TRI11_FUSSP
ID TRI11_FUSSP Reviewed; 492 AA.
AC O13317; Q7LP66;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Trichothecene C-15 hydroxylase {ECO:0000303|PubMed:9435078};
DE EC=1.-.-.- {ECO:0000269|PubMed:9435078};
DE AltName: Full=Core trichothecene cluster (CTC) protein 11 {ECO:0000303|PubMed:11352533};
DE AltName: Full=Cytochrome P450 monooxygenase TRI11 {ECO:0000303|PubMed:9435078};
GN Name=TRI11 {ECO:0000303|PubMed:9435078};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514;
RN [1]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [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=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=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).
CC -!- FUNCTION: Trichothecene C-15 hydroxylase; 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:9435078). 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC {ECO:0000269|PubMed:9435078}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 isotrichodermin, a
CC trichothecene pathway intermediate (PubMed:9435078).
CC {ECO:0000269|PubMed:9435078}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF011355; AAD12755.1; -; Genomic_DNA.
DR EMBL; AF359360; AAK33070.1; -; Genomic_DNA.
DR AlphaFoldDB; O13317; -.
DR SMR; O13317; -.
DR BioCyc; MetaCyc:MON-19576; -.
DR UniPathway; UPA00267; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Trichothecene C-15 hydroxylase"
FT /id="PRO_0000442367"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 88..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 438
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 492 AA; 55580 MW; 40FBBF4615664D2A CRC64;
MFQYSLWPLL ALSGGTGLAY LVVVVVYNLF FHPLRNFPGP WLNSITQVPH TLLMLCGLPH
KKHLALHMKY GPVVRIGPNM LSFNHPDAMK DVRGHRKSGE PEHGKDPISV QSNGDNIVGS
DRENHTRFRR ALAYGFSAQA MLEQEPTFKA YVNQLFQRLH EQSSGGTKPV DISKWYTFTT
FDMIGDLAFG ESFSCLDNST YHPWVSLAFE SLKSLAFLAE IGRYPRIAPY LGLLVPRGLL
TKFAENKELA SMKVRKRLDT ETDRPDFVGK ITQGLKSKGT SMEFNELASN ASVLIVAGSE
TTATLLSAAV YFLCAHPRTL DLLTKEVRST YTQAHDIDLV STQGLRYMQA VLDEALRMYP
PVAGGGSPRK IAKGGSFVAG HFVPENTLVE NDMWAMHYDP KYFTQPHDFI PERWLGDVRF
ANDRLDAVKP FSIGPRNCIG MNLAYAEMRM MLARTVWEFD IRLSEGSRNW YEESRVYLAW
NKPPLNVYLI PR
