ID   B0U0T7_FRAP2            Unreviewed;       324 AA.
AC   B0U0T7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
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   OrderedLocusNames=Fphi_1813 {ECO:0000313|EMBL:ABZ88040.1};
OS   Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS   O#319-036).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=484022 {ECO:0000313|EMBL:ABZ88040.1};
RN   [1] {ECO:0000313|EMBL:ABZ88040.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 25017 {ECO:0000313|EMBL:ABZ88040.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Richardson P.;
RT   "Complete sequence of chromosome of Francisella philomiragia subsp.
RT   philomiragia ATCC 25017.";
RL   Submitted (JAN-2009) 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; CP000937; ABZ88040.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0U0T7; -.
DR   KEGG; fph:Fphi_1813; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_068239_0_0_6; -.
DR   UniPathway; UPA00142; UER00210.
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   324 AA;  37048 MW;  6EA984E0A431C408 CRC64;
     MKVGFIIDNL NSFNISKDST YMMLQAAQDK GWEIYTFYLN DLSIINGKPK GDALKIKIHK
     AKESWYEILS QHHDLSLLDL DCIFMRKDPP FNMEYIYVTY MLDLAKKHGV LIINNPQALR
     DFNEKVAISN YPKFAPNTLI TRSYKQINQF YAEHKDIIVK PLDGMGGSSI FRIKDGDKNK
     NVILETLTHH ETRYIMVQDY QEAIKDGDKR ILIVNGEPIK YLLARVPSDS DNRGNLAAGA
     RAEVRELQEQ DYKIAKKVAK KLKKEGVMFA GLDVIGDKLT EVNITSPTGI QEIYKATKVN
     AASLLMQAVE KKINKMRQEQ EHGE
//