ID   D4QC24_ASPOZ            Unreviewed;       510 AA.
AC   D4QC24;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:BAJ04372.1};
GN   Name=CYP58H1 {ECO:0000313|EMBL:BAJ04372.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:BAJ04372.1};
RN   [1] {ECO:0000313|EMBL:BAJ04372.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RIB40 {ECO:0000313|EMBL:BAJ04372.1};
RA   Nazmul Hussain Nazir K.H.M., Ichinose H., Wariishi H.;
RT   "Molecular characterization and isolation of cytochrome P450 genes from the
RT   filamentous fungus Aspergillus oryzae.";
RL   Arch. Microbiol. 192:395-408(2010).
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; AB514695; BAJ04372.1; -; mRNA.
DR   AlphaFoldDB; D4QC24; -.
DR   VEuPathDB; FungiDB:AO090001000170; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd11062; CYP58-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   2: Evidence at transcript level;
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|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   510 AA;  57604 MW;  236A6CD0155D83AE CRC64;
     MDEFTISAGS LCLLSLVVGF IIQSVYRLFF HPLRKFPGPK LGAISHLYEF YYDVIYNGSY
     LFKIEQLHQK YGPVVRINPR ELHINDPYYY EQIYAGSSRI REKDPRFIGV FTTPLPMVAT
     VGHEHHRIRR GLLSSYFSRR ALKKAELIID QKVDRLLVRF HSAFKCHAVL PLQRVFAALA
     ADIVSEYCYG ASQGYLEQKV FQNQMIDAVN YVMSMCHINK SIPIIPKLLR CVPVGLMEKL
     GLQMADVIGV RNLIRRQAAK SLDKEWLSHD TNMLSKNVFD AIAAADVAPQ EKTLRRLEEE
     GAALFGAGIE TTARALTVAM FHLISDETMI RKLRDELKQV MLSPASRPTW AELEQLPYLT
     GVVNESLRLS FGLVARSPRV SPIESLAYGE YVIPPGTPVS QSAYFVHMNP QVFPEPESFN
     PERWIKAAEK GQYLSRFLVA FSKGSRQCLG MNLAYAELYL TLARIVRLVD MKLVGTTIDN
     IRVGRDLGHP APKAGNFKVK VEVMGIASKS
//