TR101_FUSSP
ID TR101_FUSSP Reviewed; 459 AA.
AC O94197;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Trichothecene 3-O-acetyltransferase TRI101 {ECO:0000303|PubMed:10583973};
DE EC=2.3.1.- {ECO:0000305|PubMed:10583973};
DE AltName: Full=Trichothecene biosynthesis protein 101 {ECO:0000303|PubMed:10583973};
GN Name=TRI101 {ECO:0000303|PubMed:10583973};
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [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=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 (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM AND COENZYME
RP A, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17923480; DOI=10.1074/jbc.m705752200;
RA Garvey G.S., McCormick S.P., Rayment I.;
RT "Structural and functional characterization of the TRI101 trichothecene 3-
RT O-acetyltransferase from Fusarium sporotrichioides and Fusarium
RT graminearum: kinetic insights to combating Fusarium head blight.";
RL J. Biol. Chem. 283:1660-1669(2008).
CC -!- FUNCTION: 3-O-acetyltransferase involved in the biosynthesis of
CC trichothecenes, a very large family of chemically related bicyclic
CC sesquiterpene compounds acting as mycotoxins, including T2-toxin
CC (PubMed:11352533, PubMed:17923480). The biosynthesis of trichothecenes
CC begins with the cyclization of farnesyl diphosphate to trichodiene and
CC is catalyzed by the trichodiene synthase TRI5 (PubMed:10583973,
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.1 uM for isotrichodermol {ECO:0000269|PubMed:17923480};
CC KM=15.8 uM for T2-toxin {ECO:0000269|PubMed:17923480};
CC KM=1463 uM for deoxynivalenol (DON) {ECO:0000269|PubMed:17923480};
CC KM=350 uM for nivalenol (NIV) {ECO:0000269|PubMed:17923480};
CC -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC {ECO:0000269|PubMed:10583973}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of T-2 toxin and
CC accumulates isotrichodermol and small amounts of 3,15-didecalonectrin
CC and 3-decalonectrin (PubMed:10583973). {ECO:0000269|PubMed:10583973}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the trichothecene 3-O-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF127176; AAD19745.1; -; Genomic_DNA.
DR PDB; 2ZBA; X-ray; 2.00 A; A/B/C/D=1-459.
DR PDBsum; 2ZBA; -.
DR AlphaFoldDB; O94197; -.
DR SMR; O94197; -.
DR BioCyc; MetaCyc:MON-19578; -.
DR UniPathway; UPA00267; -.
DR EvolutionaryTrace; O94197; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Transferase.
FT CHAIN 1..459
FT /note="Trichothecene 3-O-acetyltransferase TRI101"
FT /id="PRO_0000442376"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 253
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 266..269
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007744|PDB:2ZBA"
FT BINDING 302
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 318
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 343
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 386
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 390
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17923480,
FT ECO:0007744|PDB:2ZBA"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:2ZBA"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:2ZBA"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 269..285
FT /evidence="ECO:0007829|PDB:2ZBA"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:2ZBA"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:2ZBA"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:2ZBA"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:2ZBA"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:2ZBA"
SQ SEQUENCE 459 AA; 50336 MW; 303D8DA611563C92 CRC64;
MAATSSTSSQ SFDIELDIIG QQPPLLSIYT QISLVYPVSD PSQYPTIVST LEEGLKRLSQ
TFPWVAGQVK TEGISEGNTG TSKIIPYEET PRLVVKDLRD DSSAPTIEGL RKAGFPLEMF
DENVVAPRKT LAIGPGNGPN DPKPVLLLQL NFIKGGLILT VNGQHGAMDM TGQDAIIRLL
SKACRNESFT EEEISAMNLD RKTVVPLLEN YKVGPELDHQ IAKPAPAGDA PPAPAKATWA
FFSFTPKALS ELKDAATKTL DASSKFVSTD DALSAFIWQS TSRVRLARLD ASTPTEFCRA
VDMRGPMGVS STYPGLLQNM TYHDSTVAEI ANEPLGATAS RLRSELNSDR LRRRTQALAT
YMHGLPDKSS VSLTADANPS SSIMLSSWAK VGCWEYDFGF GLGKPESVRR PRFEPFESLM
YFMPKKPDGE FTASISLRDE DMERLKADEE WTKYAKYIG
