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Database: UniProt
Entry: J9DGP8_9PROT
LinkDB: J9DGP8_9PROT
Original site: J9DGP8_9PROT 
ID   J9DGP8_9PROT            Unreviewed;       314 AA.
AC   J9DGP8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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   ORFNames=IMCC14465_08270 {ECO:0000313|EMBL:EJW21031.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW21031.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW21031.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW21031.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT   to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW21031.1}.
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DR   EMBL; ALYF01000003; EJW21031.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9DGP8; -.
DR   STRING; 1220535.IMCC14465_08270; -.
DR   PATRIC; fig|1220535.3.peg.823; -.
DR   eggNOG; COG0189; Bacteria.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000004836; Unassembled WGS sequence.
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:UP000004836}.
FT   DOMAIN          128..309
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   314 AA;  34646 MW;  A002BB046FCCAD48 CRC64;
     MVLKVAIQMD PIESIDVGCD STFALGIEAQ KRGFELHYYL PENMSLRDGL VTARMRSLAL
     NDQSADYFSV GPEEIRNLTD MDVVLMRQDP PFDMAYISAT HMLEQICDTT LVVNDPVAVR
     NGPEKILPVL FPALQPPTLL TRDVKALADF RQEFGDIILK PVYGNGGAGV FRVTQQDENF
     SALVEMFIVS SREPIVAQQY LPDVRQGDKR VILIEGEAVA SVNRVPQPGE ARANVHVGGR
     PVASELSDRD IEIANIIGTY LRDNGIIFAG IDVIGDYLTE INVTSPTCIR EIADFGGPDV
     ASLIWDAIEV RLKR
//
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