ID A0A1I1ECK5_9SPHI Unreviewed; 332 AA.
AC A0A1I1ECK5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05421747_101467 {ECO:0000313|EMBL:SFB84322.1};
OS Parapedobacter composti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623281 {ECO:0000313|EMBL:SFB84322.1, ECO:0000313|Proteomes:UP000199577};
RN [1] {ECO:0000313|EMBL:SFB84322.1, ECO:0000313|Proteomes:UP000199577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22900 {ECO:0000313|EMBL:SFB84322.1,
RC ECO:0000313|Proteomes:UP000199577};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLL01000001; SFB84322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1ECK5; -.
DR STRING; 623281.SAMN05421747_101467; -.
DR OrthoDB; 9785415at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000199577; 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 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:UP000199577}.
FT DOMAIN 134..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 332 AA; 36987 MW; 806D67849CE1931C CRC64;
MTITFVVNQV GKESAGYTTT ALALEAHKRG HTVYYVGVGD LVYLSDGRLG GHCRRVPGRE
FRSLHTFLDA VLETEKKLVS SDKWDVLWLR NDPAADMEKR PWAQDAGMLF GQLASQQGIT
VLNSPEGLIK ASNKMYLQYF PESVRPRTVI TRNMADVEAF YREQNHRIIL KPLKGSGGKN
VFLIDKKDDK NRKQIVEAIC RDGFAIAQEY LPAAKKGDVR LFLMDGEPLM RNGKVAAIQR
VQQAGEIRSN IHQGGKAKPA GMTTEIETIV DAVGPLLRQD GMFLVGLDIV GDKLMEINVF
SPGGLIHASE FHGVDFMEEV ITAMERKVDK NR
//
