GSHB_ECO27
ID GSHB_ECO27 Reviewed; 316 AA.
AC B7UHZ4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
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 OrderedLocusNames=E2348C_3200;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000312|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [2]
RP GLYCOSYLATION AT 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};
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 -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00162}.
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DR EMBL; FM180568; CAS10748.1; -; Genomic_DNA.
DR RefSeq; WP_000593260.1; NC_011601.1.
DR AlphaFoldDB; B7UHZ4; -.
DR SMR; B7UHZ4; -.
DR EnsemblBacteria; CAS10748; CAS10748; E2348C_3200.
DR KEGG; ecg:E2348C_3200; -.
DR HOGENOM; CLU_068239_0_0_6; -.
DR OMA; WMRKDPP; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000008205; Chromosome.
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..316
FT /note="Glutathione synthetase"
FT /id="PRO_0000452589"
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"
SQ SEQUENCE 316 AA; 35613 MW; 3A79DCF61F8028EB CRC64;
MIKLGIVMDP IANINIKKDS SFAMLLEAQR RGYELHYMEM ADLYLINGEA RARTRTLSVE
QNYDKWYEFT GEQDLPLADL DVILMRKDPP FDTEFIYATY ILERAEEKGT LIVNKPQSLR
DCNEKLFTAW FSDLTPETLV TRNKAQLKAF WEKHSDIILK PLDGMGGASI FRVKEGDPNL
GVIAETLTEH GTRYCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG
RGEPRPLTES DWKIARQIGP TLKEKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPVS
ITGMLMDAIE ARLQQQ
