TRI16_FUSSP
ID TRI16_FUSSP Reviewed; 493 AA.
AC Q86Z65;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Trichothecene 8-O-acetyltransferase {ECO:0000303|PubMed:14532047};
DE EC=2.3.1.- {ECO:0000305|PubMed:14532047};
DE AltName: Full=Trichothecene biosynhesis protein 16 {ECO:0000303|PubMed:14532047};
GN Name=TRI16 {ECO:0000303|PubMed:14532047}; Synonyms=TRI15;
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ATCC 24631 / NRRL 3299;
RX PubMed=14532047; DOI=10.1128/aem.69.10.5935-5940.2003;
RA Peplow A.W., Meek I.B., Wiles M.C., Phillips T.D., Beremand M.N.;
RT "Tri16 is required for esterification of position C-8 during trichothecene
RT mycotoxin production by Fusarium sporotrichioides.";
RL Appl. Environ. Microbiol. 69:5935-5940(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24631 / NRRL 3299;
RX PubMed=14690377; DOI=10.1021/jf030607+;
RA Brown D.W., Proctor R.H., Dyer R.B., Plattner R.D.;
RT "Characterization of a fusarium 2-gene cluster involved in trichothecene C-
RT 8 modification.";
RL J. Agric. Food Chem. 51:7936-7944(2003).
RN [3]
RP FUNCTION.
RX PubMed=3800398; DOI=10.1016/0003-9861(86)90386-3;
RA Hohn T.M., Vanmiddlesworth F.;
RT "Purification and characterization of the sesquiterpene cyclase trichodiene
RT synthetase from Fusarium sporotrichioides.";
RL Arch. Biochem. Biophys. 251:756-761(1986).
RN [4]
RP FUNCTION.
RX PubMed=2317042; DOI=10.1128/aem.56.3.702-706.1990;
RA McCormick S.P., Taylor S.L., Plattner R.D., Beremand M.N.;
RT "Bioconversion of possible T-2 toxin precursors by a mutant strain of
RT Fusarium sporotrichioides NRRL 3299.";
RL Appl. Environ. Microbiol. 56:702-706(1990).
RN [5]
RP FUNCTION.
RX PubMed=7651333; DOI=10.1007/bf02456618;
RA Hohn T.M., Desjardins A.E., McCormick S.P.;
RT "The Tri4 gene of Fusarium sporotrichioides encodes a cytochrome P450
RT monooxygenase involved in trichothecene biosynthesis.";
RL Mol. Gen. Genet. 248:95-102(1995).
RN [6]
RP FUNCTION.
RX PubMed=8593041; DOI=10.1128/aem.62.2.353-359.1996;
RA McCormick S.P., Hohn T.M., Desjardins A.E.;
RT "Isolation and characterization of Tri3, a gene encoding 15-O-
RT acetyltransferase from Fusarium sporotrichioides.";
RL Appl. Environ. Microbiol. 62:353-359(1996).
RN [7]
RP FUNCTION.
RX PubMed=9435078; DOI=10.1128/aem.64.1.221-225.1998;
RA Alexander N.J., Hohn T.M., McCormick S.P.;
RT "The TRI11 gene of Fusarium sporotrichioides encodes a cytochrome P-450
RT monooxygenase required for C-15 hydroxylation in trichothecene
RT biosynthesis.";
RL Appl. Environ. Microbiol. 64:221-225(1998).
RN [8]
RP FUNCTION.
RX PubMed=10583973; DOI=10.1128/aem.65.12.5252-5256.1999;
RA McCormick S.P., Alexander N.J., Trapp S.E., Hohn T.M.;
RT "Disruption of TRI101, the gene encoding trichothecene 3-O-
RT acetyltransferase, from Fusarium sporotrichioides.";
RL Appl. Environ. Microbiol. 65:5252-5256(1999).
RN [9]
RP FUNCTION.
RC STRAIN=ATCC 24631 / NRRL 3299;
RX PubMed=11352533; DOI=10.1006/fgbi.2001.1256;
RA Brown D.W., McCormick S.P., Alexander N.J., Proctor R.H., Desjardins A.E.;
RT "A genetic and biochemical approach to study trichothecene diversity in
RT Fusarium sporotrichioides and Fusarium graminearum.";
RL Fungal Genet. Biol. 32:121-133(2001).
RN [10]
RP FUNCTION.
RX PubMed=12039755; DOI=10.1128/aem.68.6.2959-2964.2002;
RA McCormick S.P., Alexander N.J.;
RT "Fusarium Tri8 encodes a trichothecene C-3 esterase.";
RL Appl. Environ. Microbiol. 68:2959-2964(2002).
RN [11]
RP FUNCTION.
RX PubMed=12135578; DOI=10.1016/s1087-1845(02)00021-x;
RA Brown D.W., McCormick S.P., Alexander N.J., Proctor R.H., Desjardins A.E.;
RT "Inactivation of a cytochrome P-450 is a determinant of trichothecene
RT diversity in Fusarium species.";
RL Fungal Genet. Biol. 36:224-233(2002).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=12620849; DOI=10.1128/aem.69.3.1607-1613.2003;
RA Meek I.B., Peplow A.W., Ake C. Jr., Phillips T.D., Beremand M.N.;
RT "Tri1 encodes the cytochrome P450 monooxygenase for C-8 hydroxylation
RT during trichothecene biosynthesis in Fusarium sporotrichioides and resides
RT upstream of another new Tri gene.";
RL Appl. Environ. Microbiol. 69:1607-1613(2003).
