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 16-JUN-2009, entry version 43. 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=XCC2926; OS Xanthomonas campestris pv. campestris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=340; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE012407; AAM42198.1; -; Genomic_DNA. DR RefSeq; NP_638274.1; -. DR HSSP; P04425; 1GSH. DR GeneID; 999889; -. DR GenomeReviews; AE008922_GR; XCC2926. DR KEGG; xcc:XCC2926; -. DR HOGENOM; Q8P6P1; -. DR OMA; Q8P6P1; VRNAPEK. DR BioCyc; XCAM190485:XCC2926-MON; -. DR BRENDA; 6.3.2.3; 281360. 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_0000197497. 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; 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 //