ID Q2NRC8_SODGM Unreviewed; 318 AA.
AC Q2NRC8;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00162};
DE AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00162};
DE Short=GSHase {ECO:0000256|HAMAP-Rule:MF_00162};
DE AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00162};
GN Name=gshB {ECO:0000256|HAMAP-Rule:MF_00162,
GN ECO:0000313|EMBL:CRL46301.1};
GN OrderedLocusNames=SG2022 {ECO:0000313|EMBL:BAE75297.1};
GN ORFNames=SGGMMB4_04794 {ECO:0000313|EMBL:CRL46301.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75297.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE75297.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Morsitans {ECO:0000313|EMBL:BAE75297.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [2] {ECO:0000313|EMBL:CRL46301.1, ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:CRL46301.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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_00162};
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 2/2. {ECO:0000256|HAMAP-
CC Rule:MF_00162}.
CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_00162}.
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DR EMBL; AP008232; BAE75297.1; -; Genomic_DNA.
DR EMBL; LN854557; CRL46301.1; -; Genomic_DNA.
DR RefSeq; WP_011411752.1; NZ_LN854557.1.
DR STRING; 343509.SG2022; -.
DR KEGG; sgl:SG2022; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_6; -.
DR OrthoDB; 9785415at2; -.
DR BioCyc; SGLO343509:SGP1_RS18485-MONOMER; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000001932; Chromosome.
DR Proteomes; UP000245838; Chromosome sggmmb4_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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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 NCBIfam; TIGR01380; glut_syn; 1.
DR PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF02955; GSH-S_ATP; 1.
DR Pfam; PF02951; GSH-S_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00162};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW Rule:MF_00162};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00162};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00162}.
FT DOMAIN 125..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 318 AA; 35677 MW; 97B1F180C58CB216 CRC64;
MIKLGIVMDP ISTINIKKDS SFAMLLEAQS RGYEIHYMEM SSLYLRGGEA RASTRLLSVK
QDYDAWYSFN GEKDINLGEL DVILMRKDPP FDTEFIYATY ILERAEDEGA LIVNKPQSLR
DCNEKLFTAW FARHTPDTLV SHRDDHIRAF WQEHGDIILK PLDGMGGTSI FRVKQDDPNL
TVIVETLTGY GRHFCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPKSG ETRGNLAAGG
HGEARPLSDS DWKIARDVAP VLKKKGLIFV GLDIIGDRLT EINVTSPTCV REIEAAFPIS
ITGMLMDAIE KRLAAQQR
//
