ID D4QCC4_ASPOZ Unreviewed; 517 AA.
AC D4QCC4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:BAJ04472.1};
GN Name=CYP5113A1 {ECO:0000313|EMBL:BAJ04472.1};
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:BAJ04472.1};
RN [1] {ECO:0000313|EMBL:BAJ04472.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RIB40 {ECO:0000313|EMBL:BAJ04472.1};
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 ECO:0000256|PIRSR:PIRSR602402-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; AB514795; BAJ04472.1; -; mRNA.
DR AlphaFoldDB; D4QCC4; -.
DR VEuPathDB; FungiDB:AO090026000094; -.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR CDD; cd11063; CYP52; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01239; EP450IICYP52.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 2: Evidence at transcript level;
KW Heme {ECO:0000256|PIRSR:PIRSR602402-1};
KW Iron {ECO:0000256|PIRSR:PIRSR602402-1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602402-1};
KW Monooxygenase {ECO:0000313|EMBL:BAJ04472.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 463
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602402-1"
SQ SEQUENCE 517 AA; 58786 MW; 029CC8EB581DDA44 CRC64;
MTAETGFVPT VFSLPSESAY SWVWAVSAGL VAIFVLYLTQ GIARRRFAYA HGCQAPPRYA
HRDPILGLDS LRDSMQARKS DRYFRREQQL HQAYGNTFMS LLLGSWMVNT IEPKNLEVLF
STKFADYEVG FRRRNAFAPL FGKSIFQSDG TRWQTLRSQL QLCFSRVQTS QLGLLESHCQ
RLLAALPSDN QKFDLALFLH RFAADVSTDF LFGESINSLE NPQNLDGGAL KAFADTHSTC
ELRWLLGSMS WIWPQRTFMK NVRLTHRFIQ RYVDAALERE VTPPGKASDQ QNEQRILFID
QLRQRTQDPI ALRDELTTLY FAGTDAPAAL LINLFFVFSK RPDVWDRVRS EVQSLGGKAP
DLQQLKGLRY VQDCIRECLR LYPPQPSNSR VAVRDTVLPT GGGPDGGSPV LVPKGMMVHL
SVYALHHRKD LWGEDADEFR PERWSYEKQT WKYIPFLGGP RNCVGMDFGL NEVAYAVVRM
AQNFQTITSV DPDEWVEGSS IALESKNGVK VVMCRDA
//
