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Database: UniProt
Entry: G7XAJ0_ASPKW
LinkDB: G7XAJ0_ASPKW
Original site: G7XAJ0_ASPKW 
ID   G7XAJ0_ASPKW            Unreviewed;       506 AA.
AC   G7XAJ0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Benzoate 4-monooxygenase cytochrome P450 {ECO:0000313|EMBL:GAA83889.1};
GN   ORFNames=AKAW_02004 {ECO:0000313|EMBL:GAA83889.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA83889.1};
RN   [1] {ECO:0000313|EMBL:GAA83889.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA83889.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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; DF126450; GAA83889.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XAJ0; -.
DR   STRING; 1033177.G7XAJ0; -.
DR   VEuPathDB; FungiDB:AKAW_02004; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; G7XAJ0; -.
DR   Proteomes; UP000006812; 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; cd11058; CYP60B-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:SF240; CYTOCHROME P450 MONOOXYGENASE STCF-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, ECO:0000313|EMBL:GAA83889.1};
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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   506 AA;  58288 MW;  B7E86282516AB35B CRC64;
     MPTVLALIGI SYLAYTICAA IWNIYLHPLR RIPGPKLWLA FPILRYISNM RGVLDRDMRA
     LHKRYGGVVR FTPNEVSFIT TQAWKDIYGH GHRQLPKVSG SASNPKDIIS ANDSDHTRFR
     KAISHAFSAK GLQAQEPFIM DYVDKLINKL HGMAESQVAV DMAKWYNLTT FDLIGDLAFG
     QSFGGLDSTE YHYWVSTIFE FIKAIAFAKF KDDYPMVFNA LKRFLPKHLL EAKRRQDEYS
     WNTVQTRLHD QTDRGQADFM QSMLRHRGDK DGLTDEELAA NASILVIAGS ETTATLLSGL
     TYWLLRHPKE MEKVKFEVRS VMKTEEDITV NNATAKLPYM LACIDEAFRM YPPVAGHLQR
     YIPDQPTEIS GYLLPKKASP TQNSEITNAN TFQTRVSVHQ SAAYRSPLNF YKPEEFIPER
     WLPESKNDPS SPFYRDNREI LQPFSVGPRN CIGRNLAYAE MRVIFARVLW NFDIELCEES
     REWHNQKSYN LWAKPPLMCK LKARVH
//
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