ID A0A2H3CGZ1_ARMGA Unreviewed; 523 AA.
AC A0A2H3CGZ1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PBK80614.1};
GN ORFNames=ARMGADRAFT_1147692 {ECO:0000313|EMBL:PBK80614.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK80614.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293742; PBK80614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3CGZ1; -.
DR STRING; 47427.A0A2H3CGZ1; -.
DR InParanoid; A0A2H3CGZ1; -.
DR OMA; AQQHITH; -.
DR OrthoDB; 3640568at2759; -.
DR Proteomes; UP000217790; 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:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000217790};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..523
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013655544"
SQ SEQUENCE 523 AA; 58117 MW; 014BA1337E6DFB31 CRC64;
MLSIGALFPV TLTLLTLLVL RCIQHRRDPA SKPTLEAHWL WGHEYVVWQH EACAMYLKWA
TDLGPLYRIK ASFFQRDVIV AADNLASHHI LANAYRYHVL PAKAPAFLPL TDKLLGKGVV
YAQGDEHKHQ RRLIAPAFTL GAVKGMSDDV VECTQKFVER VANHVGSQGY ETTMDIAPFV
SACTLDIIGR IAFGHDFGCG ESKEARDIAE SWHKDVLLGR TMAGFLAPIM MCAFPWITEL
PIPALQTDGV AKRVAINLAG ELLRQNKAQL ESGDGKDILS ILVKDQKKSK HDERLSQTTL
LENVSLEMVG HETTSCTVSF TLLELARHPA VQQKLRQEIR DLSDFSYDHI QSLPYLDAVC
REGLRVHPAA PRTDRIALED DVIPLSQPLT TVDGKTVSSI AIKAGQVFHI PNAVQNIDPF
VWGKDAEEFK PERWLLSGGV PSADQLPHGP YGNIASFLDG PRSCIGWRLA LLEFKIMISL
LIRDFELIST PDDVKGYISG TLQAFVGEEV KMPIHVKMLR SSE
//