ID   HEPH_ASPOR              Reviewed;         521 AA.
AC   Q2U0J6;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cytochrome P450 monooxygenase hepH {ECO:0000303|PubMed:30466366};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30466366};
DE   AltName: Full=Heptelidic acid biosynthesis cluster protein H {ECO:0000303|PubMed:30466366};
GN   Name=hepH {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000415;
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: Abolishes the production of heptelidic acid.
CC       {ECO:0000269|PubMed:30466366}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AP007171; BAE64919.1; -; Genomic_DNA.
DR   RefSeq; XP_001826052.1; XM_001826000.1.
DR   AlphaFoldDB; Q2U0J6; -.
DR   SMR; Q2U0J6; -.
DR   EnsemblFungi; BAE64919; BAE64919; AO090011000415.
DR   GeneID; 5998155; -.
DR   KEGG; aor:AO090011000415; -.
DR   VEuPathDB; FungiDB:AO090011000415; -.
DR   HOGENOM; CLU_001570_14_4_1; -.
DR   OMA; WRHSMEA; -.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..521
FT                   /note="Cytochrome P450 monooxygenase hepH"
FT                   /id="PRO_0000450832"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         455
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   521 AA;  58895 MW;  824F414751E12907 CRC64;
     MASLTGAAAV LLAFILAYST ALTIYRLFFH PLARFPGPRL AAATKWYEFY FDIIKSPGGQ
     FFKELSRMHD VYGPIVRVNP DEIHVRDAAW FEVLYAPNPT KRNKYRPSAE MAGLTLGIHG
     TVDHDLHRRR RMAIAPMFNK QSILSAEHLI KQHIDELTDV FESYLGTNNP INLQTTFLAY
     TTDVLYHYMF DTDAGYQRDS GAAQQWRHSM DAVAQATPFL KQFPSLLSRV ALIPLPMLIW
     VLKRIQPDVA GLLGTHQLMA SIVSKYMASK PEEDQDELIA TKAVKPRTLF HAIEASSLPP
     HEKAPTRLAQ EGLTVLFAGG ETGSRLLAHT VYHLLKNPEI LEKVRKEILD AAGDSNQLPD
     MKALEALPWL TASVRESLRL RAATTSRLPL VTEKPLAYAD WVIPPNTPVS MSHGDILHNE
     DIFPDPMKFM PSRWFNASPQ QNRLFVPFGK GTRMCVGMNF AYCEIYMSLA VILARFDLEL
     YDTRWERDVH YTRDCFLGEP DPASPGIRVK VVADHKTFTR S