GSHAB_STRA3
ID GSHAB_STRA3 Reviewed; 750 AA.
AC Q8E399;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=gbs1862;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(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; AL766854; CAD47521.1; -; Genomic_DNA.
DR RefSeq; WP_000582678.1; NC_004368.1.
DR AlphaFoldDB; Q8E399; -.
DR SMR; Q8E399; -.
DR STRING; 211110.gbs1862; -.
DR EnsemblBacteria; CAD47521; CAD47521; CAD47521.
DR KEGG; san:gbs1862; -.
DR eggNOG; COG1181; Bacteria.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_1_0_9; -.
DR OMA; EANFNPM; -.
DR UniPathway; UPA00142; UER00209.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000000823; 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.
FT CHAIN 1..750
FT /note="Glutathione biosynthesis bifunctional protein GshAB"
FT /id="PRO_0000192558"
FT DOMAIN 489..747
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT REGION 1..333
FT /note="Glutamate--cysteine ligase"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 750 AA; 85603 MW; 97829C2C5B44174A CRC64;
MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN YHPYIQTDYS
EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP LSMPPKVREE DIQIAQLEDA
FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG QELLTSLFEL SQADNAIDFQ NQLYMKLSQN
FLRYRWLLTY LYGASPVAEE DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND
LENAVKSGQL IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL VDAMQSVIQH
FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET FGQRQGQIYH DYAWEAPYAL
KGYETMELST QLLLFDVIQK GVNFEVLDEQ DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL
AMANKVVTKK ILDEKHFPTP FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK
TSANLASYEK AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT KIELRRNSNI
STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP NATQAYSKDK KNATCIELNF
NPLMYMHTYC QEGPGQSITP RILAKLFPEL
