ID A0A0Q8EME2_9GAMM Unreviewed; 238 AA.
AC A0A0Q8EME2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KRA41591.1};
GN ORFNames=ASD72_16115 {ECO:0000313|EMBL:KRA41591.1};
OS Pseudoxanthomonas sp. Root630.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736574 {ECO:0000313|EMBL:KRA41591.1, ECO:0000313|Proteomes:UP000051081};
RN [1] {ECO:0000313|EMBL:KRA41591.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA41591.1,
RC ECO:0000313|Proteomes:UP000051081};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA41591.1, ECO:0000313|Proteomes:UP000051081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root630 {ECO:0000313|EMBL:KRA41591.1,
RC ECO:0000313|Proteomes:UP000051081};
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:KRA41591.1}.
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DR EMBL; LMGY01000020; KRA41591.1; -; Genomic_DNA.
DR RefSeq; WP_056881613.1; NZ_LMGY01000020.1.
DR AlphaFoldDB; A0A0Q8EME2; -.
DR STRING; 1736574.ASD72_16115; -.
DR OrthoDB; 9803562at2; -.
DR Proteomes; UP000051081; 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; 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; SFLDG01151; Main.2:_Nu-like; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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:KRA41591.1}.
FT DOMAIN 1..92
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 95..217
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 215..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 26487 MW; 90F1E820B32F7C49 CRC64;
MIDLYYWPTP NGHKITLMLE ELAEAGAKLD YRIVPVDIGK GDQFKPEYLA FSPNNKMPAI
IDHAPADGGE PISVFESGAI LLYLANKAGR FFGADTRQKV AVNQWLMWQM GGLGPMTGQY
GHFTVYAPEK IPYAIDRYTR EVQRLLGVLD KQLERSAFIA GADYSIADMA THPWINAYDK
APLDLTPYPA LQRWHAEIAA RPAVQRAYAL KSQVNPNAGQ PLSDEERKHL FGQGAPKA
//