ID   GSHB_SYNE7              Reviewed;         323 AA.
AC   O32463; Q31KR5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE            Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE   AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN   Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162}; Synonyms=gshII;
GN   OrderedLocusNames=Synpcc7942_2324;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9308172; DOI=10.1099/00221287-143-9-2883;
RA   Okumura N., Masamoto K., Wada H.;
RT   "The gshB gene in the cyanobacterium Synechococcus sp. PCC 7942 encodes a
RT   functional glutathione synthetase.";
RL   Microbiology 143:2883-2890(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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:0000255|HAMAP-
CC         Rule:MF_00162};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00162}.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00162}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D88540; BAA22859.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58354.1; -; Genomic_DNA.
DR   RefSeq; WP_011244088.1; NZ_CP130602.1.
DR   AlphaFoldDB; O32463; -.
DR   SMR; O32463; -.
DR   STRING; 1140.Synpcc7942_2324; -.
DR   PaxDb; 1140-Synpcc7942_2324; -.
DR   GeneID; 76401055; -.
DR   KEGG; syf:Synpcc7942_2324; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_068239_0_0_3; -.
DR   OrthoDB; 9785415at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2324-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000889800; 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; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Glutathione synthetase"
FT                   /id="PRO_0000197488"
FT   DOMAIN          133..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         159..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ   SEQUENCE   323 AA;  35418 MW;  6BFE8564548FBF72 CRC64;
     MKLAFLIDPI AALDPTHDST VALMEAAQLR GHEIWIGEIS DLSVHVGEPL GLLRPLKIEP
     VQWLGDRWQV ANPWFTAGEA KRRSLHDFAA VFMRKDPPVT TAYLYATYLL DLVDPKKTRV
     VNSPEGLRHA NEKMYALQFQ SVVPRTLVSS NKAEIRAFLD ELRAAVLKPL GGKAGEGILF
     LDPGDRNFNS LVEISTQQGQ LPVMVQQYLP EAKDGDKRII LVNGEPLGAV NRVPTGREFR
     GNMAVGGRVE AVPITDRDRE ICAAVAPRLR QDGLFFVGID VIGGYLTEVN VTSPTGIREI
     DRLNGVSIGD QTIAALEALV NQG
//