TRI11_TRIAR
ID TRI11_TRIAR Reviewed; 499 AA.
AC G0KYA9;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Trichothecene C-4 hydroxylase {ECO:0000303|PubMed:21642405};
DE EC=1.-.-.- {ECO:0000269|PubMed:21642405};
DE AltName: Full=Cytochrome P450 monooxygenase TRI11 {ECO:0000303|PubMed:21642405};
DE AltName: Full=Trichothecene biosynthesis protein 11 {ECO:0000303|PubMed:21642405};
GN Name=TRI11 {ECO:0000303|PubMed:21642405};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC STRAIN=IBT 40837;
RX PubMed=21642405; DOI=10.1128/aem.00595-11;
RA Cardoza R.E., Malmierca M.G., Hermosa M.R., Alexander N.J., McCormick S.P.,
RA Proctor R.H., Tijerino A.M., Rumbero A., Monte E., Gutierrez S.;
RT "Identification of loci and functional characterization of trichothecene
RT biosynthesis genes in filamentous fungi of the genus Trichoderma.";
RL Appl. Environ. Microbiol. 77:4867-4877(2011).
RN [2]
RP FUNCTION.
RX PubMed=30121242; DOI=10.1016/j.fgb.2018.08.002;
RA Lindo L., McCormick S.P., Cardoza R.E., Brown D.W., Kim H.S.,
RA Alexander N.J., Proctor R.H., Gutierrez S.;
RT "Effect of deletion of a trichothecene toxin regulatory gene on the
RT secondary metabolism transcriptome of the saprotrophic fungus Trichoderma
RT arundinaceum.";
RL Fungal Genet. Biol. 119:29-46(2018).
CC -!- FUNCTION: Trichothecene C-4 hydroxylase; part of the gene cluster that
CC mediates the production of the antimicrobial trichothecene harzianum A
CC (HA) that plays a role in Botrytis cinerea antagonistic activity and
CC plant defense priming (PubMed:21642405). The biosynthesis of harzianum
CC A begins with the cyclization of farnesyl diphosphate to trichodiene
CC and is catalyzed by the trichodiene synthase TRI5 (PubMed:21642405).
CC Trichodiene undergoes a series of oxygenations catalyzed by the
CC cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3
CC oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the
CC intermediate isotrichodiol (PubMed:21642405). Isotrichodiol then
CC undergoes a non-enzymatic isomerization and cyclization to form 12,13-
CC epoxytrichothec-9-ene (EPT) which is further converted to trichodermol
CC by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation
CC (PubMed:21642405). The last step of HA synthesis is esterification of
CC an octatriendioyl moiety to the C-4 oxygen of trichodermol. The
CC octatriendioyl moiety is probably produced by the polyketide synthase
CC TRI17 and the esterification performed by the trichothecene O-
CC acetyltransferase TRI3 (Probable). {ECO:0000269|PubMed:21642405,
CC ECO:0000305|PubMed:21642405, ECO:0000305|PubMed:30121242}.
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:21642405}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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; FN394493; CAY87359.1; -; Genomic_DNA.
DR AlphaFoldDB; G0KYA9; -.
DR SMR; G0KYA9; -.
DR BioCyc; MetaCyc:MON-19548; -.
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 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="Trichothecene C-4 hydroxylase"
FT /id="PRO_0000445613"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 499 AA; 57322 MW; 4E38C324CE574EF7 CRC64;
MANAISVGVA VQLVLTVLLA SIPLRVIWNL FFHPLSYIPG PRLWIAFPIF RQIASIRGVF
DAQMCEYHRK YGNAVRFSPN EVSFITEQAW RDIYDHRPNQ LERFILSTTR RPDIFDANEI
DHARYRKAML PAFSPKGLQE QEPIVRGYID TFIERLREVS ATGESTDMVK WYNFTTFDII
GDLAFGESFG GLRNREYHFT ISFTFEAFKL LSYLEAGAAY PLLLKILMAF TPQSLIEARD
KKEEHAETTV RKRLDNRALH GRGDFMDYLL RNRGEKQGLN DKELVANAST LITAGSETTA
TILSGITYWL LQTPNVLQKV TEEVRSAFQS EADITFTSAT SQLPYMLACF QEAFRHYPPV
PTGMPRVTPS HGITKISGYD ISPNTKVSVH QLAAYSHPDN FHRPREFVPE RWLPDAKTNP
SSPWYNDRRE TVQPFNVGPR NCVGRNLAEQ EIRVMLARVL WNFDLELAPE SKNWTDQKTH
FLWEKGALMC KLHDRFASK
