TRI3_FUSSP
ID TRI3_FUSSP Reviewed; 519 AA.
AC Q9C1B7;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Trichothecene 15-O-acetyltransferase TRI3 {ECO:0000303|PubMed:8593041};
DE EC=2.3.2.- {ECO:0000269|PubMed:19319932, ECO:0000269|PubMed:8593041};
DE AltName: Full=Core trichothecene cluster (CTC) protein 3 {ECO:0000303|PubMed:8593041};
GN Name=TRI3 {ECO:0000303|PubMed:8593041};
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], DISRUPTION PHENOTYPE, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 24631 / NRRL 3299;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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 [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=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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION.
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 [11]
RP INDUCTION.
RX PubMed=12732543; DOI=10.1128/aem.69.5.2731-2736.2003;
RA Peplow A.W., Tag A.G., Garifullina G.F., Beremand M.N.;
RT "Identification of new genes positively regulated by Tri10 and a regulatory
RT network for trichothecene mycotoxin production.";
RL Appl. Environ. Microbiol. 69:2731-2736(2003).
RN [12]
RP FUNCTION.
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 [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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH 15-DECALONECTRIN,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19319932; DOI=10.1002/pro.80;
RA Garvey G.S., McCormick S.P., Alexander N.J., Rayment I.;
RT "Structural and functional characterization of TRI3 trichothecene 15-O-
RT acetyltransferase from Fusarium sporotrichioides.";
RL Protein Sci. 18:747-761(2009).
CC -!- FUNCTION: 15-O-acetyltransferase; part of the core gene cluster that
CC mediates the biosynthesis of trichothecenes, a very large family of
CC chemically related bicyclic sesquiterpene compounds acting as
CC mycotoxins, including T2-toxin (PubMed:8593041, PubMed:19319932). 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, PubMed:19319932). A third
CC hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase
CC TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is
CC subsequently acetylated by the 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:19319932,
CC ECO:0000269|PubMed:2317042, ECO:0000269|PubMed:3800398,
CC ECO:0000269|PubMed:7651333, ECO:0000269|PubMed:8593041,
CC ECO:0000269|PubMed:9435078}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for 15-decalonectrin {ECO:0000269|PubMed:19319932};
CC -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC {ECO:0000269|PubMed:8593041}.
CC -!- INDUCTION: Expression is positively regulated by the trichothecene
CC cluster-specific transcription activator TRI10 (PubMed:12732543).
CC {ECO:0000269|PubMed:12732543}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of deacetylated
CC calonectrins (PubMed:8593041). {ECO:0000269|PubMed:8593041}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the trichothecene O-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF359360; AAK33072.1; -; Genomic_DNA.
DR PDB; 3FOT; X-ray; 1.75 A; A=1-519.
DR PDB; 3FP0; X-ray; 1.90 A; A=1-519.
DR PDBsum; 3FOT; -.
DR PDBsum; 3FP0; -.
DR AlphaFoldDB; Q9C1B7; -.
DR SMR; Q9C1B7; -.
DR UniPathway; UPA00267; -.
DR EvolutionaryTrace; Q9C1B7; -.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR009992; Tri3/Sat12/Sat16/Mac1.
DR Pfam; PF07428; Tri3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Transferase.
FT CHAIN 1..519
FT /note="Trichothecene 15-O-acetyltransferase TRI3"
FT /id="PRO_0000442371"
FT BINDING 414
FT /ligand="15-deacetylcalonectrin"
FT /ligand_id="ChEBI:CHEBI:157609"
FT /evidence="ECO:0000269|PubMed:19319932,
FT ECO:0007744|PDB:3FP0"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3FOT"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3FOT"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 246..264
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 379..401
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 406..423
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:3FP0"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:3FP0"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:3FOT"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 458..469
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:3FOT"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:3FOT"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:3FOT"
FT HELIX 500..516
FT /evidence="ECO:0007829|PDB:3FOT"
SQ SEQUENCE 519 AA; 58105 MW; 8BAF0BF59BA6C90A CRC64;
MSASSSSALP PLVPALYRWK STGSSGRQVQ RRCVGAEAIV GLEEKNRRAL YDLYIATSLR
NIAPASTLLT LQNLKEMFEL ALLDARFEHP ECACTVSWDD EVPAIITYES PESNESARDW
ARGCIHVQPT AKSALDLWSE MEEGRAAAND NTPSKSIELF LLSDVSTDST PIPQDATVEI
LFHSNHLFWD GIGCRKFVGD LFRLVGSYIG RSDSREMKKI QWGQEIKNLS PPVVDSLKLD
INTLGSEFDD KCTEYTSALV ANYKSRGMKF QPGLALPRCV IHKLSADESI AIVKAVKTRL
GPGFTISHLT QAAIVLALLD HLKPNDLSDD EVFISPTSVD GRRWLREDIA SNFYAMCQTA
AVVRIENLKS IAVSHKDEKE LQVRALESAC RNIKKSYRQW LENPFLQALG LRVHNFEASY
LHAKPIPFEG EANPLFISDG INERFIPHEI KQTATGENVL SVESIDFVVN QSLPYLAIRL
DSWRDASTLN IIYNDANYTE AEVQKYLQSI VEFMLAFRL
