GSHAB_STRMU
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 03-AUG-2022, entry version 117.
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; Firmicutes; 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 glutamate--
CC cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
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DR EMBL; AE014133; AAN58035.1; -; Genomic_DNA.
DR RefSeq; NP_720729.1; NC_004350.2.
DR RefSeq; WP_002262729.1; NC_004350.2.
DR AlphaFoldDB; Q8DW15; -.
DR SMR; Q8DW15; -.
DR STRING; 210007.SMU_267c; -.
DR PRIDE; Q8DW15; -.
DR EnsemblBacteria; AAN58035; AAN58035; 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 OMA; EANFNPM; -.
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 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 InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01435; glu_cys_lig_rel; 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
