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Database: UniProt
Entry: O32463
LinkDB: O32463
Original site: O32463 
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   13-FEB-2019, entry version 106.
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 PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; 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
RT   encodes a functional glutathione synthetase.";
RL   Microbiology 143:2883-2890(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942;
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., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = 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
CC       from 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}.
DR   EMBL; D88540; BAA22859.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58354.1; -; Genomic_DNA.
DR   RefSeq; WP_011244088.1; NC_007604.1.
DR   ProteinModelPortal; O32463; -.
DR   SMR; O32463; -.
DR   STRING; 1140.Synpcc7942_2324; -.
DR   PRIDE; O32463; -.
DR   EnsemblBacteria; ABB58354; ABB58354; Synpcc7942_2324.
DR   KEGG; syf:Synpcc7942_2324; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OrthoDB; 878336at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2324-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000002717; 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; 3.30.1490.20; -; 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; PTHR21621:SF4; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01380; glut_syn; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    323       Glutathione synthetase.
FT                                /FTId=PRO_0000197488.
FT   DOMAIN      133    317       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00162}.
FT   NP_BIND     159    215       ATP. {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       288    288       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       290    290       Magnesium or manganese.
FT                                {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
//
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