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Database: UniProt
Entry: C6DA58_PECCP
LinkDB: C6DA58_PECCP
Original site: C6DA58_PECCP 
ID   C6DA58_PECCP            Unreviewed;       208 AA.
AC   C6DA58;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Glutathione S-transferase domain protein {ECO:0000313|EMBL:ACT13814.1};
GN   OrderedLocusNames=PC1_2784 {ECO:0000313|EMBL:ACT13814.1};
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13814.1, ECO:0000313|Proteomes:UP000002736};
RN   [1] {ECO:0000313|EMBL:ACT13814.1, ECO:0000313|Proteomes:UP000002736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1 {ECO:0000313|EMBL:ACT13814.1,
RC   ECO:0000313|Proteomes:UP000002736};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; CP001657; ACT13814.1; -; Genomic_DNA.
DR   RefSeq; WP_015840976.1; NC_012917.1.
DR   AlphaFoldDB; C6DA58; -.
DR   STRING; 561230.PC1_2784; -.
DR   GeneID; 67793329; -.
DR   KEGG; pct:PC1_2784; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_14_4_6; -.
DR   OrthoDB; 9803562at2; -.
DR   Proteomes; UP000002736; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
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; SFLDG01150; Main.1:_Beta-like; 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:ACT13814.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..208
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   208 AA;  23971 MW;  03F6ACFEE31914B7 CRC64;
     MIDLYYAPTP NGHKITLFLE EANIPYQLHR VNISKGEQFR PEFLAISPNN KIPAIVDTQP
     AEGNAPISLF ESGAILLYLA EKHGVLLSSS LRERTATLQW LFWQVAGFGP MLGQNHHFNH
     YAPQPVPYAI ERYQQETQRL YRVLDKHLQD NPWLAGEQYS IADIATYPWV VSYARQRVDL
     DDYPAVKAWY TRISERPATQ RAYQLADQ
//
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