ID F6AQT9_DELSC Unreviewed; 316 AA.
AC F6AQT9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 07-SEP-2016, entry version 30.
DE RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00162};
DE AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00162};
GN Name=gshB {ECO:0000256|HAMAP-Rule:MF_00162};
GN OrderedLocusNames=DelCs14_5871 {ECO:0000313|EMBL:AEF92840.1};
OS Delftia sp. (strain Cs1-4).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=742013 {ECO:0000313|EMBL:AEF92840.1, ECO:0000313|Proteomes:UP000009225};
RN [1] {ECO:0000313|Proteomes:UP000009225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cs1-4 {ECO:0000313|Proteomes:UP000009225};
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. {ECO:0000256|HAMAP-Rule:MF_00162}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00162};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00162};
CC Note=Binds 1 magnesium or manganese ion per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_00162};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC from L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
CC Rule:MF_00162}.
CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_00162}.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP-
CC Rule:MF_00162}.
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DR EMBL; CP002735; AEF92840.1; -; Genomic_DNA.
DR RefSeq; WP_013804762.1; NC_015563.1.
DR EnsemblBacteria; AEF92840; AEF92840; DelCs14_5871.
DR KEGG; del:DelCs14_5871; -.
DR KO; K01920; -.
DR OMA; GMGIFRV; -.
DR BioCyc; DSP742013:GH2F-5965-MONOMER; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000009225; Chromosome.
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 {ECO:0000256|HAMAP-Rule:MF_00162};
KW Complete proteome {ECO:0000313|Proteomes:UP000009225};
KW Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000313|EMBL:AEF92840.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00162};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00162};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00162};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162}.
FT DOMAIN 125 310 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT NP_BIND 151 207 ATP. {ECO:0000256|HAMAP-Rule:MF_00162}.
FT METAL 281 281 Magnesium or manganese.
FT {ECO:0000256|HAMAP-Rule:MF_00162}.
FT METAL 283 283 Magnesium or manganese.
FT {ECO:0000256|HAMAP-Rule:MF_00162}.
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
//
