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Database: UniProt
Entry: S5RKE3_9STRE
LinkDB: S5RKE3_9STRE
Original site: S5RKE3_9STRE 
ID   S5RKE3_9STRE            Unreviewed;       749 AA.
AC   S5RKE3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000256|HAMAP-Rule:MF_00782};
DE   AltName: Full=Gamma-GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE            Short=GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_00782};
DE              Short=GCS {ECO:0000256|HAMAP-Rule:MF_00782};
DE     AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE   Includes:
DE     RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE              EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00782};
DE     AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE              Short=GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE              Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00782};
DE              Short=GSHase {ECO:0000256|HAMAP-Rule:MF_00782};
DE     AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00782};
GN   Name=gshAB {ECO:0000256|HAMAP-Rule:MF_00782};
GN   Synonyms=gshF {ECO:0000256|HAMAP-Rule:MF_00782};
GN   ORFNames=KE3_1920 {ECO:0000313|EMBL:AGS06371.1};
OS   Streptococcus lutetiensis 033.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS06371.1, ECO:0000313|Proteomes:UP000015268};
RN   [1] {ECO:0000313|EMBL:AGS06371.1, ECO:0000313|Proteomes:UP000015268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=033 {ECO:0000313|EMBL:AGS06371.1,
RC   ECO:0000313|Proteomes:UP000015268};
RX   PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA   Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA   Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA   Xu J.;
RT   "Dynamics of fecal microbial communities in children with diarrhea of
RT   unknown etiology and genomic analysis of associated Streptococcus
RT   lutetiensis.";
RL   BMC Microbiol. 13:141-141(2013).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via
CC       gamma-L-glutamyl-L-cysteine. {ECO:0000256|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:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-
CC         Rule:MF_00782};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006,
CC       ECO:0000256|HAMAP-Rule:MF_00782}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00782}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00782}.
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DR   EMBL; CP003025; AGS06371.1; -; Genomic_DNA.
DR   RefSeq; WP_020917562.1; NC_021900.1.
DR   AlphaFoldDB; S5RKE3; -.
DR   KEGG; slu:KE3_1920; -.
DR   PATRIC; fig|1076934.5.peg.1889; -.
DR   HOGENOM; CLU_020728_1_0_9; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000015268; 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   InterPro; IPR020561; PRibGlycinamid_synth_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; PF01071; GARS_A; 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 {ECO:0000256|HAMAP-Rule:MF_00782, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW   Rule:MF_00782};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00782};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_00782};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00782, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          488..746
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..332
FT                   /note="Glutamate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00782"
SQ   SEQUENCE   749 AA;  84307 MW;  563C67076B57F7F9 CRC64;
     MSLNGLLEKS PATLPILQAT FGLERESLRI GKDHRIAQTD HPACLGSRSF HPYIQTDYSE
     AQLELITPIA HSTKEALRFL GALTDVAGRS IDKSEYLWPL SIPPKLCETD IHIAKLEDDY
     ECYYRKHLAD VYGKTLQSMS GIHFNMELGK DLVASLFKES GYQSIIDFKN DIHLKLAQNF
     LRFRWLLTYL YGASPIAEEG FFSKTLAKPV RSIRNSHLGY VNHKDIQVSY ESLEKYISDI
     EAHIASGKLI AEKEFYSAVR LRGSKHVRDY LTNGVTYLEL RTFDLNPFDN RGITQETLDT
     VHLFVLALLW LDSSSAIDQD ITEASKLNDK IALSHPLDKL PEDAPVEIIL LAMQGIVDYF
     ELSDYYQGLI DAIKNQIEHP EQTIAGRLLE EIDTLSLESF GQKQGQAFHD YAWQAPYALK
     GYENMELSTQ LLMFDAIQKG VHLEVLDEND QFIKLWHGEH VEYVKNANMT GKDSYITPLI
     MENKVVTKKL LSKAGFPVPK GEEFADKAAA LRYFSQIKDK AIVVKPKSTN FGLGISIFKE
     SADLTAYQKA LDIAFAEDDT VLIEEFISGT EYRFFVLDGK CEAMLLRVPA NVVGDGKHTI
     AQLVEMKNQD PLRGRDHRSP LEIIDLGDVE KLMLQQQGYT PDDIPADRVR VDLRRNSNIS
     TGGDSIDVTD IMPDDYKTLA AQMARAVGAW VCGVDLIIPD KSLPASKEEP NCACIELNFN
     PAIYLHTYCH EGPGQALTPK ILAKLFPEL
//
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