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TRI4_FUSSP
ID   TRI4_FUSSP              Reviewed;         520 AA.
AC   Q12612; Q9C1B6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytochrome P450 monooxygenase TRI4 {ECO:0000303|PubMed:7651333};
DE            EC=1.-.-.- {ECO:0000269|PubMed:16917519};
DE   AltName: Full=Core trichothecene cluster (CTC) protein 4 {ECO:0000303|PubMed:7651333};
GN   Name=TRI4 {ECO:0000303|PubMed:7651333};
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=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   [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=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   [6]
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   [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, AND CATALYTIC ACTIVITY.
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   FUNCTION.
RX   PubMed=19319932; DOI=10.1002/pro.80;
RA   Garvey G.S., McCormick S.P., Alexander N.J., Rayment I.;
RT   "Structural and functional characterization of TRI3 trichothecene 15-O-
RT   acetyltransferase from Fusarium sporotrichioides.";
RL   Protein Sci. 18:747-761(2009).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; 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:16917519). 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:7651333}.
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: Results in the loss of production of both
CC       trichothecenes and apotrichodiol and the accumulation of the
CC       unoxygenated pathway intermediate trichodiene (PubMed:7651333).
CC       {ECO:0000269|PubMed:7651333}.
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; U22462; AAB72032.1; -; Genomic_DNA.
DR   EMBL; AF359360; AAK33073.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12612; -.
DR   SMR; Q12612; -.
DR   BioCyc; MetaCyc:MON-19573; -.
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..520
FT                   /note="Cytochrome P450 monooxygenase TRI4"
FT                   /id="PRO_0000442366"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         455
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        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        378
FT                   /note="F -> C (in Ref. 1; AAB72032)"
SQ   SEQUENCE   520 AA;  59118 MW;  D8A8716B14E18E64 CRC64;
     MVDQDWIKAL VNIPISHAVG VVAASTVIYF LSSCFYNLYL HPLRKIPGPK LAAIGPYLEF
     YHEVIRDGQY LWEIAKMHDK YGPIVRVNDK EVHIRDPSYY STIYTAGARK TNKDPATVGA
     FDVPTATAAT VDHDHHRARR GYLNPYFSKR SITNLEPFIH ERVTKLLSRF QEHLDNDQVL
     SLDGAFCALT ADVITSRFYG KHYNYLDLPD FHFVVRDGFL GLTKVYHLAR FIPVLVTVLK
     RLPYSCLRLI APSVSDLLQM RNEIHERGGD EFLSSKTSEA KSSILFGALA DTHIPPVERT
     VERMLDEGTV ILFAGTETTS RTLAITFFYL LTHPECLRKL REELNSLPKV EGDRFPLATL
     ENLPYLNGVV HEGFRLAFGP ISRSGRVATQ ENLKYKEHVI PAGTPVSQST YFMHTDPKIF
     PEPEKFKPER WIEAAEKKIP LKKYITNFSQ GSRQCIGYTM AFAEMYLAMS RIARAYDVEL
     YDTTKADIDM THARIVAYPK AIPGKTEHVG EIRVKVLKAL
 
 
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