GSH1_VIBPA
ID GSH1_VIBPA Reviewed; 522 AA.
AC Q87LS2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=VP2539;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC60802.1; -; Genomic_DNA.
DR RefSeq; NP_798918.1; NC_004603.1.
DR RefSeq; WP_005462538.1; NC_004603.1.
DR AlphaFoldDB; Q87LS2; -.
DR SMR; Q87LS2; -.
DR STRING; 223926.28807537; -.
DR EnsemblBacteria; BAC60802; BAC60802; BAC60802.
DR GeneID; 1190054; -.
DR KEGG; vpa:VP2539; -.
DR PATRIC; fig|223926.6.peg.2436; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000002493; Chromosome 1.
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..522
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192543"
SQ SEQUENCE 522 AA; 59086 MW; 159C37B2102CBB2F CRC64;
MTDFAARLKK VASNPEVFKQ FGRGVERETL RYRQDGHLAT TPHPEGLGSA FTNKWITTDF
SESLLEFITP VSHDIPELMA QLKDIHHFTQ TKMGEEKMWP LSMPCYVGSE DDIQLAQYGS
SNSAKMKTLY REGLKRRYGS LMQIISGVHF NFSFPESFWD ALYGEQDEQA RQDTKSAAYF
ALIRNYYRFG WMIPYFFGAS PALCGSFIQG RETKLPFESI GGTLYLPKAT SLRLSDLGYT
NSAQSVLKIG FNSIDQYLEG LGDAIRRPSE EFAKIGVKVD GEYRQLNTNI LQIENELYAP
IRPKRVAKSG EKPSDALSRA GVEYIEVRSL DVNPFSAVGV SEEQVRFLDL FLTWAALSDS
DPMDNCELEC WRDNWNKVII SGREKGLMLQ IGCQGERLSL QDWAKRVFVE LRQIAVEMDS
AAGGDAYQAV CDKLEAWIDN PELTISGQLL ELTKELGGLG KVGCALGMKF REENLAHGYQ
HYSQDIMETE VASSVEKQRK AEESDTLSFD EFLENYFAYL KQ
