GSH1_YERE8
ID GSH1_YERE8 Reviewed; 519 AA.
AC A1JK14;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=YE0838;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00578}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR EMBL; AM286415; CAL10938.1; -; Genomic_DNA.
DR RefSeq; WP_005167429.1; NC_008800.1.
DR RefSeq; YP_001005176.1; NC_008800.1.
DR AlphaFoldDB; A1JK14; -.
DR SMR; A1JK14; -.
DR STRING; 393305.YE0838; -.
DR EnsemblBacteria; CAL10938; CAL10938; YE0838.
DR KEGG; yen:YE0838; -.
DR PATRIC; fig|393305.7.peg.932; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00578; Glu_cys_ligase; 1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006334; Glut_cys_ligase.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF04262; Glu_cys_ligase; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT CHAIN 1..519
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025193"
SQ SEQUENCE 519 AA; 58444 MW; 942E8889854DE9CF CRC64;
MIPDVSHALT WLEAHPKALK GIRRGIERET LRVTADGQLA STGHPESLGA ALTHQWITTD
FAEALLEFIT PVDGDIDHLL TFLRDIHRYT ARKLGDERMW PLSMPCFIGA EQDIELAKYG
SSNIGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPLEFW QAWAGVTDEK SGKEEISAGY
FRLIRNYYRF GWVIPYLFGA SPAICASFLQ GRETALPFER NDKGMCYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLHTYV AGLKRAIQTP SEEYAALGLK DGDRHLQLNT NVLQIENELY
APIRPKRVTR AGESPSDALL RGGIEYIEVR SLDINPFSPI GVDAVQARFL DLFLIWCVLA
DAPEMSSDEL LCTRKNWNRV ILEGRKPGQT IGMGCNDTRE PLEKVGKDLF TDLRRVAEVL
DGKDSTEYQQ VCDELVASFD DPSLTFSARI LQAMKEGGIG GVGLELAERY REMLQNEPLE
LLTEEQLSEE GAASWVRQRE LELKDKLSFE EYLALHGGQ