TRI8_FUSSP
ID TRI8_FUSSP Reviewed; 447 AA.
AC Q9C1B9;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Trichothecene C-3 esterase {ECO:0000303|PubMed:12039755};
DE EC=3.1.1.- {ECO:0000269|PubMed:12039755};
DE AltName: Full=Core trichothecene cluster (CTC) protein 8 {ECO:0000303|PubMed:11352533};
DE Flags: Precursor;
GN Name=TRI8 {ECO:0000303|PubMed:11352533};
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, AND DISRUPTION PHENOTYPE.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ren Q., Tag A., Peplow A., Lai H., Kupfer D., Peterson A., Beremand M.,
RA Roe B.;
RT "Fusarium sporotrichioides TRI8 cDNA.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 C-3 esterase; part of the core gene cluster
CC that mediates the biosynthesis of trichothecenes, a very large family
CC of chemically related bicyclic sesquiterpene compounds acting as
CC mycotoxins, including T2-toxin (PubMed:11352533, PubMed:12039755). 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 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: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:12039755}.
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: Does not produce T-2 toxin, but accumulates 4,15-
CC diacetoxyscirpenol, presumably by 3-deacetylation of 3,4,15-
CC diacetoxyscirpenol (PubMed:11352533). {ECO:0000269|PubMed:11352533}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF359360; AAK33077.1; -; Genomic_DNA.
DR EMBL; AY032744; AAK77934.1; -; mRNA.
DR AlphaFoldDB; Q9C1B9; -.
DR SMR; Q9C1B9; -.
DR ESTHER; fussp-TRI8; Fungal-Bact_LIP.
DR UniPathway; UPA00267; -.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005152; Lipase_secreted.
DR PANTHER; PTHR34853; PTHR34853; 1.
DR Pfam; PF03583; LIP; 1.
DR PIRSF; PIRSF029171; Esterase_LipA; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..447
FT /note="Trichothecene C-3 esterase"
FT /id="PRO_5007716291"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 447 AA; 47921 MW; 0F6E2C78FC9D2D0A CRC64;
MALNRLVFSL SLWLGFIGAA QAASSEPLPP SKDPWYTAPP GFESAEPGTV LRVRPAPGNL
TSITANSSAS YNILYRTTDS HFKPTWAVTT LLVPELGPDS LAQQKFQQSA LLSFQVPYDS
ADVDASPSYS MYSASNDSSA PYTAALGSGL FVSVPDYEGP LAAFTAGIIS GYATLDSIRA
VLSLGLGLNI TNSPRAALWG YSGGAFATEW ASELAVQYAP DLVAGPVVGA AMGAPLANIT
TFMHSVNGQA TSGLVPNTLL GLTSQYPDVR KYLVSKLNDD SEYNRTGFLA AEGFTVTESG
VAFAGIDINK YFQNGTDILN DPKILALVNR EGIMGYHGVP KWPLFIYQAI PDEVTPISAT
DALVEKYCAV GADILYERNT VGSHYEETNN SYKAAVQWLE DVFSSQHDIN RAQGCVIQDV
TRNTTSGDLV RRKDVQKSVF DLWSAAW
