ID   A9BMC1_DELAS            Unreviewed;       206 AA.
AC   A9BMC1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Glutathione S-transferase domain {ECO:0000313|EMBL:ABX37466.1};
GN   OrderedLocusNames=Daci_4837 {ECO:0000313|EMBL:ABX37466.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX37466.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX37466.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000884; ABX37466.1; -; Genomic_DNA.
DR   RefSeq; WP_012206636.1; NC_010002.1.
DR   AlphaFoldDB; A9BMC1; -.
DR   STRING; 398578.Daci_4837; -.
DR   GeneID; 24114940; -.
DR   KEGG; dac:Daci_4837; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_1_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW   Transferase {ECO:0000313|EMBL:ABX37466.1}.
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..206
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   206 AA;  22482 MW;  F5650AE92EFE77A9 CRC64;
     MTTLKLYYAP GTCALATRIA LIEANAPHEV IKLDFPKGEQ RSPEYLAINP KGRVPALVTE
     RGVLTETPAL LAYVARRFPE ARLAPLDDAY AFAHMQDFHS YLSSTVHVAH AHGRRAGRWA
     DDEAAIASMQ RKVAANMAEC FGVIERHYLG DAPWVLGADY SVADAYLFTI AGWLEGDGVD
     IAGFPKVQAH FKRMGERAAV RGALGS
//