ID F5Y4J1_RAMTT Unreviewed; 319 AA.
AC F5Y4J1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 01-MAY-2013, entry version 13.
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 (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 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: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 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
//
