HEPD_ASPOR
ID HEPD_ASPOR Reviewed; 500 AA.
AC Q2U0K0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cytochrome P450 monooxygenase hepD {ECO:0000303|PubMed:30466366};
DE EC=1.-.-.- {ECO:0000305|PubMed:30466366};
DE AltName: Full=Heptelidic acid biosynthesis cluster protein D {ECO:0000303|PubMed:30466366};
GN Name=hepD {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000411;
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; BAE64915.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2U0K0; -.
DR SMR; Q2U0K0; -.
DR EnsemblFungi; BAE64915; BAE64915; AO090011000411.
DR HOGENOM; CLU_001570_14_11_1; -.
DR OMA; MEQSTHI; -.
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..500
FT /note="Cytochrome P450 monooxygenase hepD"
FT /id="PRO_0000450830"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 445
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 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 500 AA; 56950 MW; 6FAAF223920A09BD CRC64;
MNSISALFSA GGFQWILLSL SLAFIVVYSL FYLAVGLYNL YFHPLARYPG PLLGRASSLW
YARSLARGTV AQDTLKLHEK YGDVVRIAPD ELSFIQPENW SAIYGHQLGK DYRELIKDPR
YHDTVKPTPT ILTGDWDEHT FYRKILSNSF SEKSLKDQEH ILHHFVDLFV QRLKETSAEG
TRELNMTDQW NYLTFDVIGF LTYGEEFHCL TSSKLHDWIE AMLCVAILMS LGQAARHLPF
PFDKIYKQWA IPSNVKRQVA LHRDLTEVAI PHIPIQYASA YRLNSRKGDI PYSVLKEHAN
ILTIGGSETT ATLLAGATFH LGKNPPVLQK LATEIRTTFV NDGEITVARL SECKYLLATV
EECLRIYPPS PANHTRMVPK EGIVLNDQHI PGGIGVGMPM YAAFRASSNF TYPDRFAPER
WLGDPMYSKD KKGALQPFSF GPRNCLGRHL AYQEIKLALA KLVYHFDLEL NPKCGDWDEQ
KNFTFWVKPP LWVNLHPVKS
