GSHB_VIBPA
ID GSHB_VIBPA Reviewed; 316 AA.
AC Q87LK1;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=VP2611;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000031; BAC60874.1; -; Genomic_DNA.
DR RefSeq; NP_798990.1; NC_004603.1.
DR RefSeq; WP_005482451.1; NC_004603.1.
DR AlphaFoldDB; Q87LK1; -.
DR SMR; Q87LK1; -.
DR STRING; 223926.28807621; -.
DR EnsemblBacteria; BAC60874; BAC60874; BAC60874.
DR GeneID; 1190135; -.
DR KEGG; vpa:VP2611; -.
DR PATRIC; fig|223926.6.peg.2507; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_6; -.
DR OMA; WMRKDPP; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000002493; 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: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; Reference proteome.
FT CHAIN 1..316
FT /note="Glutathione synthetase"
FT /id="PRO_0000197492"
FT DOMAIN 124..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 150..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ SEQUENCE 316 AA; 35241 MW; B234FB14C99FB675 CRC64;
MIKLGIVMDP ISSINIKKDS SFAMMLEAQR RGYEIHYMEM NDLHLDQGKA IADTKVVELK
EDPNGWYEFK SEQMIELSEL DAVLMRKDPP FDTEYIYATY ILERAEEQGA LIVNKPQSLR
DCNEKLFTAW FPELTPTTIV TRKAEKIKAF REEHGDVILK PLDGMGGASI FRVKENDPNV
SVIIETLTNH GQNYAMAQTF VPDISNGDKR ILVVDGEPMP YCLARIPAKG ETRGNLAAGG
TGEARPLSET DMKIAQAVAP TLKEKGLIFV GLDVIGDKLT EINVTSPTCI REIEAAFDIS
ITGKLMDAIE RRVKGE
