GSH1_ECOLC
ID GSH1_ECOLC Reviewed; 518 AA.
AC B1IUY6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=EcolC_1019;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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; CP000946; ACA76688.1; -; Genomic_DNA.
DR RefSeq; WP_000611804.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IUY6; -.
DR SMR; B1IUY6; -.
DR KEGG; ecl:EcolC_1019; -.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
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..518
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000082358"
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
