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SIRG_LEPMC
ID   SIRG_LEPMC              Reviewed;         234 AA.
AC   Q6Q882;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Glutathione S-transferase sirG {ECO:0000303|PubMed:15387811};
DE            EC=2.5.1.18 {ECO:0000305|PubMed:15387811};
DE   AltName: Full=Sirodesmin biosynthesis protein G {ECO:0000303|PubMed:15387811};
GN   Name=sirG {ECO:0000303|PubMed:15387811};
OS   Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=5022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=15387811; DOI=10.1111/j.1365-2958.2004.04215.x;
RA   Gardiner D.M., Cozijnsen A.J., Wilson L.M., Pedras M.S., Howlett B.J.;
RT   "The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus
RT   Leptosphaeria maculans.";
RL   Mol. Microbiol. 53:1307-1318(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=18272357; DOI=10.1016/j.mycres.2007.08.017;
RA   Fox E.M., Howlett B.J.;
RT   "Biosynthetic gene clusters for epipolythiodioxopiperazines in filamentous
RT   fungi.";
RL   Mycol. Res. 112:162-169(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=19762440; DOI=10.1099/mic.0.033886-0;
RA   Kremer A., Li S.M.;
RT   "A tyrosine O-prenyltransferase catalyses the first pathway-specific step
RT   in the biosynthesis of sirodesmin PL.";
RL   Microbiology 156:278-286(2010).
RN   [4]
RP   FUNCTION.
RX   PubMed=21038099; DOI=10.1007/s00253-010-2956-x;
RA   Zou H.X., Xie X., Zheng X.D., Li S.M.;
RT   "The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-
RT   prenylations.";
RL   Appl. Microbiol. Biotechnol. 89:1443-1451(2011).
RN   [5]
RP   FUNCTION.
RX   PubMed=24083562; DOI=10.1021/cb400691z;
RA   Rudolf J.D., Poulter C.D.;
RT   "Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on
RT   tyrosine and tryptophan derivatives.";
RL   ACS Chem. Biol. 8:2707-2714(2013).
RN   [6]
RP   FUNCTION.
RX   PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA   Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT   "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT   dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT   unknown clapurines.";
RL   PLoS ONE 11:E0158945-E0158945(2016).
CC   -!- FUNCTION: Glutathione S-transferase; part of the gene cluster that
CC       mediates the biosynthesis of sirodesmin PL, an
CC       epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged
CC       cyclic dipeptide and that acts as a phytotoxin which is involved in the
CC       blackleg didease of canola (PubMed:15387811, PubMed:18272357,
CC       PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-
CC       Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-
CC       dimethylallyl-L-Tyr, and therefore represents probably the first
CC       pathway-specific enzyme in the biosynthesis of sirodesmin PL
CC       (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-
CC       L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed
CC       by the non-ribosomal peptide synthase sirP to form the diketopiperazine
CC       (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP
CC       performed by the cytochrome P450 monooxygenase sirC leads to the
CC       production of the intermediate phomamide (PubMed:27390873). This step
CC       is essential to form the reactive thiol group required for toxicity of
CC       sirodesmin PL (PubMed:27390873). The next steps of sirodesmin
CC       biosynthesis are not well understood yet, but some predictions could be
CC       made from intermediate compounds identification (PubMed:18272357).
CC       Phomamide is converted into phomalizarine via oxidation, probably by
CC       sirT (PubMed:18272357). Further oxidation, methylation (by sirM or
CC       sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin
CC       (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates
CC       deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).
CC       {ECO:0000269|PubMed:19762440, ECO:0000269|PubMed:21038099,
CC       ECO:0000269|PubMed:24083562, ECO:0000269|PubMed:27390873,
CC       ECO:0000305|PubMed:15387811, ECO:0000305|PubMed:18272357}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000305|PubMed:15387811};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}.
CC   -!- INDUCTION: Expression is co-regulated with the other genes from the
CC       sirodesmin cluster and corresponds with sirodesmin production
CC       (PubMed:15387811). {ECO:0000269|PubMed:15387811}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AY553235; AAS92546.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Q882; -.
DR   SMR; Q6Q882; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Transferase; Virulence.
FT   CHAIN           1..234
FT                   /note="Glutathione S-transferase sirG"
FT                   /id="PRO_0000437725"
FT   DOMAIN          15..99
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          105..230
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   234 AA;  26775 MW;  A7AE8D3838E32C98 CRC64;
     MTERPKDIPE DKLVLYVVKA TPTSTANTVK PLIVMNELSI DHEIYVVPSP TRDEWFHQIN
     PHKMVPAIES AETRDGKRLN IWESTSCLTY LTDAYDHEGL WKGSDLWERT QVNNWLTLHT
     AALGATGKYW LYFSAIHPEK IPAVIEKLAN NIKVQYDILE RRLSEKGQKY IALPDRPTIA
     DVANLPFVTE ELALKAGLRL GDWPNLQAWS EKMLARPSVQ KALSQKFRPS VMIR
 
 
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