ID   GSHB_XANAC              Reviewed;         316 AA.
AC   Q8PHZ5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Glutathione synthetase;
DE            EC=6.3.2.3;
DE   AltName: Full=Glutathione synthase;
DE   AltName: Full=GSH synthetase;
DE            Short=GSH-S;
DE            Short=GSHase;
GN   Name=gshB; OrderedLocusNames=XAC3103;
OS   Xanthomonas axonopodis pv. citri (Citrus canker).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=92829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   MEDLINE=22022145; 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: ATP + gamma-L-glutamyl-L-cysteine + glycine =
CC       ADP + phosphate + glutathione.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 2/2.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; AE011954; AAM37948.1; -; Genomic_DNA.
DR   RefSeq; NP_643412.1; -.
DR   HSSP; P04425; 1GLV.
DR   GeneID; 1157174; -.
DR   GenomeReviews; AE008923_GR; XAC3103.
DR   KEGG; xac:XAC3103; -.
DR   NMPDR; fig|190486.1.peg.3056; -.
DR   HOGENOM; Q8PHZ5; -.
DR   OMA; Q8PHZ5; VRNAPEK.
DR   BioCyc; XAXO190486:XAC3103-MON; -.
DR   BRENDA; 6.3.2.3; 289771.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00162; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006284; Glut_synth_pro.
DR   InterPro; IPR004218; GSHS_ATP_bd.
DR   InterPro; IPR004215; GSHS_N.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 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    316       Glutathione synthetase.
FT                                /FTId=PRO_0000197496.
FT   DOMAIN      124    311       ATP-grasp.
FT   NP_BIND     151    208       ATP (By similarity).
FT   METAL       282    282       Magnesium or manganese (By similarity).
FT   METAL       284    284       Magnesium or manganese (By similarity).
SQ   SEQUENCE   316 AA;  34321 MW;  BAEABE5F8A0FF268 CRC64;
     MSLDVVVVMD PIASIKIAKD TTFAMLLEAQ RRGHRLHYVR PGGLSLREGR AVAQVAPLSV
     REDKTSWFTL GEFAELAFGP GQVVLMRKDP PVDAEFVYDT QVLSVAQRAG AQIVNDPQGL
     RDYNEKLAAL LFPQCCPPTL VSRDAAALKA FVLEHGQAVL KPLDGMGGRS IFRSGSGDPN
     LNVILETLTD GNRKLTLAQR FIPDITAGDK RILLVDGLPV DYCLARIPQG DEFRGNLAAG
     GRGEGRPLSE RDRWIAAQVG PEMRRRGMRF VGLDVIGDYL TEVNVTSPTC VRELDAQFGL
     NIAGLLFDAI EAGAAQ
//