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Database: UniProt/TrEMBL
Entry: F5Y4J1_RAMTT
LinkDB: F5Y4J1_RAMTT
Original site: F5Y4J1_RAMTT 
ID   F5Y4J1_RAMTT            Unreviewed;       319 AA.
AC   F5Y4J1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   19-FEB-2014, entry version 16.
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=Rta_02450;
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543
OS   / TTB310).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310;
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M.,
RA   Py B., Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A.,
RA   Mejean V., DuBow M., Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) 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; CP000245; AEG91309.1; -; Genomic_DNA.
DR   RefSeq; YP_004617328.1; NC_015677.1.
DR   EnsemblBacteria; AEG91309; AEG91309; Rta_02450.
DR   GeneID; 10830801; -.
DR   KEGG; rta:Rta_02450; -.
DR   KO; K01920; -.
DR   OMA; PTCFQEI; -.
DR   BioCyc; RTAT365046:GHCU-250-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   319 AA;  35106 MW;  8875A2EF373F07C4 CRC64;
     MNLLFVADPL EAFKTYKDTT FSMMREAQRR GHRIAACEPR HLSWRSGGVV QARVREITLT
     GGEDDWFREN ATPVRPLKEF GAVLMRKDPP FDSEYFYATH LLEQAEREGA RVFNRPASLR
     DHPEKLAVME FPRFVSPTLV TRDPEEVRRF HAEHGDVILK PLDGMGGMGI FRVKTDGLNL
     GSITETLNNA GATTIMVQRF VPEIAAGDKR VLVIGGKPVP FSLARIPQGS EVRGNLAAGG
     KGVAQPLTPR DHEIAQALGP VLAARGLLLV GLDVIGDWLT EINVTSPTCF QEITQQAGFD
     VPAMFIDALE AALAQPVSR
//
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