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Database: UniProt
Entry: A2W768_9BURK
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Original site: A2W768_9BURK 
ID   A2W768_9BURK            Unreviewed;       318 AA.
AC   A2W768; A0A0D5J185;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 94.
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=BDAG_00507 {ECO:0000313|EMBL:EAY67814.1};
OS   Burkholderia dolosa AU0158.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY67814.1, ECO:0000313|Proteomes:UP000053482};
RN   [1] {ECO:0000313|Proteomes:UP000053482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA   Alvarado L., Lory S., LiPuma J.;
RT   "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       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; CH482380; EAY67814.1; -; Genomic_DNA.
DR   RefSeq; WP_006763309.1; NZ_CP009795.1.
DR   AlphaFoldDB; A2W768; -.
DR   GeneID; 64460038; -.
DR   PATRIC; fig|350701.8.peg.274; -.
DR   HOGENOM; CLU_068239_0_0_4; -.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000053482; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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   NCBIfam; TIGR01380; glut_syn; 1.
DR   PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00162};
KW   Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW   Rule:MF_00162};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00162};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00162}; Reference proteome {ECO:0000313|Proteomes:UP000053482}.
SQ   SEQUENCE   318 AA;  34880 MW;  20FD99FDCAE5AA3E CRC64;
     MDILFIADPL ERFKIYKDST YAMMAEAARR GHAVYACEPR HLAWTGSAVE ADVRRIAFVG
     DLDDLHRDTW FDAGPVDARR LESFGAVLMR KDPPFDMEYV TSTWLLELAE RAGARVFNNA
     QSIRDHSEKL AIGEFAQFVA PTLVTRDAAR LRAFHAEHGD VILKPLDGMG GMGVFRVKPD
     GMNLGSIIEM LSHDGTRTVM AQKFIPEIKD GDKRILLIGG EPVPYSLARI PQGSEVRGNL
     AAGGLGVAQP LTPRDREIAE TLGPVLASRG LLLVGLDAIG DWLTEVNVTS PTCFREIMEQ
     TGFDVAAMFI DALERAAA
//
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