ASTF_ASPOR
ID ASTF_ASPOR Reviewed; 521 AA.
AC Q2UEK7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome P450 monooxygenase astF {ECO:0000303|PubMed:27628599};
DE EC=1.-.-.- {ECO:0000305|PubMed:27628599};
DE AltName: Full=Astellolide biosynthesis cluster protein F {ECO:0000303|PubMed:27628599};
GN Name=astF {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000579;
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 INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27628599; DOI=10.1038/srep32865;
RA Shinohara Y., Takahashi S., Osada H., Koyama Y.;
RT "Identification of a novel sesquiterpene biosynthetic machinery involved in
RT astellolide biosynthesis.";
RL Sci. Rep. 6:32865-32865(2016).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of astellolides, drimane-type sesquiterpene
CC esters that show antimicrobial, anti-inflammatory, and anti-tumor
CC activities (PubMed:27628599). The first step in astellolide
CC biosynthesis is performed by the sesquiterpene cyclase astC that
CC catalyzes the formation of drimanyl pyrophosphate from farnesyl
CC pyrophosphate (PubMed:27628599). Drimanyl pyrophosphate is then
CC dephosphorylated by the sesquiterpene phosphatase astI to produce
CC drimanyl monophosphate which is further dephosphorylated to drim-8-ene-
CC 11-ol by atsK (PubMed:27628599). Drim-8-ene-11-ol is converted to
CC confertifolin, probably by the cytochrome P450 monooxygenase astD
CC and/or the dehydrogenase astE (PubMed:27628599). The cytochrome P450
CC monooxygenases astB, astF and astJ then hydroxylate confertifolin at
CC C6, C14, or C15 to form trihydroxy confertifolin (PubMed:27628599). The
CC nonribosomal peptide synthetase astA catalyzes ester bond formation
CC between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy
CC benzoic acid (4HBA), leading to the formation of dideacetyl
CC astellolides A and B, respectively (PubMed:27628599). Finally, the O-
CC acetyltransferase astG converts dideacetyl astellolides A and B into
CC deacetyl astellolides A and B (PubMed:27628599).
CC {ECO:0000269|PubMed:27628599}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:27628599}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is regulated by the secondary metabolite
CC regulator cclA. {ECO:0000269|PubMed:27628599}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of trihydroxy
CC confertifolin and deacetyl astellolides A and B.
CC {ECO:0000269|PubMed:27628599}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AP007159; BAE60008.1; -; Genomic_DNA.
DR RefSeq; XP_001822010.2; XM_001821958.2.
DR AlphaFoldDB; Q2UEK7; -.
DR SMR; Q2UEK7; -.
DR EnsemblFungi; BAE60008; BAE60008; AO090026000579.
DR GeneID; 5994038; -.
DR KEGG; aor:AO090026000579; -.
DR VEuPathDB; FungiDB:AO090026000579; -.
DR HOGENOM; CLU_001570_2_1_1; -.
DR OMA; IWENAER; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006564; Chromosome 3.
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 GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..521
FT /note="Cytochrome P450 monooxygenase astF"
FT /id="PRO_0000450116"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 430
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 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 59544 MW; 0141E25DE7763C74 CRC64;
MLPTLPNIAG RINTMATFLL PVAIGTIILL FLYGKYVTST LIPGPPTLPL IGNLHQLPSD
DRRHVLAQWH KKHGPIISLK FGWSSVVILG NIAVTKELFG KRSLKYGSRP RMVMARDCMT
KQMQTSTLPW GEKWKIHNRI QLSLVGGPKI RSYQSLLDIE SCKVLYQLLS TESLVTCFNR
FKFNIIYTLA YGKDPDQNES DFHEILELAD HFTQTLTNAT WVVDLFPILN CLPRRLAPWK
AVGDDFHRRA MGWFRRNSEA AVKSNSWNWT KHVQFNEDTG NLSVSEMQYL IGVLFEAGVD
STATVLHFFV LACTLYPDAV TKARQELDKV VGSARLPTPK DLPQLPYVKA FIQEVLRWRP
ITAEGLPHFT LEDDKYQGYD IPKGSTVIFN YWSGHMDEDT YQHADQFCPE RWIERPDLPL
GVFGYGRRAC AGRRLALMSL ETLIPKLLWA FDFRSPAGTD HGKSRDPGTE HQGALIKPRS
FPVSWHPVSN DRRLIIERLF QERDKDLDTV LDDIGKAFER Y
