ID A0A0D2BX16_9EURO Unreviewed; 532 AA.
AC A0A0D2BX16;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_05572 {ECO:0000313|EMBL:KIW56961.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW56961.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW56961.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW56961.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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; KN847319; KIW56961.1; -; Genomic_DNA.
DR RefSeq; XP_013317545.1; XM_013462091.1.
DR AlphaFoldDB; A0A0D2BX16; -.
DR STRING; 348802.A0A0D2BX16; -.
DR GeneID; 25327480; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000054342; 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 CDD; cd11061; CYP67-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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF172; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 532 AA; 60363 MW; F2D3BB5524AEF9B0 CRC64;
MLSLCILPLI FASLLLSWLS WCLFSYLKDG KKLRQYPSAS LLAGLSSIWI MWKNYTHQRS
FTLYDAHMKL GKVVRIAPNH LSFISPDAIK DVYGHGTPAL KDKFYNAFVG SHPNLLDVRD
KELHGKKRKL FAVALAQKSV EEKEHAIRDD ISKLVVQWDK LATLPPKAGE SAFPNHELVD
IRRWFNLLML DLVCDLTFSI KQGFVTQGDD LTTCETVDGR KYLARPEAGT NANLQYVSTL
GSGDPNWLRF LQKLFFWHRG VKDGETFTGY VLHLIRRRFA LESGKDAKDF NDFFSGLNYT
REGIPIGMDL GELVQECSLL MNAGSETTTC ALQNIMYYLI INPRCMQKLY EEVSTVFEGD
DDDNNSDSAE AAVPSYDRIK FLPYLRACID ETLRHRPSLA IGLPRVTPPE GMYVAGTWVP
GETTVSIPTW GMHHDPAVFE KPFDFIPERW LGDSASNLQR NMLAFSAGAR QCVGRNVAYT
EMSLIVATIV NRYEFALCRP DWEPTVYETM VLKSGPMPVK IWRRQKGVRK TG
//
