastwood D.C., Kingsnorth C.S., Jones H., Burton K.S.;
RT "Genes with increased transcript levels following harvest of the sporophore
RT of Agaricus bisporus have multiple physiological roles.";
RL Mycol. Res. 105:1223-1230(2001).
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|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ271707; CAB85700.1; -; mRNA.
DR AlphaFoldDB; Q9P8A1; -.
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 Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB85700.1"
FT NON_TER 366
FT /evidence="ECO:0000313|EMBL:CAB85700.1"
SQ SEQUENCE 366 AA; 41269 MW; 8EA9706A3EE3725E CRC64;
QLKSVRTFIR NVMESPDEFS EWIHFYTSSS IMEIIYGMKA KPEDPYVDNA KKAIEGFNEA
AVPGKFLVET FPVMKHIPSW FPGAGWKRQA LFWRDVNREV RVRPFNLVKD QVNEGTATRS
VCRTLIGNLP DSTAPDRIVK ENIAIDTCAV SFIGAAETSH SAARVFFMAM LMNPEVQKKG
QAELDKVLNG RLPEPNDGPN LPYISAMVKE TLRWQLVLPL AVPHVAIEAD EYNGYYIPKG
TIVFGNSWTF MHDPEVYKDP ESYMPERFLK DGKLDSSIRD PSTAVFGYGR RICPGRYFAL
NALYLMIAHT LAVFDIKPAL DENDNEKEFK ADVTGGMISQ PVPFQCMIVP RSKAAADLIQ
NSDLME
//
