ID   GSHB_CITRO              Reviewed;         315 AA.
AC   A0A482PU20;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162, ECO:0000305|PubMed:31974499};
DE   AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN   Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162, ECO:0000303|PubMed:31974499};
GN   ORFNames=E2R62_21965 {ECO:0000312|EMBL:QBY31206.1};
OS   Citrobacter rodentium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=67825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DBS100;
RA   Popov G., Fiebig A., Shideler S., Coombes B., Savchenko A.;
RT   "Complete genome sequence of enteropathogenic Citrobacter rodentium strain
RT   DBS100.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CATALYTIC ACTIVITY, GLYCOSYLATION AT ARG-256, AND MUTAGENESIS OF ARG-256.
RX   PubMed=31974499; DOI=10.1038/s41598-020-58062-y;
RA   El Qaidi S., Scott N.E., Hays M.P., Geisbrecht B.V., Watkins S.,
RA   Hardwidge P.R.;
RT   "An intra-bacterial activity for a T3SS effector.";
RL   Sci. Rep. 10:1073-1073(2020).
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_00162, ECO:0000305|PubMed:31974499};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00162};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00162};
CC       Note=Binds 1 magnesium or manganese ion per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00162};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00162}.
CC   -!- PTM: Glycosylation at Arg-256 by NleB enhances the glutathione
CC       synthetase activity, leading to an increase in glutathione production
CC       (PubMed:31974499). Glycosylation may promote C.rodentium survival in
CC       oxidative stress conditions (PubMed:31974499).
CC       {ECO:0000269|PubMed:31974499}.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00162}.
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DR   EMBL; CP038008; QBY31206.1; -; Genomic_DNA.
DR   RefSeq; WP_012908854.1; NZ_JXUN01000147.1.
DR   AlphaFoldDB; A0A482PU20; -.
DR   SMR; A0A482PU20; -.
DR   OMA; WMRKDPP; -.
DR   UniPathway; UPA00142; UER00210.
DR   GO; GO:0005524; F:ATP binding; 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; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00162; GSH_S; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006284; Glut_synth_pro.
DR   InterPro; IPR004218; GSHS_ATP-bd.
DR   InterPro; IPR004215; GSHS_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR21621:SF4; PTHR21621:SF4; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01380; glut_syn; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glutathione biosynthesis; Glycoprotein; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..315
FT                   /note="Glutathione synthetase"
FT                   /id="PRO_0000452588"
FT   DOMAIN          125..310
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   CARBOHYD        256
FT                   /note="N-beta-linked (GlcNAc) arginine"
FT                   /evidence="ECO:0000269|PubMed:31974499"
FT   MUTAGEN         256
FT                   /note="R->A: Abolished glycosylation by NleB."
FT                   /evidence="ECO:0000269|PubMed:31974499"
SQ   SEQUENCE   315 AA;  35289 MW;  6A97F25FBDF9BE28 CRC64;
     MIKLGIVMDP IASINIKKDS SFAMLLEAQR RGYELHYMEM ADLYLINGEA RARTRTLSVE
     QNYDKWYDFT GEQDLALDSL DAILMRKDPP FDTEFIYATY ILERAEEKGT LIVNKPQSLR
     DCNEKLFTAW FSDLTPETLV TRNKAQLKAF WQKHSDIILK PLDGMGGASI FRVKEGDPNL
     GVIAETLTEH GTRYCMAQNY LPAIVDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG
     RGEPRPLTDS DWAIARRIGP TLKAKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPIS
     ITGMLMDAIE ARLQK