ID A0A0D2DSA1_9EURO Unreviewed; 557 AA.
AC A0A0D2DSA1;
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 monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_01599 {ECO:0000313|EMBL:KIW45893.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW45893.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW45893.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW45893.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
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}.
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DR EMBL; KN847333; KIW45893.1; -; Genomic_DNA.
DR RefSeq; XP_016266109.1; XM_016402212.1.
DR AlphaFoldDB; A0A0D2DSA1; -.
DR STRING; 215243.A0A0D2DSA1; -.
DR GeneID; 27353673; -.
DR VEuPathDB; FungiDB:PV06_01599; -.
DR HOGENOM; CLU_001570_14_11_1; -.
DR OrthoDB; 1774992at2759; -.
DR Proteomes; UP000053342; 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: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.
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:UP000053342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 557 AA; 63165 MW; 2203EFBBA2A46FB2 CRC64;
MDKWGLSGYQ YTCRTPIQQT NVEDMAGSIL SEGPSSQLLG LVTQNHGSLP IVILASLVGY
VLLKSIYRVY FHPLAKYPGP FWAKVTSLYD FYQAWSEHRA HNLLALHREY GPIVRYAPDK
LVFNEPQAWQ DIYAYKANVR KSDLSIASQS NPESTDTFSE LYKEPALKKR KVLSYGFSES
SLRSFEAYML DQINLFCHQL LNPSNEKVKD MSLWFNYLSY DIMGEMVFGR GFGMLTDPSL
RYILELIDAT VFSYLLGGII PWLHRSGVIT LLMPRIFFGR KRFVAEAGKR ITERIKLGPD
AEGINGRKDF FHWLLNGKDE NGQPLQHARL GAEGVLLILA GSDTSSASLA GTLFYLMQQP
RCQKKLLEEL ERTFDNIDEI RLGDKLTSCV YLRACVDEAL RMASAGPGIS ERTVLKGGTT
INGEYFPEGT TVGSGGWASS YNEKYIRDCE KYWPERHIPG EEFSAEEVQI ARSAYWPFGL
GARKCVGMKV ALNELHLTIA RLIYLLEPIP EKPEEFQKNF EILDHQNPKK VGPWASFKLR
LGKKLPDLKP TQMQGQD
//
