ID   GSHAB_STRMU             Reviewed;         754 AA.
AC   Q8DW15;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000255|HAMAP-Rule:MF_00782};
DE   AltName: Full=Gamma-GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE            Short=GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GCS {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00782};
DE              Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00782};
DE     AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00782};
GN   Name=gshAB {ECO:0000255|HAMAP-Rule:MF_00782};
GN   Synonyms=gshF {ECO:0000255|HAMAP-Rule:MF_00782};
GN   OrderedLocusNames=SMU_267c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via
CC       gamma-L-glutamyl-L-cysteine. {ECO:0000255|HAMAP-Rule:MF_00782}.
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_00782};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00782};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00782}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glutamate--cysteine ligase type 1 family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00782}.
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DR   EMBL; AE014133; AAN58035.1; -; Genomic_DNA.
DR   RefSeq; NP_720729.1; NC_004350.2.
DR   AlphaFoldDB; Q8DW15; -.
DR   SMR; Q8DW15; -.
DR   STRING; 210007.SMU_267c; -.
DR   KEGG; smu:SMU_267c; -.
DR   PATRIC; fig|210007.7.peg.233; -.
DR   eggNOG; COG1181; Bacteria.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_1_0_9; -.
DR   OrthoDB; 9803907at2; -.
DR   PhylomeDB; Q8DW15; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.590.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   HAMAP; MF_00782; Glut_biosynth; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006335; Glut_biosynth.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   InterPro; IPR040657; GshAB_ATP-grasp.
DR   NCBIfam; TIGR01435; glu_cys_lig_rel; 1.
DR   PANTHER; PTHR38761; GLUTAMATE--CYSTEINE LIGASE; 1.
DR   PANTHER; PTHR38761:SF1; GLUTAMATE--CYSTEINE LIGASE; 1.
DR   Pfam; PF18419; ATP-grasp_6; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 2.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..754
FT                   /note="Glutathione biosynthesis bifunctional protein GshAB"
FT                   /id="PRO_0000192560"
FT   DOMAIN          489..752
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   REGION          1..333
FT                   /note="Glutamate--cysteine ligase"
FT   BINDING         516..574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         696
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         696
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         717
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         717
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         717
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         717
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         719
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT   BINDING         719
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
SQ   SEQUENCE   754 AA;  86187 MW;  103479A8536A10CB CRC64;
     MHINQLLQHA NSDLPLLQAN FGLERESLRI NKTNHRLAQT PHPTALGSRQ FHPYIQTDYS
     ESQMELITPV AHSSKEVLRF LGAITDVAER SIDQNQYLWP LSMPPQITED EIEIAQLEDD
     FEFSYRQYLD KKYGKILQSI SGIHYNMELG ADLMNELFEL SGYQSFIDFK NDLYLKVAQN
     FLNYRWFLTY LYGASPLAEK GFLNEELSQT VRSIRNSHLG YVNTDDIKVP FDSLENYISS
     IEHYVKSGAL SAEKEFYSAV RLRGSKHNRD YLTKGITYLE FRCFDLNPFN NRGITQETID
     SVHLFILAML WLDTPKKLNQ ALDKAQKLND KIALSHPLEK LPKENSASLI IEAMEALIKH
     FKLPSYYDDL LIAIKKQVEN PKLTLSGRLF EHIKHASLEH FGQKKGQDYH NYAWQNYYAL
     KGYENMELST QMLLFDTIQK GIHFEILDEN DQFLKLWHND HIEYVKNGNM TSKDNYVIPL
     AMANKVVTKK ILRENGYPVP AGAEFDNKDE ALRYYSQIKN KPIVVKPKTT NFGLGISIFE
     TAASHNDYEK ALDIAFIEDY SVLVEEFIPG TEYRFFILDG KCEAVLLRVA ANVVGDGHST
     VRQLVAQKNR DPLRGREHRS PLEIIDLGDI ELLMLQQEGY TLEDILPKGK KVNLRGNSNI
     STGGDSIDVT ETMDPSYKQL AANMATAMGA WVCGVDLIIP DTNLKASKGK PNCTCIELNF
     NPSMYMHTYC YQGPGQVITG KILAKLFPEI STKI
//