GSH1_ALISL
ID GSH1_ALISL Reviewed; 521 AA.
AC B6EGB3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=VSAL_I0643;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ78328.1; -; Genomic_DNA.
DR RefSeq; WP_012549450.1; NC_011312.1.
DR AlphaFoldDB; B6EGB3; -.
DR SMR; B6EGB3; -.
DR STRING; 316275.VSAL_I0643; -.
DR PRIDE; B6EGB3; -.
DR EnsemblBacteria; CAQ78328; CAQ78328; VSAL_I0643.
DR KEGG; vsa:VSAL_I0643; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000001730; 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.
FT CHAIN 1..521
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000129585"
SQ SEQUENCE 521 AA; 59104 MW; A07B87E642269471 CRC64;
MTEFTNRLQK VASNPKAFKN TGRGIERETL RFTLDAALSS KPHPAGVGSA LTHKYITTDF
AESLLEFITP VSHDVKTVLK QLEDVHHYTV SHMGEEKLWP LSMPCFVSKD DDITLAQYGK
SNVGQLKTTY REGLKRRYGS VMQVISGVHF NFSFSNEFWD ELLGEQTEKD RQDSVSDAYF
GLIRNYYRFG WLIPYFFGAS PALCGSFIQG RETTMNFESL GKTLYLPYAT SLRLSDLGYT
NDAQSDLKIS LNSIDEYIEG LNKAIRTPSE EFAKIGLKEG DKHIQLNANV LQIENELYAP
IRPKRVAKSG EKPSEALERS GIEYIEVRSL DVNPFSPIGV DEDQVRFLDL FLTWSVLTDS
APMDDSEMAC WKDNWNKIVE LGRKPGLELQ IGCQGERLTQ KAWAERVFDD LFTIAKKMDA
VNGDDAYQQT HQRLSAMIEN PELTISGRLL AETKKAGGIG IIGCKLAIQH RQAHLDHKYS
FYTKDELDAE VERSVLAQKE IEASDTMPFS EYLDDYFNYL K
