GSH1_VIBCH
ID GSH1_VIBCH Reviewed; 524 AA.
AC Q9KUG5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=VC_0556;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93724.1; -; Genomic_DNA.
DR PIR; E82309; E82309.
DR RefSeq; NP_230207.1; NC_002505.1.
DR RefSeq; WP_000032608.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUG5; -.
DR SMR; Q9KUG5; -.
DR STRING; 243277.VC_0556; -.
DR PRIDE; Q9KUG5; -.
DR DNASU; 2615233; -.
DR EnsemblBacteria; AAF93724; AAF93724; VC_0556.
DR GeneID; 57739279; -.
DR KEGG; vch:VC_0556; -.
DR PATRIC; fig|243277.26.peg.531; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR BioCyc; VCHO:VC0556-MON; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0006750; P:glutathione biosynthetic process; IBA:GO_Central.
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..524
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192541"
SQ SEQUENCE 524 AA; 58961 MW; 1A4B4CEAEAA0D07B CRC64;
MSKFAERLQT VANKPEVFQK FSRGLERESL RYTPEGALTQ TPHPKALGAA LTHRWITTDF
AESLLEFITP VSHEVDTLLA QMSDIHHFAQ TKLGDEKLWP LSMPCYVGSE EGIVLAQYGS
SNTGKMKTLY REGLKRRYGS LMQIISGVHF NFSFPESFWD ALFGEQEESA RQASKSAAYF
GVIRNYYRFG WLIPYLFGAS PALCSSFLQG RKTDLPFESI GKTLYLPYAT SLRLSDLGYT
NSAQSVLQIG FNSIEQYLQG LNEAIRTPSA EFAKLGVKVE GEYRQLNSNV LQIENELYAP
IRPKRVTQSG ERPSQALARA GVEYIEVRSL DVNPFSPIGI NEDQVRFLDL FLAWTALSDS
DPMDGCELAC WRDNWRKVVL EGRKPGLELQ IGCHGEVLTL QAWAKRVFAD LRVIAETMDA
ALGGDAYQAV CAKLETWIEN PELTLSAQIL AEIKQHGGLG KTGCALGNEY RAVNLQHQYQ
FYSQDEMEQE VRRSTQAQAD IEAKETLNFD AYLTQYFAYL QAVS