(data stored in SCRATCH zone)

SWISSPROT: C5BCS2_EDWI9

ID   C5BCS2_EDWI9            Unreviewed;       316 AA.
AC   C5BCS2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=NT01EI_0286 {ECO:0000313|EMBL:ACR67528.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67528.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67528.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67528.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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; CP001600; ACR67528.1; -; Genomic_DNA.
DR   RefSeq; WP_015869737.1; NC_012779.2.
DR   EnsemblBacteria; ACR67528; ACR67528; NT01EI_0286.
DR   GeneID; 7960066; -.
DR   KEGG; eic:NT01EI_0286; -.
DR   PATRIC; fig|634503.3.peg.258; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   OrthoDB; 878336at2; -.
DR   BioCyc; EICT634503:G1GVC-265-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000001485; 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; C5BCS2.
DR   SWISS-2DPAGE; C5BCS2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000313|EMBL:ACR67528.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162,
KW   ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      125    310       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   316 AA;  35268 MW;  AD8A3BC659714801 CRC64;
     MIKLGIVMDP IASINIKKDT SFAMLLEAQH RDYQLHYMEM SDLYLQQGEA RAQTRLLSVS
     DDKTSWYRFD GEQDIALADL DVILMRKDPP FDTEFIYATY ILERAEARGT LIVNKPQSLR
     DCNEKLFTAW FADLTPDTLV TRSAAHLRDF HARHGDIILK PLDGMGGASI FRIQQDDPNL
     SVIIETLTEH GKRFCMAQNY LPAIVDGDKR VLVVDGEPVP YCLARIPKSG ETRGNLAAGG
     RGEARPLSES DWAIARKVAP MLKEKGLIFV GLDIIGDRLT EINVTSPTCA REIEAAFPVS
     ITGMLMDAIE ARLAAR
//

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