ID   HEPC_ASPOR              Reviewed;         509 AA.
AC   Q2U0K1;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cytochrome P450 monooxygenase hepC {ECO:0000303|PubMed:30466366};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30466366};
DE   AltName: Full=Heptelidic acid biosynthesis cluster protein C {ECO:0000303|PubMed:30466366};
GN   Name=hepC {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000410;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Reduces the production of heptelidic acid.
CC       {ECO:0000269|PubMed:30466366}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE64914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007171; BAE64914.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2U0K1; -.
DR   SMR; Q2U0K1; -.
DR   EnsemblFungi; BAE64914; BAE64914; AO090011000410.
DR   HOGENOM; CLU_001570_14_0_1; -.
DR   Proteomes; UP000006564; Chromosome 7.
DR   GO; GO:0016021; C:integral component of 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   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Cytochrome P450 monooxygenase hepC"
FT                   /id="PRO_0000450829"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         454
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"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   509 AA;  57829 MW;  4EA7E6DC5335A6F6 CRC64;
     MQQNMIIPSF WTGTAIIGLV ACAYVSYQCL LSPLARFPGP FAAKLSKGWR AYKTANGQWH
     RKLVDLHRKY GHVVRIAPNE LSVGDPSSFR KIYSPAEAGN GFNKAACYSV VQGNRPFDLT
     GERNEKVHSE QRKLVATAYS MSSMVHFESK VNVVIETVIH KLEARCRKTI DLGHWLQMWA
     FEPTRPLLNS LKPDVIGSVS FSQPFGYVES GDDEGVFKRI QNAMGSAAWL MHAGWLFRLH
     QKLIPICGNW LAVNDRNGYF FQVACREVSG RINRGGDDKD IIGQLLETQK IKPQLKDLDI
     SFMMTSNVFA GSDSTSIAFQ SIFYLLLTHP AAHDRLMREL REREEKGELS DPVSFQEAES
     WPYLQAIIYE AMRLYAPAAF VLDRVVPPEG MMIEDKFVPG NTVVGSSAWV IHRNPEIWGP
     DVDTFRPERW LDDSTFLIDK KGALQPFSFG PRNCLGRHLA YQEIKLALAK LVYHFDLELN
     PKCGDWDEQK NFTFWVKPPL WVNLHPVKS