ID   Q6F702_ACIAD            Unreviewed;       314 AA.
AC   Q6F702;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 139.
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   ECO:0000313|EMBL:CAG70163.1};
GN   OrderedLocusNames=ACIAD3518 {ECO:0000313|EMBL:CAG70163.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG70163.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG70163.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG70163.1; -; Genomic_DNA.
DR   RefSeq; WP_004923332.1; NC_005966.1.
DR   AlphaFoldDB; Q6F702; -.
DR   STRING; 202950.GCA_001485005_01693; -.
DR   GeneID; 45235696; -.
DR   KEGG; aci:ACIAD3518; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_068239_0_0_6; -.
DR   OrthoDB; 9785415at2; -.
DR   BioCyc; ASP62977:ACIAD_RS15910-MONOMER; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000430; 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; 3.40.50.20; -; 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:UP000000430}.
FT   DOMAIN          123..309
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   314 AA;  35298 MW;  67AD06369AED36EB CRC64;
     MRVLVVMDPI ENVNLKKDST MAMLWAASRR GHELGYALQH DLYIDQGRAF GLISPLKVFE
     DYQHYYELGN KQKESLADYD VILMRKDPPF DMNFVYTTYI LEQAEREGAW IINKPQSLRD
     CNEKLFATQF PELQVPTLVT SQQSLIREFI QEHGDVIVKP LDGMGGMGIF RLYQDGVNIG
     STLEMLTEMG TCPIMAQRYI PEIVEGDKRI LMVNGEPIPY CLARIPQNGE VRGNLAAGGL
     GEARPLTEND KMIAAKVGPY LRDKGLVFVG LDVIGNYVTE INVTSPTCIR EIDAQFGTSI
     ADTLFDVLEA GRQH
//