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Database: UniProt/TrEMBL
Entry: F6AQT9_DELSC
LinkDB: F6AQT9_DELSC
Original site: F6AQT9_DELSC 
ID   F6AQT9_DELSC            Unreviewed;       316 AA.
AC   F6AQT9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   19-FEB-2014, entry version 17.
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=DelCs14_5871;
OS   Delftia sp. (strain Cs1-4).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=742013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cs1-4;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Bradfield C.,
RA   Sheety A., Cheng S., Chain P., Denef V., Hickey W., Woyke T.;
RT   "Complete sequence of Delftia sp. Cs1-4.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002735; AEF92840.1; -; Genomic_DNA.
DR   RefSeq; YP_004491195.1; NC_015563.1.
DR   EnsemblBacteria; AEF92840; AEF92840; DelCs14_5871.
DR   GeneID; 10642769; -.
DR   KEGG; del:DelCs14_5871; -.
DR   KO; K01920; -.
DR   BioCyc; DSP742013:GH2F-5965-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-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; 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.
FT   DOMAIN      125    310       ATP-grasp (By similarity).
FT   NP_BIND     151    207       ATP (By similarity).
FT   METAL       281    281       Magnesium or manganese (By similarity).
FT   METAL       283    283       Magnesium or manganese (By similarity).
SQ   SEQUENCE   316 AA;  34723 MW;  1C8709984327D6F6 CRC64;
     MQILFVADPL ESFQTYKDTT FAMMREAQRR GHSIVACEPR QLSWQRGGKV VAHVRNIQLT
     GDAQQWFETT QEGLAELAGF DAILMRKDPP FDSEYFYSTH LLEQAEREGA KVFNKPRALR
     DHPEKLAILE FPQFIGPTLV TRSAQDIRAF HEEHQDIILK PLDGMGGMGI FRVGADGRNL
     GSIIETLNQG GASSVMVQKF LPEITQGDKR VLVIGGKPVP YCLARIPQGN EVRGNLAAGG
     KGVAQPLSEH DKAMAEEIGP ILMERGLLLA GVDVIGQCIT EINVTSPTCF QEIYDQTGCD
     VASLFVDALE QALATA
//
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