ID F0J0T1_ACIMA Unreviewed; 317 AA.
AC F0J0T1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:BAJ81617.1};
GN OrderedLocusNames=ACMV_22700 {ECO:0000313|EMBL:BAJ81617.1};
GN ORFNames=Apmu_0139_13 {ECO:0000313|EMBL:GAN74136.1};
OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ81617.1, ECO:0000313|Proteomes:UP000007100};
RN [1] {ECO:0000313|EMBL:BAJ81617.1, ECO:0000313|Proteomes:UP000007100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ81617.1}, and DSM 11245 / JCM 8867
RC / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA Hosoyama A., Yamada R., Fujita N.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAN74136.1, ECO:0000313|Proteomes:UP000032662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN74136.1,
RC ECO:0000313|Proteomes:UP000032662};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (NOV-2012) 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; AP012035; BAJ81617.1; -; Genomic_DNA.
DR EMBL; BANA01000137; GAN74136.1; -; Genomic_DNA.
DR RefSeq; WP_013640495.1; NZ_BANA01000137.1.
DR AlphaFoldDB; F0J0T1; -.
DR KEGG; amv:ACMV_22700; -.
DR HOGENOM; CLU_068239_0_0_5; -.
DR OrthoDB; 9785415at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000007100; Chromosome.
DR Proteomes; UP000032662; 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}.
FT DOMAIN 126..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 317 AA; 35246 MW; CCD7CA554EF79EB1 CRC64;
MSGLRVAVQM DPMESVDIDG DSTFVLMLEA QRRGHALWHY TVRDMWLENG ALNARLRPVT
VRREAGNHFA FGPAETMDLA VMDVVLMRQD PPFDMGYITA THLLEHIHPR TLVVNDPAAV
RNAPEKLLVT DFPDLMPPTL IAWDRTAIRE FRARHKDIIV KPLYGNGGMG IFRIKPDDEN
LGALLDTHFA GSREPLMVQR YEPAVRAGDK RIILIDGEPL GAINRVPAEG DARSNMHAGG
IAAPTEMTAR DREICARIGP TLKERGLLFA GIDVIGDYLT EINVTSPTGL QQVARFNGLH
LEATIWDRIE ARRASGH
//
