GSHAB_LACPL
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 03-AUG-2022, entry version 97.
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 Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
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., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA 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 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 via
CC gamma-L-glutamyl-L-cysteine. {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = 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 from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC 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}.
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DR EMBL; AL935263; CCC79530.1; -; Genomic_DNA.
DR RefSeq; WP_011101718.1; NC_004567.2.
DR RefSeq; YP_004890044.1; NC_004567.2.
DR AlphaFoldDB; Q88UW5; -.
DR SMR; Q88UW5; -.
DR STRING; 220668.lp_2336; -.
DR EnsemblBacteria; CCC79530; CCC79530; lp_2336.
DR KEGG; lpl:lp_2336; -.
DR PATRIC; fig|220668.9.peg.1975; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_1_0_9; -.
DR OMA; EANFNPM; -.
DR PhylomeDB; Q88UW5; -.
DR BioCyc; LPLA220668:G1GW0-2014-MON; -.
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 InterPro; IPR040657; GshAB_ATP-grasp.
DR PANTHER; PTHR38761; PTHR38761; 2.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR SUPFAM; SSF55931; SSF55931; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..751
FT /note="Glutathione biosynthesis bifunctional protein GshAB"
FT /id="PRO_0000192552"
FT REGION 1..336
FT /note="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
