ID S6CGS4_9GAMM Unreviewed; 316 AA.
AC S6CGS4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:BAN69765.1};
GN ORFNames=EBS_1900 {ECO:0000313|EMBL:BAN69765.1};
OS endosymbiont of unidentified scaly snail isolate Monju.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN69765.1, ECO:0000313|Proteomes:UP000015562};
RN [1] {ECO:0000313|EMBL:BAN69765.1, ECO:0000313|Proteomes:UP000015562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Monju {ECO:0000313|EMBL:BAN69765.1};
RX PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT "Allying with armored snails: the complete genome of gammaproteobacterial
RT endosymbiont.";
RL ISME J. 8:40-51(2014).
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; AP012978; BAN69765.1; -; Genomic_DNA.
DR RefSeq; WP_043108510.1; NZ_AP012978.1.
DR AlphaFoldDB; S6CGS4; -.
DR STRING; 1248727.EBS_1900; -.
DR KEGG; enm:EBS_1900; -.
DR HOGENOM; CLU_068239_0_0_6; -.
DR OrthoDB; 9785415at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000015562; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015562}.
FT DOMAIN 126..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 316 AA; 34849 MW; D16F76EF9514212E CRC64;
MAPALLVIMD PIAQIKIHKD STFAMLLEAQ ARGWALHYAE QRDLSQRDGR TLVCSRPLRV
KDDAAGWFEL DTTEEGPVDR FPVVLMRKDP PFDLDYITTT WLLDQPAASG TLVVNHPKAL
RNHNEKLAAT RFPQLCPPVL VASDMAALER FVDEQGDVIL KPLDGMGGAS IFRVRPDDPN
RRVILETLTH HGRRQVMAQR FIPEIRDGDK RILVIDGEAV PWALARVPAE GETRGNLAAG
GQGVGVALND RDRDIVAAVA PFLREAGILF AGLDVIGDYL TEINITSPTC IRELDALYSL
NIAGTLMDHI EQTIAV
//
