ID G8PVG2_PSEUV Unreviewed; 288 AA.
AC G8PVG2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Glutathione S-transferase YghU {ECO:0000313|EMBL:AEV39750.1};
GN OrderedLocusNames=PSE_p0168 {ECO:0000313|EMBL:AEV39750.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OG Plasmid FO-BEG1 {ECO:0000313|Proteomes:UP000005634}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39750.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV39750.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39750.1,
RC ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU003494}.
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DR EMBL; CP003148; AEV39750.1; -; Genomic_DNA.
DR RefSeq; WP_014290282.1; NC_016646.1.
DR AlphaFoldDB; G8PVG2; -.
DR KEGG; psf:PSE_p0168; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_14_4_5; -.
DR Proteomes; UP000005634; Plasmid FO-BEG1.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd10292; GST_C_YghU_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; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; 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 Plasmid {ECO:0000313|EMBL:AEV39750.1};
KW Transferase {ECO:0000313|EMBL:AEV39750.1}.
FT DOMAIN 47..134
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 137..273
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 258..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32376 MW; 21E395DD8C228D0F CRC64;
MSDKQEYTPP KVWKWEQKNG GQFANINRPI AGPTHDKDLQ VGKHPLQLYS LATPNGVKVT
IMLEELLAAG FSEAEYDAWL INIGEGDQFS SGFVGANPNS KIPALVDHST DTPTRVFESG
SILLYLAEKF GAFLPKDPAA RTEAMNWLFW QMGSAPYLGG GFGHFYAYAP EKFEYPINRF
AMEAKRQLDV LDRNLAERRF MAGDEYSIAD MAIFPWYGAL VLGSLYSAAE FLSVDEYKNV
KRWAEEIAER PAVKRGKRVN RTWGDEDQQV PERHDASDLD PKPASEKA
//
