GSH1_CITK8
ID GSH1_CITK8 Reviewed; 518 AA.
AC A8ANP6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CKO_04038;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV15109.1; -; Genomic_DNA.
DR RefSeq; WP_012134801.1; NC_009792.1.
DR AlphaFoldDB; A8ANP6; -.
DR SMR; A8ANP6; -.
DR STRING; 290338.CKO_04038; -.
DR EnsemblBacteria; ABV15109; ABV15109; CKO_04038.
DR GeneID; 45137681; -.
DR KEGG; cko:CKO_04038; -.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000008148; 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;
KW Reference proteome.
FT CHAIN 1..518
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025169"
SQ SEQUENCE 518 AA; 58371 MW; FCFD28E181D44E8C CRC64;
MIPDVSQALT WLERHPQALK GIQRGLERET LRVNADGTLA TTGHPDALGS ALTHKWVTTD
FAEALLEFIT PVDGDIQHML TLMRDLHRYT ARNLGDERMW PLSMPCYIAE GQDIELAQYG
TSNIGRLKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVVDGE DAKEKISAGY
FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEK TDCGMYYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP STEYAEIGLE KDGKRLQINS NVLQIENELY
APIRPKRVTR SGETPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCVLA
DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCETAQF PLPKVGKDLF RDLKRVAQTL
DSIHGGEDYQ KVCDELVACF DNPELTFSAR ILRSMIDTGI GGTGKALGEA YRNLLREEPL
EILREEDFIA EREASTRRQL EVEAADTEPF DAWLEKHA
