ID GSH1_ECOUT Reviewed; 518 AA. AC Q1R808; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=Glutamate--cysteine ligase; DE EC=6.3.2.2; DE AltName: Full=Gamma-glutamylcysteine synthetase; DE AltName: Full=Gamma-ECS; DE Short=GCS; GN Name=gshA; OrderedLocusNames=UTI89_C3050; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP + CC phosphate + gamma-L-glutamyl-L-cysteine. CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 1/2. CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 CC family. Type 1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE08506.1; -; Genomic_DNA. DR RefSeq; YP_542037.1; -. DR SMR; Q1R808; 1-515. DR GeneID; 3990585; -. DR GenomeReviews; CP000243_GR; UTI89_C3050. DR KEGG; eci:UTI89_C3050; -. DR HOGENOM; Q1R808; -. DR OMA; Q1R808; EYIEVRA. DR BioCyc; ECOL364106:UTI89_C3050-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:HAMAP. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00578; -; 1. DR InterPro; IPR007370; Glu_cys_ligase. DR InterPro; IPR006334; Glut_cys_ligase. DR Pfam; PF04262; Glu_cys_ligase; 1. DR TIGRFAMs; TIGR01434; glu_cys_ligase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; KW Nucleotide-binding. FT CHAIN 1 518 Glutamate--cysteine ligase. FT /FTId=PRO_1000025171. SQ SEQUENCE 518 AA; 58269 MW; 4E58C447B4D7FF16 CRC64; MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD FAEALLEFIT PVDGDIEHML TFMRDLHRYT ARNMGDERMW PLSMPCYIAE GQDIELAQYG TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGDISGA DAKEKISAGY FRVIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTSLPFEK TECGMYYLPY ATSLRLSDLG YTNKSQSNLG ITFNDLYEYV AGLKQAIKTP SEEYAKIGIE KDGKRLQINS NVLQIENELY APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCALA DAPEMSSSEL ACTRVNWNRV ILEGRKPGLT LGIGCETAQF PLPQVGKDLF RDLKRVAQTL DSINGGEAYQ KVCDELVACF DNPDLTFSAR ILRSMIDTGI GGTGKAFAEA YRNLLREEPL EILREEDFVA EREASERRQQ EMEAADTEPF AVWLEKHA //