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Database: UniProt
Entry: Q8P6P1
LinkDB: Q8P6P1
Original site: Q8P6P1 
ID   GSHB_XANCP              Reviewed;         316 AA.
AC   Q8P6P1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 102.
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=XCC2926;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
OS   NCPPB 528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(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; AE008922; AAM42198.1; -; Genomic_DNA.
DR   RefSeq; NP_638274.1; NC_003902.1.
DR   RefSeq; WP_011038049.1; NC_003902.1.
DR   ProteinModelPortal; Q8P6P1; -.
DR   SMR; Q8P6P1; -.
DR   STRING; 190485.XCC2926; -.
DR   EnsemblBacteria; AAM42198; AAM42198; XCC2926.
DR   GeneID; 999889; -.
DR   KEGG; xcc:XCC2926; -.
DR   PATRIC; fig|190485.4.peg.3131; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   BioCyc; XCAM190485:XCC2926-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000001010; 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    316       Glutathione synthetase.
FT                                /FTId=PRO_0000197497.
FT   DOMAIN      124    311       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00162}.
FT   NP_BIND     151    208       ATP. {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       282    282       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
FT   METAL       284    284       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00162}.
SQ   SEQUENCE   316 AA;  34173 MW;  B6818474D0D17641 CRC64;
     MSLDVVVVMD PIASIKIAKD TTFAMLLEAQ RRGHRLHYVR PGGLSLHEGR AVAQVAPLSV
     REDKASWFTL GAFTELVFGP GQVVLMRKDP PVDAEFIYDT QVLAVAQRAG AQVVNDPQGL
     RDYNEKLAAL LFPQCCPPTL VSRDAAALKA FVLAHGQAVL KPLDGMGGRS IFRSGTGDPN
     LNVILETLTD GGRKLTLAQR FIPDITAGDK RILLVDGEPV DYCLARIPQG DEFRGNLAAG
     GRGEGRPLSE RDRWIAAQVG PEMKRRGMRF VGLDVIGDYL TEVNVTSPTC VRELDAQFGL
     NIAGLLFDAI EAGTAQ
//
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