GenomeNet

Database: UniProt
Entry: Q8YE82
LinkDB: Q8YE82
Original site: Q8YE82 
ID   GSHB_BRUME              Reviewed;         312 AA.
AC   Q8YE82;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 97.
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=BMEI1996;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL53177.1; -; Genomic_DNA.
DR   PIR; AF3501; AF3501.
DR   RefSeq; WP_004684568.1; NZ_GG703778.1.
DR   ProteinModelPortal; Q8YE82; -.
DR   SMR; Q8YE82; -.
DR   STRING; 224914.BAWG_0251; -.
DR   EnsemblBacteria; AAL53177; AAL53177; BMEI1996.
DR   GeneID; 29594884; -.
DR   KEGG; bme:BMEI1996; -.
DR   KEGG; bmel:DK63_1495; -.
DR   PATRIC; fig|224914.52.peg.1576; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   BioCyc; BMEL224914:G1FZL-2129-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000419; Chromosome I.
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.
FT   CHAIN         1    312       Glutathione synthetase.
FT                                /FTId=PRO_0000197457.
FT   DOMAIN      125    309       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00162}.
FT   NP_BIND     151    207       ATP. {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       280    280       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       282    282       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
SQ   SEQUENCE   312 AA;  35446 MW;  B47548715CF963F7 CRC64;
     MALKVAVQMD HISTVNITGD TTFALSLEAQ KRGHELFHYT PDWLSMRDGV VSARVEKMEV
     RDVKGDHYTL GEPVRRDLTE MDVILLRQDP PFDMNYITTT HLLERIHPKT LVVNDPTWVR
     NSPEKIFVTE FPDLMPETLI TKDPQEVMDF RREFGDIILK PLYGNGGAGV FHLADGDRNL
     TSLLEMFGQL FREPFIAQRY LKDVRAGDKR IILIDGEPVG ALNRVPSETD ARSNMHVGGR
     PEQSKLTPRE REICARIGPS LKERGFILVG IDVIGDYMTE INVTSPTGIR EIERFDGTNI
     AALFWDAVEA RR
//
DBGET integrated database retrieval system