RN [13]
RP FUNCTION.
RX PubMed=16917519; DOI=10.1139/w06-011;
RA McCormick S.P., Alexander N.J., Proctor R.H.;
RT "Fusarium Tri4 encodes a multifunctional oxygenase required for
RT trichothecene biosynthesis.";
RL Can. J. Microbiol. 52:636-642(2006).
CC -!- FUNCTION: Trichothecene 8-O-acetyltransferase; part of 2-gene cluster
CC involved in trichothecene C-8 modification that mediates the
CC biosynthesis of T2-toxin (PubMed:14532047, PubMed:14690377). The
CC biosynthesis of trichothecenes begins with the cyclization of farnesyl
CC diphosphate to trichodiene and is catalyzed by the trichodiene synthase
CC TRI5 (PubMed:3800398). Trichodiene undergoes a series of oxygenations
CC catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333).
CC TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the
CC C-12, C-13-epoxide to form the intermediate isotrichotriol
CC (PubMed:16917519). Isotrichotriol then undergoes a non-enzymatic
CC isomerization and cyclization to form isotrichodermol (PubMed:2317042).
CC During this process, the oxygen at the C-2 position becomes the pyran
CC ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042).
CC More complex type A trichothecenes are built by modifying
CC isotrichodermol through a series of paired hydroxylation and
CC acetylation or acylation steps (PubMed:11352533). Isotrichodermol is
CC converted to isotrichodermin by the acetyltransferase TRI101
CC (PubMed:10583973). TRI101 encodes a C-3 transacetylase that acts as a
CC self-protection or resistance factor during biosynthesis and that the
CC presence of a free C-3 hydroxyl group is a key component of Fusarium
CC trichothecene phytotoxicity (PubMed:10583973). A second hydroxyl group
CC is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing
CC 15-decalonectrin, which is then acetylated by TRI3, producing
CC calonectrin (PubMed:9435078, PubMed:8593041). A third hydroxyl group is
CC added at C-4 by the cytochrome P450 monooxygenase TRI13, converting
CC calonectrin to 3,15-diacetoxyspirpenol, which is subsequently
CC acetylated bythe acetyltransferase TRI7 (PubMed:12135578,
CC PubMed:11352533). A fourth hydroxyl group is added to C-8 by the
CC cytochrome P450 monooxygenase TRI1, followed by the addition of an
CC isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047). Finally,
CC the acetyl group is removed from the C-3 position by the trichothecene
CC C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755).
CC {ECO:0000269|PubMed:10583973, ECO:0000269|PubMed:11352533,
CC ECO:0000269|PubMed:12039755, ECO:0000269|PubMed:12135578,
CC ECO:0000269|PubMed:12620849, ECO:0000269|PubMed:14532047,
CC ECO:0000269|PubMed:16917519, ECO:0000269|PubMed:2317042,
CC ECO:0000269|PubMed:3800398, ECO:0000269|PubMed:7651333,
CC ECO:0000269|PubMed:8593041, ECO:0000269|PubMed:9435078}.
CC -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC {ECO:0000269|PubMed:14532047}.
CC -!- INDUCTION: Expression is positively regulated by the TRI6 and TRI10
CC core trichothecenes biosynthesis gene cluster transcription factor
CC (PubMed:12620849). {ECO:0000269|PubMed:12620849}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of the three C-8
CC esterified compounds T-2 toxin, 8-propionyl-neosolaniol (P-NEO) and 8-
CC isobutyryl-neosolaniol (B-NEO), and accumulates the C-8-hydroxylated
CC compound neosolaniol (NEO) along with secondary levels of 4,15-
CC diacetoxyscirpenol (DAS) (PubMed:14532047).
CC {ECO:0000269|PubMed:14532047}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
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DR EMBL; AY187275; AAO31979.1; -; Genomic_DNA.
DR EMBL; AY217783; AAO61771.1; -; Genomic_DNA.
DR AlphaFoldDB; Q86Z65; -.
DR SMR; Q86Z65; -.
DR BioCyc; MetaCyc:MON-19569; -.
DR UniPathway; UPA00267; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Acyltransferase; Transferase.
FT CHAIN 1..493
FT /note="Trichothecene 8-O-acetyltransferase"
FT /id="PRO_0000442375"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54586 MW; 57EAD5596215ABC9 CRC64;
MALSRCLRTR TAFLSPLDQL NSSFYIRWSL VLHAKDRDKA VNRLSKGLNA VTSKLPFLKG
RINYHTDTAN NKIASASRAV ISMSDDSPNL SLRELRPAKE LPSLARIKQQ GAPSHLFTDD
LYSLPIFIDT TSKQSHPVLK TTYAPIEGGL ILNICVHHGV MDGQGLATLT DLWASFTRQQ
DQNENEVQQP KNLPDPDEPL TRTARLATAI NATADPEITD IETSLQRYRN DRILEQNIAA
STGDSRKKTS RIFAFSSNKL KDAKEVLANN GCHVTTNSIL NAAVWSNLTR VRLSRRTQLP
PTPFARFTQM VDGRRQLLPK INKPGPYMGN VVLTSSADVS LDTLVATGFF NYLSVSLMAP
VAQAIYDASR KVTTEYIDGF LKTLQKVDDP ASLGIGSMSQ HGVDFISTSV ANAPFYECDF
GPSLSEDSAG GKEGKPVFVR YPYIDWADGN MILLPRRRQP TENDETIEAY IMLAEDDLVA
LAEDPGFCSW LKE
