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Database: UniProt
Entry: Q9JYJ3
LinkDB: Q9JYJ3
Original site: Q9JYJ3 
ID   GSHB_NEIMB              Reviewed;         319 AA.
AC   Q9JYJ3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 103.
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};
GN   OrderedLocusNames=NMB1559;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41913.1; -; Genomic_DNA.
DR   PIR; D81069; D81069.
DR   RefSeq; NP_274566.1; NC_003112.2.
DR   RefSeq; WP_002225038.1; NC_003112.2.
DR   ProteinModelPortal; Q9JYJ3; -.
DR   SMR; Q9JYJ3; -.
DR   STRING; 122586.NMB1559; -.
DR   PaxDb; Q9JYJ3; -.
DR   PRIDE; Q9JYJ3; -.
DR   EnsemblBacteria; AAF41913; AAF41913; NMB1559.
DR   GeneID; 904122; -.
DR   KEGG; nme:NMB1559; -.
DR   PATRIC; fig|122586.8.peg.2006; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   BioCyc; NMEN122586:G1G1B-1507-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IBA:GO_Central.
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    319       Glutathione synthetase.
FT                                /FTId=PRO_0000197470.
FT   DOMAIN      129    314       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00162}.
FT   NP_BIND     155    211       ATP. {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       285    285       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       287    287       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
SQ   SEQUENCE   319 AA;  35146 MW;  327C0F342F09C2F0 CRC64;
     MMKVLFIADP MASFKTYKDT TYAMMREMAK RGWRLFHTLS GELSVNGGLV TAQASAFEFL
     GAKNDDDHAW FKSADKVQTA LEAFDAVIMR TDPPFDMQYL YATQLLTLAE QQGAKVFNSG
     QAMRDFNEKL AILNFSRFIA PTLVTTRSAD VRTFLKEHGD IIIKPLDGMG GMGIFRLTEK
     DPNIGSILET LMQLDSRTIM AQRYIPEIVH GDKRILIIGG EVVPYALARI PQNGETRGNL
     AAGGRGVAQE LGGRDREIAE TLAPELKRRG ILLAGLDVIG SNLTEVNVTS PTGFQEIMKQ
     KGFDVAAMFA DAVAAWSVR
//
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