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Database: UniProt
Entry: A0A0T0PSJ5_9SPHN
LinkDB: A0A0T0PSJ5_9SPHN
Original site: A0A0T0PSJ5_9SPHN 
ID   A0A0T0PSJ5_9SPHN        Unreviewed;       229 AA.
AC   A0A0T0PSJ5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KQT31856.1};
GN   ORFNames=ASG29_08140 {ECO:0000313|EMBL:KQT31856.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT31856.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT31856.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT31856.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT31856.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT31856.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT31856.1}.
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DR   EMBL; LMQP01000003; KQT31856.1; -; Genomic_DNA.
DR   RefSeq; WP_055982724.1; NZ_LMQP01000003.1.
DR   AlphaFoldDB; A0A0T0PSJ5; -.
DR   STRING; 1736370.ASG29_08140; -.
DR   OrthoDB; 9803562at2; -.
DR   Proteomes; UP000051178; Unassembled WGS sequence.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW   Transferase {ECO:0000313|EMBL:KQT31856.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..213
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   229 AA;  25105 MW;  7610B757E2EBADEB CRC64;
     MIDLYFAATP NGWKATIALE ELGLPYVVRP VNIGAGEQFA ADFLAIAPNN RIPAIVDHDP
     ADGGGPLSVF ESGAILLYLA QKAGRLMPRD VRGRTAVTEW VMWQMGGLGP MLGQNGHFRL
     YAPDRIPYAM DRYAKEADRL YGVLDRQLAR TGAHVAGADY SIADIACFPW IITHKAQGID
     MTRFPHVARW FATVRARPAV AAGTAVGRMS RPEEISDEAK RVMMGIERP
//
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