HEPA_ASPOR
ID HEPA_ASPOR Reviewed; 160 AA.
AC Q2U0K2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Sesquiterpene cyclase hepA {ECO:0000303|PubMed:30466366};
DE EC=4.2.3.- {ECO:0000305|PubMed:30466366};
DE AltName: Full=Heptelidic acid biosynthesis cluster protein A {ECO:0000303|PubMed:30466366};
DE Flags: Precursor;
GN Name=hepA {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000408;
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, INDUCTION, 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: Sesquiterpene cyclase; part of the gene cluster that mediates
CC the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that
CC acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH)
CC and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy
CC sauce brewing. {ECO:0000269|PubMed:30466366}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UR08};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UR08};
CC -!- INDUCTION: The expression is positively regulated by the 2 cluster-
CC specific transcription factors hepR and hepS.
CC {ECO:0000269|PubMed:30466366}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:Q9UR08}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of heptelidic acid.
CC {ECO:0000269|PubMed:30466366}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AP007171; BAE64913.1; -; Genomic_DNA.
DR RefSeq; XP_001826046.2; XM_001825994.2.
DR AlphaFoldDB; Q2U0K2; -.
DR SMR; Q2U0K2; -.
DR EnsemblFungi; BAE64913; BAE64913; AO090011000408.
DR GeneID; 5998149; -.
DR KEGG; aor:AO090011000408; -.
DR HOGENOM; CLU_1917780_0_0_1; -.
DR OMA; IRIYLEM; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Lyase; Magnesium; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..160
FT /note="Sesquiterpene cyclase hepA"
FT /id="PRO_5005362042"
FT MOTIF 25..29
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:B2J4A4"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ SEQUENCE 160 AA; 18825 MW; 6BEF6E425B26CFE7 CRC64;
MWWPRATADR LQTCTFWFLW LFTWDDEIDQ STSDLFIHIH KANDFRKESL EYVKFCLGVG
DDETAKWDFQ NNPPNRPLIR SLDVIGAHLQ KVYNHDQIMT FVNEIDYYMG CQQREQKRKL
TGRLPIVAEY LETRMGTSAV TSMLALNEYG GALILGLKRR
