(data stored in SCRATCH zone)

SWISSPROT: E6V4D0_VARPE

ID   E6V4D0_VARPE            Unreviewed;       317 AA.
AC   E6V4D0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=Varpa_0454 {ECO:0000313|EMBL:ADU34676.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34676.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34676.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34676.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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; CP002417; ADU34676.1; -; Genomic_DNA.
DR   RefSeq; WP_013538922.1; NC_014931.1.
DR   STRING; 595537.Varpa_0454; -.
DR   EnsemblBacteria; ADU34676; ADU34676; Varpa_0454.
DR   GeneID; 29720218; -.
DR   KEGG; vpe:Varpa_0454; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   OrthoDB; 878336at2; -.
DR   BioCyc; VPAR595537:G1GQO-455-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000008917; 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; E6V4D0.
DR   SWISS-2DPAGE; E6V4D0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000313|EMBL:ADU34676.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162,
KW   ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   DOMAIN      126    311       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   317 AA;  34957 MW;  6A601F2774E963FE CRC64;
     MKNILFVADP LDHFKIYKDT TFSMMREAQR RGHRIAACLP QDIQWKSGGL VTATVQQITL
     TGDAKDWYTV DITESKALKD FDAVLMRKDP PFDAEYIYST HLLQQAEREG AQVVNSPRAL
     RDHPEKLAIM EFPQFVTPTL VTRSAQAVRD FHAEHGDIIL KPLDGMGGMG IFRVKQDALN
     LGSIVETLNK DGAETIMVQR FVPEVSQGDK RILIIAGEPA PFVLARIPQG TEVRGNLAAG
     GKGVAQPLTP RNREIAEAIG KVLAPRGLLL IGLDVIGDSV TEINVTSPTC FQEITEQTGF
     DVPKMFIDAL EKTLRPA
//

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