(data stored in SCRATCH zone)

SWISSPROT: Q146C6_PARXL

ID   Q146C6_PARXL            Unreviewed;       318 AA.
AC   Q146C6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
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   ORFNames=Bxe_A4187 {ECO:0000313|EMBL:ABE28813.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28813.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28813.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28813.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE28813.1; -; Genomic_DNA.
DR   RefSeq; WP_011486652.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4187; -.
DR   EnsemblBacteria; ABE28813; ABE28813; Bxe_A4187.
DR   GeneID; 4002256; -.
DR   KEGG; bxb:DR64_1865; -.
DR   KEGG; bxe:Bxe_A4187; -.
DR   PATRIC; fig|266265.5.peg.290; -.
DR   eggNOG; ENOG4105D7Z; Bacteria.
DR   eggNOG; COG0189; LUCA.
DR   HOGENOM; HOG000265022; -.
DR   KO; K01920; -.
DR   OMA; WMRKDPP; -.
DR   OrthoDB; 878336at2; -.
DR   BioCyc; BXEN266265:BXE_RS01360-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q146C6.
DR   SWISS-2DPAGE; Q146C6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00162, ECO:0000313|EMBL:ABE28813.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162,
KW   ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN      129    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   318 AA;  34861 MW;  B6CDDA7B8AD6F440 CRC64;
     MDILFIADPL TQFKIYKDST YAMMAEAARR AHVVYTCEPQ HLAWTGGEVE ANVQRVEIVG
     DGADLQRDVW YSAEAAAPRS LRSFSAVVMR KDPPFDMEYV TSTWLLEMAE RAGARIFNKP
     QAIRDHSEKL AIGEFAQFVT PTLVTRDATR LRAFHEEHGD VILKPLDGMG GMGVFRVKAD
     GMNLGSIIEM LSHDGTRSVM AQKFIPEIKE GDKRILLIGG EAVPYSLARI PQGNEVRGNL
     AAGGLGMARP LTEHDRKIAA TLAPVLAARG LLLVGLDAIG DWLTEVNVTS PTCFREIMDQ
     TGFDVAAMFI DALERAAG
//

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