ID Q2PGZ5_ASPOZ Unreviewed; 528 AA.
AC Q2PGZ5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Oxidoreductase A;oxidoreductase/cytochrome P450 monooxygenase {ECO:0000313|EMBL:BAE71330.1};
GN Name=ordA {ECO:0000313|EMBL:BAE71330.1};
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:BAE71330.1};
RN [1] {ECO:0000313|EMBL:BAE71330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RIB40 {ECO:0000313|EMBL:BAE71330.1};
RX PubMed=16391082; DOI=10.1128/AEM.72.1.484-490.2006;
RA Tominaga M., Lee Y.H., Hayashi R., Suzuki Y., Yamada O., Sakamoto K.,
RA Gotoh K., Akita O.;
RT "Molecular analysis of an inactive aflatoxin biosynthesis gene cluster in
RT Aspergillus oryzae RIB strains.";
RL Appl. Environ. Microbiol. 72:484-490(2006).
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|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; AB196490; BAE71330.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2PGZ5; -.
DR VEuPathDB; FungiDB:AO090026000027; -.
DR OMA; HYESGSH; -.
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; cd11065; CYP64-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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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, ECO:0000313|EMBL:BAE71330.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004213430"
SQ SEQUENCE 528 AA; 60227 MW; DEF1C5E14215B7DA CRC64;
MIYSIIICAG ALLGLWILEK LLAPKDTRPP LPPGPWRKPI IGNLTDFPPK GTPEWLFWAK
HQERYGPMSS LEVMGQTIIM INDAQLGIEI MHKKSALSQM IPDAPFAHMA GWGMSLATER
NRQAWKTIRA NMKQEIGTRR AISTFHSKME IGIRRFLLRT LDNPDDLRFH IRKEANAFMM
DVAYGYTIAP HGKDELYDLT QQSVRQFSHI FSPGEWSVNF FPILRYVPSW FPGASFQIKA
AEYKWTIERM TMVPYLWIKD QVARGCSRPS ILLRLLQKGH YESGSHQEQV LVWTNAEFVM
GGSDTTVSAV SSLFVAMALY PEVQRKAREE LDRVVGPTTL ATFEHRSQLP FIDALVKEVF
RWHPASPLGA PHITQEDQIW DGYLLPKGAL LLPNIWTFTH DPSVYHDPMV FKPERFLEGK
DSPPETDPMK FVFGFGRRIC PGRFVTDEKL FLIACHAVSC FFISPKDPGA PEPDWLPGVI
SQPGTFDLNV VPRSPAHEEL IRSIETDHPW KNADATDISR FMARNQMI
//
