ID A0A074X0V5_AURPU Unreviewed; 469 AA.
AC A0A074X0V5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative cytochrome P450 {ECO:0000313|EMBL:KEQ79075.1};
GN ORFNames=M438DRAFT_400813 {ECO:0000313|EMBL:KEQ79075.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ79075.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ79075.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ79075.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KL585010; KEQ79075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X0V5; -.
DR STRING; 1043002.A0A074X0V5; -.
DR HOGENOM; CLU_001570_14_2_1; -.
DR OrthoDB; 509202at2759; -.
DR Proteomes; UP000030706; 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11059; CYP_fungal; 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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF164; P450, PUTATIVE (EUROFUNG)-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 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
SQ SEQUENCE 469 AA; 53120 MW; 0277691D6C862F5A CRC64;
MFFIYLVPLL SLIYFLYTRL TSPLAKLPGP LYTLFTPLYL IYNEFTGNRR LYVHSLHTIH
GPIVRLGPNE ISFASYEAMK EIYTSGGSGF DRTEFYELFK QFGTKTLFSM PPRGEHSKRK
RILADRYANT NVMRPETIEA LTVRARQCLQ NCLAEDGGDA DVYVHLHCFA LDGASQHLFA
PNGTNSLSDP EDLKIMEEMS YADSLRAPYL EYYAPGLAAF FDKFNSKRSR SVPLANDFVL
GAAQKSNPAS YSLISKLHSK ASDLEELSAP AECMDHLAAG IDTTGDGLCF LMHELSLPHN
MHIQQKLREE INSSEGKSFD QLPYLDAVVK EGLRVFPPIP MSFPRYTPDS GTTLDGYYIP
GRVIVSCQPW TLHKDPHVFP SPELFNPQRW LEEEGELERN RMFFAFSQGA RGCIGKHLAL
AEMKILLREV YGTYQTKLGK EKADMRLDDQ IISSRPKGQK CRLAFEKVV
//
