GSHB_BORBR
ID GSHB_BORBR Reviewed; 318 AA.
AC Q7WKF5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
DE AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162}; Synonyms=gsh-II;
GN OrderedLocusNames=BB2152;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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:0000255|HAMAP-
CC Rule:MF_00162};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00162}.
CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00162}.
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DR EMBL; BX640443; CAE32648.1; -; Genomic_DNA.
DR RefSeq; WP_003812603.1; NC_002927.3.
DR AlphaFoldDB; Q7WKF5; -.
DR SMR; Q7WKF5; -.
DR STRING; 257310.BB2152; -.
DR EnsemblBacteria; CAE32648; CAE32648; BB2152.
DR GeneID; 56478327; -.
DR KEGG; bbr:BB2152; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_4; -.
DR OMA; WMRKDPP; -.
DR OrthoDB; 878336at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000001027; 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:UniProtKB-KW.
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;
KW ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..318
FT /note="Glutathione synthetase"
FT /id="PRO_0000197453"
FT DOMAIN 129..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 155..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ SEQUENCE 318 AA; 34652 MW; 5902082AD5DC4F97 CRC64;
MHVLFIIDPL PLLKAYKDSS VAMMQALQAR GHTLSVALQG DLYIDAGEVR TRFAPIALRD
GADLHGHDWW RETGAADEAP LARFDAVVMR KDPPFDMEYV YSTHLLEYAQ QQGARVFNSG
AAIRNHPEKL AITEFPDLTT PTLVTRDMGR IRAFHAAQGD VIVKPLDGMG GTGIFRLQRS
EPNLNAILET LTDNGTRTIM AQRYIPEIVK GDKRILLIGG EPVPYSLARI PLAGETRGNL
AAGGRGVAQP LSERDLHLAR TVADRLAGRG LLLVGLDVIG DYITEVNVTS PTCFVEITEQ
TGFNVPEMFA VALESAAG
