位置:首页 > 蛋白库 > BOA2_BOTFB
BOA2_BOTFB
ID   BOA2_BOTFB              Reviewed;         529 AA.
AC   B1GVX4;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=FAD-binding monooxygenase BOA2 {ECO:0000303|PubMed:21722295};
DE            EC=1.14.13.- {ECO:0000305|PubMed:21722295};
DE   AltName: Full=Botcinic acid biosynthesis cluster A protein 2 {ECO:0000303|PubMed:21722295};
GN   Name=BOA2 {ECO:0000303|PubMed:21722295};
GN   Synonyms=MO1 {ECO:0000303|PubMed:18208491};
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=B05.10;
RX   PubMed=18208491; DOI=10.1111/j.1365-2958.2008.06105.x;
RA   Schumacher J., Viaud M., Simon A., Tudzynski B.;
RT   "The Galpha subunit BCG1, the phospholipase C (BcPLC1) and the calcineurin
RT   phosphatase co-ordinately regulate gene expression in the grey mould fungus
RT   Botrytis cinerea.";
RL   Mol. Microbiol. 67:1027-1050(2008).
RN   [2]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=21722295; DOI=10.1111/j.1364-3703.2010.00692.x;
RA   Dalmais B., Schumacher J., Moraga J., Le Pecheur P., Tudzynski B.,
RA   Collado I.G., Viaud M.;
RT   "The Botrytis cinerea phytotoxin botcinic acid requires two polyketide
RT   synthases for production and has a redundant role in virulence with
RT   botrydial.";
RL   Mol. Plant Pathol. 12:564-579(2011).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23203902; DOI=10.1002/cbic.201200487;
RA   Massaroli M., Moraga J., Bastos Borges K., Ramirez-Fernandez J., Viaud M.,
RA   Gonzalez Collado I., Duran-Patron R., Hernandez-Galan R.;
RT   "A shared biosynthetic pathway for botcinins and botrylactones revealed
RT   through gene deletions.";
RL   ChemBioChem 14:132-136(2013).
CC   -!- FUNCTION: FAD-binding monooxygenase; part of the gene cluster A that
CC       mediates the biosynthesis of botcinic acid and its botcinin
CC       derivatives, acetate-derived polyketides that contribute to virulence
CC       when combined with the sesquiterpene botrydial (PubMed:18208491,
CC       PubMed:21722295). Botcinic acid and its derivatives have been shown to
CC       induce chlorosis and necrosis during host plant infection, but also
CC       have antifungal activities (PubMed:18208491, PubMed:21722295). Two
CC       polyketide synthases, BOA6 and BOA9, are involved in the biosynthesis
CC       of botcinins. BOA6 mediates the formation of the per-methylated
CC       tetraketide core by condensation of four units of malonyl-CoA with one
CC       unit of acetyl-CoA, which would be methylated in activated methylene
CC       groups to yield a bicyclic acid intermediate that could then either be
CC       converted to botrylactone derivatives or lose the starter acetate unit
CC       through a retro-Claisen type C-C bond cleavage to yield botcinin
CC       derivatives (PubMed:23203902). The second polyketide synthase, BOA9, is
CC       probably required for the biosynthesis of the tetraketide side chain of
CC       botcinins (Probable). The methyltransferase (MT) domain within BOA6 is
CC       probably responsible for the incorporation of four methyl groups
CC       (Probable). The trans-enoyl reductase BOA5 might take over the enoyl
CC       reductase function of BOA6 that misses an ER domain (Probable). The
CC       monooxygenases BOA2, BOA3 and BOA4 might be involved in further
CC       hydroxylations at C4, C5 and C8, whereas BOA7, close to BOA9, could
CC       potentially be involved in the hydroxylation at C4 in the side chain of
CC       botcinins (Probable). {ECO:0000269|PubMed:18208491,
CC       ECO:0000269|PubMed:21722295, ECO:0000269|PubMed:23203902,
CC       ECO:0000305|PubMed:23203902}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:H3JQW0};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0};
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:21722295,
CC       ECO:0000305|PubMed:23203902}.
CC   -!- INDUCTION: Expression of the botcinic acid clusters genes BOA1-13 and
CC       BOA17 is coregulated by BCG1 during both in vitro and in planta growth.
CC       {ECO:0000269|PubMed:18208491, ECO:0000269|PubMed:21722295}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM930229; CAP58783.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1GVX4; -.
DR   SMR; B1GVX4; -.
DR   VEuPathDB; FungiDB:Bcin01g00020; -.
DR   PHI-base; PHI:2289; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Virulence.
FT   CHAIN           1..529
FT                   /note="FAD-binding monooxygenase BOA2"
FT                   /id="PRO_0000444658"
FT   BINDING         58..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         68..70
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         70..71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         76
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         198..204
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT   BINDING         221..222
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:H3JQW0"
SQ   SEQUENCE   529 AA;  61060 MW;  FBC694BFAE7945B5 CRC64;
     MSSEKMPIET LQADEHRFAI ILGAGAAGII QGCTFIREKT LPLEEFQILE RQSAFGGVWW
     KNTYPGAACD IPSHEYQISF ALNPYWSRTF APQPEIQKYF EDVALQYELH KSTTFNTEIV
     EAKWDDSRLL WLVETTDLTT GDTKLWSCHV LIGALGAFTV PKKAPVKNVD AFKGEEWHSV
     DWPKNANLKG KTVAVIGTGP SACQFIPNIY PEVKSLIVYQ RSPGHVLPRN DVVVGSLTKW
     MFAHIPFLMR FNRWFWMKKD EILRPRLFTV GSWLQKIVIS MTRNHLYKQI KDDTLRRKLE
     SKDVFGCKRP LMLSDYYPIF NNDNVELVTD SVTELTENGI KSRNTDTGEE MERETDVLIW
     GTGYNPVDFG LPVPTKGRSG QLLCDKYQPE LFSLYGVAVD DFPNYFNFLG PNSSSFETSV
     MELFELQAHH NSIATEYLFQ KNVGTFRYAI MPKEERVRSW TLSLRPGQAK LPPANPNCKS
     YYRSKIGHVY RYPYPYWQYK ALIAKLDFKR DWVLLQQRIG QKEVKVLEF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024