ASTB_ASPOR
ID ASTB_ASPOR Reviewed; 512 AA.
AC Q2UEK3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cytochrome P450 monooxygenase astB {ECO:0000303|PubMed:27628599};
DE EC=1.-.-.- {ECO:0000305|PubMed:27628599};
DE AltName: Full=Astellolide biosynthesis cluster protein B {ECO:0000303|PubMed:27628599};
DE Flags: Precursor;
GN Name=astB {ECO:0000303|PubMed:27628599}; ORFNames=AO090026000584;
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 -!- 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; BAE60012.1; -; Genomic_DNA.
DR RefSeq; XP_001822014.2; XM_001821962.2.
DR AlphaFoldDB; Q2UEK3; -.
DR SMR; Q2UEK3; -.
DR EnsemblFungi; BAE60012; BAE60012; AO090026000584.
DR GeneID; 5994042; -.
DR KEGG; aor:AO090026000584; -.
DR HOGENOM; CLU_001570_2_1_1; -.
DR OMA; TWAVMAD; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006564; Chromosome 3.
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 Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..512
FT /note="Cytochrome P450 monooxygenase astB"
FT /id="PRO_0000450114"
FT BINDING 418
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 512 AA; 58861 MW; 8BF630BF0CA3205F CRC64;
MGLILAFAVI LLSTCWFLWY SRKAVFDRLP PGPRPLPFLK SRQELRQTRQ WEALDDLHRQ
YGPLVGMTWG GRPAVLIGKR EIAKDLFGKR GSIYSSRARL VMGLDIMTGG DHVFFLPYGP
KWKKLSRIQA TFLNRPAVKH YRPLQELESL HTLQDLLHSD DYEACFSRFQ ASLTHALAYG
TRLHSATDPQ LTELENIART FISAATNSHW MVDSFPILKY VPACLAPWKR FGQQIHAQTV
SLFQGKMAVA EHTRSWNWVK HIRALKHTSG VTDHEMVYVI GSIYQAGVGI ITATLRLFIM
ACVLHPEAVK AAQDELDRVV GSDRLPTLND LGHLPYVEAF VKEVLRWRPL VLAATHSVTQ
DDDYRGYRIP RHAVILSNQW AMDMDREVWD SPEQFRPDRW MSDRKRMPSA FGLGQRMCAG
QYMAMESLLI MASRMLWAFT FEHAWEGGKR VEIDSWAFHE ESLFLVPKPY RARIQPRDPH
RLHVIQSTWQ AAEKDIDPLL DQIGREIHTA SA
