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Database: UniProt
Entry: J1FHI9_9BACT
LinkDB: J1FHI9_9BACT
Original site: J1FHI9_9BACT 
ID   J1FHI9_9BACT            Unreviewed;       349 AA.
AC   J1FHI9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-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=O71_13169 {ECO:0000313|EMBL:EJF09754.1};
OS   Pontibacter sp. BAB1700.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF09754.1, ECO:0000313|Proteomes:UP000003746};
RN   [1] {ECO:0000313|EMBL:EJF09754.1, ECO:0000313|Proteomes:UP000003746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB1700 {ECO:0000313|EMBL:EJF09754.1,
RC   ECO:0000313|Proteomes:UP000003746};
RX   PubMed=23105068; DOI=10.1128/JB.01550-12;
RA   Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT   Industrially Important Bacterium.";
RL   J. Bacteriol. 194:6329-6330(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:EJF09754.1}.
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DR   EMBL; AKIS01000090; EJF09754.1; -; Genomic_DNA.
DR   RefSeq; WP_007656791.1; NZ_AKIS01000090.1.
DR   AlphaFoldDB; J1FHI9; -.
DR   PATRIC; fig|1144253.3.peg.2599; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000003746; 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   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          137..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   349 AA;  38537 MW;  148DF85F873DD8AA CRC64;
     MTIGFVVNDI HTERPGYATI FLAQRMHNLG HTVFLMGVGD LAYYPDGYMG ATAVQADPKH
     KYKSPATYLD AIQGEKAIQV RVTAPDLDVL MLRNDPSAEG EGRAWAQNAG IIFGQLALRH
     GVIVLNDPTS LSDAVNKMYF QHFPEAVRPR TLITRDKEEI KQFFQKQKNN IILKPLQGSG
     GSGVFMVKKN DSTNLNQIVE AISRDGYVIA QEYLPQATEG DVRLFVVNGE ALQHKGKYCA
     LRRVGAKDDI RSNLHAGGSA QSVKVDQTML DLVELVRPKL IQDGMFMVGL DIVGNKLMEI
     NVFSPGGLSD VSELEGVDFS TPIIEAIERK VHYKNTYGTQ IDNKTVAMI
//
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