ID Q1BTA5_BURCA Unreviewed; 318 AA.
AC Q1BTA5;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Glutathione synthetase;
DE EC=6.3.2.3;
DE AltName: Full=GSH synthetase;
DE AltName: Full=Glutathione synthase;
GN Name=gshB; OrderedLocusNames=Bcen_2249;
OS Burkholderia cenocepacia (strain AU 1054).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU 1054;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., LiPuma J.J.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU
RT 1054.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
CC ADP + phosphate + glutathione.
CC -!- COFACTOR: Binds (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; CP000378; ABF77150.1; -; Genomic_DNA.
DR RefSeq; YP_622123.1; NC_008060.1.
DR ProteinModelPortal; Q1BTA5; -.
DR STRING; 331271.Bcen_2249; -.
DR EnsemblBacteria; ABF77150; ABF77150; Bcen_2249.
DR GeneID; 4092991; -.
DR KEGG; bcn:Bcen_2249; -.
DR PATRIC; 19048209; VBIBurCen11237_2348.
DR eggNOG; COG0189; -.
DR HOGENOM; HOG000265022; -.
DR KO; K01920; -.
DR OMA; WMRKDPP; -.
DR ProtClustDB; PRK05246; -.
DR BioCyc; BCEN331271:GHKX-5896-MONOMER; -.
DR UniPathway; UPA00142; UER00210.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
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:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_00162; GSH_S; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom.
DR Pfam; PF02955; GSH-S_ATP; 1.
DR Pfam; PF02951; GSH-S_N; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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 DOMAIN 129 314 ATP-grasp (By similarity).
FT NP_BIND 155 211 ATP (By similarity).
FT METAL 285 285 Magnesium or manganese (By similarity).
FT METAL 287 287 Magnesium or manganese (By similarity).
SQ SEQUENCE 318 AA; 34943 MW; 5F07D34AECEE48DF CRC64;
MDILFIADPL DHFKIYKDST YAMMAEAARR GHAVYAGEPR HLAWTGSAVE ADVRRITFVG
ELDDLHRDTW FEAGPVDARR LESFGAVLMR KDPPFDMEYV TSTWLLELAE RAGARVFNKA
QSIRDHSEKL AIGEFPQFVA PTLVTRDAKR LRAFHAEHGD VILKPLDGMG GMGVFRVKPD
GMNLGSIVEM LSHDRTRSVM AQKFIPEIKA GDKRILLIGG EPVPYSLARI PQGSEVRGNL
AAGGLGVAQP LTARDREIAD TLGPVLASRG LLLVGLDAIG DWLTEVNVTS PTCFREIMEQ
TGFDVAAMFI DALERAAA
//
