ID   HEPE_ASPOR              Reviewed;         548 AA.
AC   Q2U0J9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cytochrome P450 monooxygenase hepE {ECO:0000303|PubMed:30466366};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30466366};
DE   AltName: Full=Heptelidic acid biosynthesis cluster protein E {ECO:0000303|PubMed:30466366};
GN   Name=hepE {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000412;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=30466366; DOI=10.1080/09168451.2018.1549934;
RA   Shinohara Y., Nishimura I., Koyama Y.;
RT   "Identification of a gene cluster for biosynthesis of the sesquiterpene
RT   antibiotic, heptelidic acid, in Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 83:1506-1513(2019).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene
CC       lactone that acts as an inhibitor of glyceraldehyde-3-
CC       phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-
CC       tolerant lactic acid bacteria in soy sauce brewing.
CC       {ECO:0000269|PubMed:30466366}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30466366}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of heptelidic acid.
CC       {ECO:0000269|PubMed:30466366}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007171; BAE64916.1; -; Genomic_DNA.
DR   RefSeq; XP_001826049.1; XM_001825997.1.
DR   AlphaFoldDB; Q2U0J9; -.
DR   SMR; Q2U0J9; -.
DR   EnsemblFungi; BAE64916; BAE64916; AO090011000412.
DR   GeneID; 5998152; -.
DR   KEGG; aor:AO090011000412; -.
DR   HOGENOM; CLU_022195_0_3_1; -.
DR   OMA; LAMTSMH; -.
DR   Proteomes; UP000006564; Chromosome 7.
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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..548
FT                   /note="Cytochrome P450 monooxygenase hepE"
FT                   /id="PRO_0000450831"
FT   BINDING         485
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:0000250|UniProtKB:P04798"
SQ   SEQUENCE   548 AA;  62129 MW;  C306D5B2AF67961D CRC64;
     MDHFNLAGPE SNTSITSLEW LGIKNSFTGS HWAHITGLSE LHPTGFLCLI ATLIIGIVHL
     TRGPKPTVLP VVNPPGTFEL TANRVKKEWL VDARQIIRRG FEKFPGKPFN MIAADVGLTT
     VLPPEYASEI RNNPSLSFVA FMAHLFFSEL PGFEPTREGM FDNDIGITVV HKYLTVNLAR
     ITEPLSREAT AALKDIFTDN SEWHDANLKA INLALVARLS SRIFLGEELC RNEEWLKITV
     NYTVDVMKAA ERLRRVPGPL RRIVHWFLPE AQKCRDEVKR AGKVIRPVLE KRRREKATME
     SEGKEALQYN DAIEWFEQMA KSQGTSYDPE VVQLFLSTVA IHTTSDLLTV VMADLARNPE
     IIEPLREEIS SVLRDGGWKK TSLTDMKLLD SVLKESLRLK PIAVVSMRRV AMDHLKLSDG
     TFLPKGTKMA VSSHRMWDPD VYENPEQWDG FRYVNLRETP GQDKHAQFVS TSERHLGFGH
     GKHACPGRFF ASSELKVALC HILMKYDFEL APGTVVQHRY SGASYYADPA IRVMLRRRNV
     ALPSWFER