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Database: UniProt
Entry: Q88UW5
LinkDB: Q88UW5
Original site: Q88UW5 
ID   GSHAB_LACPL             Reviewed;         751 AA.
AC   Q88UW5; F9UQP1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 85.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB;
DE   AltName: Full=Gamma-GCS-GS;
DE            Short=GCS-GS;
DE   Includes:
DE     RecName: Full=Glutamate--cysteine ligase;
DE              EC=6.3.2.2;
DE     AltName: Full=Gamma-ECS;
DE              Short=GCS;
DE     AltName: Full=Gamma-glutamylcysteine synthetase;
DE   Includes:
DE     RecName: Full=Glutathione synthetase;
DE              EC=6.3.2.3;
DE     AltName: Full=GSH synthetase;
DE              Short=GS;
DE              Short=GSH-S;
DE              Short=GSHase;
DE     AltName: Full=Glutathione synthase;
GN   Name=gshAB; Synonyms=gshF; OrderedLocusNames=lp_2336;
OS   Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA   Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA   Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA   Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA   De Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/JB.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
CC       via gamma-L-glutamyl-L-cysteine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
CC         glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.3;
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 2/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC       cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000305}.
DR   EMBL; AL935263; CCC79530.1; -; Genomic_DNA.
DR   RefSeq; WP_011101718.1; NC_004567.2.
DR   RefSeq; YP_004890044.1; NC_004567.2.
DR   ProteinModelPortal; Q88UW5; -.
DR   SMR; Q88UW5; -.
DR   STRING; 220668.lp_2336; -.
DR   EnsemblBacteria; CCC79530; CCC79530; lp_2336.
DR   GeneID; 1062357; -.
DR   KEGG; lpl:lp_2336; -.
DR   PATRIC; fig|220668.9.peg.1975; -.
DR   eggNOG; ENOG4105D9M; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   eggNOG; COG2918; LUCA.
DR   HOGENOM; HOG000112828; -.
DR   KO; K01919; -.
DR   OMA; EANFNPM; -.
DR   BioCyc; LPLA220668:G1GW0-2014-MONOMER; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_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; 2.
DR   Pfam; PF04262; Glu_cys_ligase; 2.
DR   SUPFAM; SSF55931; SSF55931; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    751       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192552.
FT   REGION        1    336       Glutamate--cysteine ligase.
SQ   SEQUENCE   751 AA;  83018 MW;  605A494E7A7DCBF7 CRC64;
     MELDAVGKAI VQYHLVPLVH QANLGLEVTM HRVDAHGHLA TTAHPQAFGS AQQNHQLRPG
     FSASALKFTT PVRRDIPALM AYLKGLNTAA RRSLDADERL WPLSSTPVLP DDLTNVPLAD
     VDQVSYQRRR DLARKYELQR LMTTGSHVNM SLNEALFTRL YTETFHQQYH SYVDFRNAIY
     LKVAQGLVRM NWLIQYLFGA SPRLAVTDTT SRPQRSSVQH PDGRYSQVTG DYTSIDRYVA
     KLTAAVRQQQ LLSVNDFDGP VRLRSNGQLA MMARQGVYYL EYRGLDLDPT SPVGVDANAV
     AFVRLLASYF VMMPALPAKM VSQVNAQADQ LTRQVLGENP TTASAQAVPA VQVLDALADF
     VKTYGLPNED AVLLKQLKSW VTDPKKTLSA QIAMQADPLA WALERAARYQ ESSNERPFEL
     AGFTALDLSS QQLAQQALTR GVQVDVVDPH ANILRLTKLG RSQLVVNGSG TDLNPQALTT
     VLTHKAAAKQ ILAEHGVPVP ASQTYHTANQ LIADYDRYVQ AGGIVLKAAD ESHKVIVFRI
     MPERGLFEQV VRQLFEQTSA VMAEEVVVAS SYRFLVIDSR VQAIVERIPA NIVGDGRSTV
     KTLLDRKNGR ALRGTAFKWP QSALQLGTIE RYRLDSYHLT LDSVVSRGTQ ILLREDATFG
     NGADVLDATA DMHQSYVQAV EKLVADLHLA VAGVDVMIPN LYAELVPEHP EMAVYLGIHA
     APYLYPHLFP MFGTAQPVAG QLLDALFKNE D
//
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