TRI4_TRIAR
ID TRI4_TRIAR Reviewed; 517 AA.
AC G0KYB2;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Cytochrome P450 monooxygenase TRI4 {ECO:0000303|PubMed:21642405};
DE EC=1.-.-.- {ECO:0000269|PubMed:21642405};
DE AltName: Full=Trichothecene biosynthesis protein 4 {ECO:0000303|PubMed:21642405};
GN Name=TRI4 {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, AND INDUCTION.
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29623313; DOI=10.1039/c8ob00338f;
RA Izquierdo-Bueno I., Moraga J., Cardoza R.E., Lindo L., Hanson J.R.,
RA Gutierrez S., Collado I.G.;
RT "Relevance of the deletion of the Tatri4 gene in the secondary metabolome
RT of Trichoderma arundinaceum.";
RL Org. Biomol. Chem. 16:2955-2965(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; 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, PubMed:29623313). The
CC biosynthesis of harzianum A begins with the cyclization of farnesyl
CC diphosphate to trichodiene and is catalyzed by the trichodiene synthase
CC TRI5 (PubMed:21642405). Trichodiene undergoes a series of oxygenations
CC catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the
CC addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form
CC the 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:0000269|PubMed:29623313, ECO:0000305|PubMed:21642405,
CC 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 -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor TRI6. {ECO:0000269|PubMed:30121242}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of harzianum A and leads
CC to the production of a larger quantity of the aspinolides B and C, as
CC well as other secondary metabolites including additional aspinolides
CC and their degradation products, gamma-lactones, and hemi-ketals.
CC {ECO:0000269|PubMed:29623313}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; FN394496; CAY87362.1; -; Genomic_DNA.
DR AlphaFoldDB; G0KYB2; -.
DR SMR; G0KYB2; -.
DR BioCyc; MetaCyc:MON-19547; -.
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..517
FT /note="Cytochrome P450 monooxygenase TRI4"
FT /id="PRO_0000445609"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 452
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 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 517 AA; 58029 MW; 679D68607B17D7A2 CRC64;
MLDINALKEI PPATAVGAAV AVGALYFFCQ CFYNLYLHPL RKIPGPKLAA IGPYLEFYHE
VLRDGQYLWE IEKMHQKYGP IVRVNAREVH VKDTSYYNTI YTAGARKTNK DPATVGAFDV
PTATAATVDH DLHRARRGYL NPYFSKRAVA GLEPTIHERI TKLLSRFDQH RKDDQVLSLD
GAFSALTADV ITARFYGEHK DYLDVPDFHF VVRDGFQGLS RVYHLGRFLP SVVGALKGLP
KFLIRIIFPP IAELLTMREE IEAGGIDEFT KSKSSGIKSS VLVGALSDPH IPPQERTVAR
MLDEGTVFLF AGTETTSRTL GITMFYLLSN PDILNKLREE LKSLPPSDDN MHSLGQLENL
PYLTGVVHEG LRLSFGPISR SSRVATHEAL QYKEHTIPAG TPVSQSTYFV HTDTEIFPDP
WEFKPERWIK AAEDGVALKK YITNFSQGSR QCIGYSMSFA EMFLTLSRII PAFDLELYDT
TKADIDMTHA RIVGYPKKVP GKTESLGELR VKVIKKL
