ID   GSHB_BUCAP              Reviewed;         320 AA.
AC   Q8K931;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
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=BUsg_529;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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; AE013218; AAM68070.1; -; Genomic_DNA.
DR   RefSeq; NP_660859.1; -.
DR   HSSP; P04425; 1GSH.
DR   GeneID; 1005649; -.
DR   GenomeReviews; AE013218_GR; BUsg_529.
DR   KEGG; bas:BUsg529; -.
DR   HOGENOM; Q8K931; -.
DR   OMA; Q8K931; VRNAPEK.
DR   BioCyc; BAPH198804:BUSG529-MON; -.
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    320       Glutathione synthetase.
FT                                /FTId=PRO_0000197460.
FT   DOMAIN      130    315       ATP-grasp.
FT   NP_BIND     156    212       ATP (By similarity).
FT   METAL       286    286       Magnesium or manganese (By similarity).
FT   METAL       288    288       Magnesium or manganese (By similarity).
SQ   SEQUENCE   320 AA;  37166 MW;  20D4A253EEBBD83E CRC64;
     MRKKKNLKIG IVMDSITLIN IKKDSSFAIL LEAQKRQHEI YYMEMNDLYL RKGQSYATTK
     SIEIQKNQNN YFKFIQKKDI SLNELDAILM RKDPPFNTEF IYATYILERA EEKGVLVINK
     PKSLRDCNEK IFISWFSRFT TDTLVTRKLS KIHNFWKEKN DIILKPLDAM GGKGVFRIKK
     DDPNFSVIVE TLTNYEKKYC MIQTYLPEVQ FGDKRILIVN GKPIPWSLTR IPKHGETRAN
     LAVGGEGRVQ KLNDKDWEIA NYLAPILKKR GLILVGLDVI GDKLTEINVT SPTCICEIEE
     KKNISITGIL IDYIEDKIYK
//