(data stored in SCRATCH zone)
SWISSPROT: A0A0E1NRQ0_YERPA
ID A0A0E1NRQ0_YERPA Unreviewed; 319 AA.
AC A0A0E1NRQ0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 13-FEB-2019, entry version 28.
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 Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00162};
DE Short=GSHase {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=YPA_0330 {ECO:0000313|EMBL:ABG12298.1};
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12298.1, ECO:0000313|Proteomes:UP000001971};
RN [1] {ECO:0000313|EMBL:ABG12298.1, ECO:0000313|Proteomes:UP000001971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua {ECO:0000313|EMBL:ABG12298.1,
RC ECO:0000313|Proteomes:UP000001971};
RX PubMed=16740952; DOI=10.1128/JB.00124-06;
RA Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and
RT Nepal516: evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; CP000308; ABG12298.1; -; Genomic_DNA.
DR RefSeq; WP_002209976.1; NZ_CP009906.1.
DR SMR; A0A0E1NRQ0; -.
DR EnsemblBacteria; ABG12298; ABG12298; YPA_0330.
DR EnsemblBacteria; AJJ79585; AJJ79585; CH58_3178.
DR KEGG; ypa:YPA_0330; -.
DR PATRIC; fig|360102.15.peg.3334; -.
DR KO; K01920; -.
DR OMA; WMRKDPP; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000001971; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_00162; GSH_S; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006284; Glut_synth_pro.
DR InterPro; IPR004218; GSHS_ATP-bd.
DR InterPro; IPR004215; GSHS_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR21621:SF4; PTHR21621:SF4; 1.
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;
DR PRODOM; A0A0E1NRQ0.
DR SWISS-2DPAGE; A0A0E1NRQ0.
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00162};
KW Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000313|EMBL:ABG12298.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162}.
SQ SEQUENCE 319 AA; 36015 MW; 4A26161F2A979AE6 CRC64;
MIKLGIVMDP ISSINIKKDT SFAMLLEAQR RGWELHYMEM GDLYMRGGDG RARTRRLNVK
QDKDNWFSFG AEQDLPLYDL DVILMRKDPP FDTEFIYATY ILERAEDKGT LVVNKPQSLR
DCNEKLFTAW FPELTPDTLV SRSKDHIRKF HQEHGDIILK PLDGMGGTSI FRVKQDDPNL
SVIIETLTEL SSRFCMAQNF LPAIKEGDKR VLVVDGEPVP YCLARIPAQG ETRGNLAAGG
RGEARPLSES DWEIARTVAP ILKQKGLIFV GLDIIGDRLT EINVTSPTCV REIEAAFPEI
SITGMLMDAI ERRLADKKA
//
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