GSH1_EDWI9
ID GSH1_EDWI9 Reviewed; 519 AA.
AC C5BGG7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=NT01EI_3229;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR70373.1; -; Genomic_DNA.
DR RefSeq; WP_015872457.1; NC_012779.2.
DR AlphaFoldDB; C5BGG7; -.
DR SMR; C5BGG7; -.
DR STRING; 67780.B6E78_07780; -.
DR PRIDE; C5BGG7; -.
DR EnsemblBacteria; ACR70373; ACR70373; NT01EI_3229.
DR GeneID; 7961065; -.
DR KEGG; eic:NT01EI_3229; -.
DR PATRIC; fig|634503.3.peg.2879; -.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000001485; 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..519
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000212104"
SQ SEQUENCE 519 AA; 57761 MW; A730B3838D216323 CRC64;
MIPDVSQALS WLESHPNALD GIRRGIERET LRVTPEGHLA TTPHPAVLGK ALTHPWITTD
FAESLLEFIT PVDGSIDHML TFLSDIHRYV ARNLGDERMW PLSMPCFIGS EQDIILAQYG
SSNLGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPLSFW QARAGVQDAD SGKAAISDGY
FRLIRNYYRF GWVIPYLFGA SPAICSSFLN GRESALPFER RGGTLFLPYA TSLRLSDLGY
TNKSQSNLGI TFNHLNQYVE GLKRAIHTPS AEFARLGVEE SGHYHQLNAN ILQIENELYA
PIRPKRVTRD GESPSDALLR GGVEYIEVRS LDINPFTPIG VDADQARFLD LFLIWCVLAD
APEMSSDELL CTRQNWNRVI LEGRKPGQTI GIGCHDARQP LAYVGQSLFA DLHRVAEVLD
GINGDARYQQ VCARLVAAFE DVSLTYSARV VAQMGERGIG GYGLTLAQHY RDRLCSEPLA
LLDETTLAVQ AQRSVTRQAA LESQSCESFA SYLRQHAGG
