ID Q0AHG9_NITEC Unreviewed; 316 AA.
AC Q0AHG9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-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=Neut_0953;
OS Nitrosomonas eutropha (strain C91).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C91;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J., Shin M.,
RA Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium,
RT Nitrosomonas eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59213.1; -; Genomic_DNA.
DR RefSeq; YP_747178.1; NC_008344.1.
DR ProteinModelPortal; Q0AHG9; -.
DR STRING; 335283.Neut_0953; -.
DR EnsemblBacteria; ABI59213; ABI59213; Neut_0953.
DR GeneID; 4272424; -.
DR KEGG; net:Neut_0953; -.
DR PATRIC; 22719091; VBINitEut7577_1212.
DR eggNOG; COG0189; -.
DR HOGENOM; HOG000265022; -.
DR KO; K01920; -.
DR OMA; WMRKDPP; -.
DR ProtClustDB; PRK05246; -.
DR BioCyc; NEUT335283:GHT6-999-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 127 312 ATP-grasp (By similarity).
FT NP_BIND 153 209 ATP (By similarity).
FT METAL 283 283 Magnesium or manganese (By similarity).
FT METAL 285 285 Magnesium or manganese (By similarity).
SQ SEQUENCE 316 AA; 35343 MW; 730671BCA8747ED4 CRC64;
MKLAFILDPL DSIKIGKDSS YAMMCEAASR HHQLYTLQQS GLAWKNHQVI GFARSLTLID
PPDNPHRWYE EGVIEEIPLT EFDAVLMRKD PPFDTEYIYS TYLLELAERQ GAYVVNSPRG
IRDHNEKLAI TEFPQFIPSS LVTSQEQLIL QFLAEHKDII LKPLDGMGGA GIFRMQNTDH
NIGVIIETLT RYGTRTIMAQ RFLPEIREGD KRILLIAGKP VDYALARIPK PGETRGNLAV
GGTGKVQPLS ARDRKISEEL GQILYARGLM LIGLDVIGNH LTEINVTSPT GMREISDQTG
INVAGLMIDA LEQNIH
//