GenomeNet

Database: UniProt
Entry: Q1R6M8_ECOUT
LinkDB: Q1R6M8_ECOUT
Original site: Q1R6M8_ECOUT 
ID   Q1R6M8_ECOUT            Unreviewed;       328 AA.
AC   Q1R6M8;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Putative transferase {ECO:0000313|EMBL:ABE08986.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:ABE08986.1};
GN   Name=yqjG {ECO:0000313|EMBL:ABE08986.1};
GN   OrderedLocusNames=UTI89_C3540 {ECO:0000313|EMBL:ABE08986.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE08986.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE08986.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000243; ABE08986.1; -; Genomic_DNA.
DR   RefSeq; WP_000531180.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1R6M8; -.
DR   KEGG; eci:UTI89_C3540; -.
DR   HOGENOM; CLU_037263_0_1_6; -.
DR   OMA; PWANRAI; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03190; GST_C_Omega_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; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR32419:SF6; GLUTATHIONE S-TRANSFERASE OMEGA-LIKE 1-RELATED; 1.
DR   PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SFLD; SFLDG01148; Xi_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:ABE08986.1}.
FT   DOMAIN          172..296
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   ACT_SITE        63
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        195
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   328 AA;  37389 MW;  F42F1ABB74AB9A36 CRC64;
     MGQLIDGVWH DTWYDTKSTG GKFQRSASAF RNWLTADGAP GPTGKGGFAA EKDRYHLYVS
     LACPWAHRTL IMRKLKGLEP FISVSVVNPL MLENGWTFDD SFPGATGDTL YQHEFLYQLY
     LHADPHYSGR VTVPVLWDKK NHTIVSNESA EIIRMFNTAF DALGAKAGDY YPPALQPKID
     ELNGWIYDTV NNGVYKAGFA TSQQAYDEAV AKVFESLARL EQILGQHRYL TGNQLTEADI
     RLWTTLVRFD PVYVTHFKCD KHRISDYLNL YGFLRDIYQM PGIAETVNFD HIRNHYFRSH
     KTINPTGIIS IGPWQDLDEP HGRDVRFG
//
DBGET integrated database retrieval system