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Database: UniProt/TrEMBL
Entry: F0B9L4_9XANT
LinkDB: F0B9L4_9XANT
Original site: F0B9L4_9XANT 
ID   F0B9L4_9XANT            Unreviewed;       229 AA.
AC   F0B9L4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:EGD10975.1};
GN   ORFNames=XVE_0768 {ECO:0000313|EMBL:EGD10975.1};
OS   Xanthomonas vesicatoria ATCC 35937.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD10975.1, ECO:0000313|Proteomes:UP000003299};
RN   [1] {ECO:0000313|EMBL:EGD10975.1, ECO:0000313|Proteomes:UP000003299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD10975.1,
RC   ECO:0000313|Proteomes:UP000003299};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGD10975.1}.
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DR   EMBL; AEQV01000016; EGD10975.1; -; Genomic_DNA.
DR   RefSeq; WP_005989397.1; NZ_CP018725.1.
DR   AlphaFoldDB; F0B9L4; -.
DR   GeneID; 46981896; -.
DR   KEGG; xve:BJD12_10950; -.
DR   eggNOG; COG0625; Bacteria.
DR   Proteomes; UP000003299; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03048; GST_N_Ure2p_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR44051:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:EGD10975.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..212
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          209..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  25670 MW;  90EB15E7BE54ABF0 CRC64;
     MIDLYYWPTP NGHKVTLFLE EAGLDYTLKP VNIGKGEQFE PAFLQISPNN KMPAIVDHTP
     ADGGAPQAVF ESGAILLYLA EKTGRFLPRD ARGRIAALEW LFWQMGGLGP MTGQMGHFNV
     YAPEKILYAI DRYNAEVRRL HGVLDKRLAD HAFLAGDDYG IADMASYPWL EVYGDLKPDF
     AAFPNLQRWH AAIAARPATQ RAYALKEKVN PDAGKPLSDE ERKHLFGKR
//
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