ID A0A1V2YBN5_9FIRM Unreviewed; 771 AA.
AC A0A1V2YBN5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000256|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE Short=GCS-GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_00782};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_00782};
DE Short=GCS {ECO:0000256|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00782};
DE AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00782};
DE Short=GS {ECO:0000256|HAMAP-Rule:MF_00782};
DE Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00782};
DE Short=GSHase {ECO:0000256|HAMAP-Rule:MF_00782};
DE AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00782};
GN Name=gshAB {ECO:0000256|HAMAP-Rule:MF_00782};
GN Synonyms=gshF {ECO:0000256|HAMAP-Rule:MF_00782};
GN ORFNames=BEN19_02990 {ECO:0000313|EMBL:OOB76993.1};
OS Epulopiscium sp. Nuni2H_MBin003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884657 {ECO:0000313|EMBL:OOB76993.1, ECO:0000313|Proteomes:UP000189211};
RN [1] {ECO:0000313|EMBL:OOB76993.1, ECO:0000313|Proteomes:UP000189211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nuni2H_MBin003 {ECO:0000313|EMBL:OOB76993.1};
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via
CC gamma-L-glutamyl-L-cysteine. {ECO:0000256|HAMAP-Rule:MF_00782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_00782};
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_00782};
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 1/2. {ECO:0000256|ARBA:ARBA00005006,
CC ECO:0000256|HAMAP-Rule:MF_00782}.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
CC Rule:MF_00782}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00782}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glutamate--cysteine ligase type 1 family. Type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOB76993.1}.
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DR EMBL; MDJN01000194; OOB76993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YBN5; -.
DR STRING; 1884657.BEN19_02990; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000189211; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; 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; 3.30.590.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR HAMAP; MF_00782; Glut_biosynth; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006335; Glut_biosynth.
DR InterPro; IPR006334; Glut_cys_ligase.
DR InterPro; IPR040657; GshAB_ATP-grasp.
DR NCBIfam; TIGR01435; glu_cys_lig_rel; 1.
DR PANTHER; PTHR38761; GLUTAMATE--CYSTEINE LIGASE; 1.
DR PANTHER; PTHR38761:SF1; GLUTAMATE--CYSTEINE LIGASE; 1.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR Pfam; PF08443; RimK; 2.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00782, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW Rule:MF_00782};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00782};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00782};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00782, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000189211}.
FT DOMAIN 511..765
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..349
FT /note="Glutamate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00782"
SQ SEQUENCE 771 AA; 88280 MW; D5E51E83230DF606 CRC64;
MINILKDNFI PSELLEGNYG IEREGLRCTA EGVLVDTPHP AAFGSKLHNK YITADFSESQ
LEFITPILKN VDEVYDFLEN LYNIVSLEIG EEYIWPQSMP CALPEDGNIP VATFCKTPQG
EKAYCYRLHL LQKYGGKKQV VSGIHYNFSF SEKIIECLYK NSNTEHCYKT FRDNLYLKVA
RNYLRYRWLI IYLLGGSSVV HNTYEQGCID NLENVYNDTH SNKGALSYRN GECGYTNKYE
LYADYTNIDT YIKSIQTFVD NKKIDSPKEL YTQIRIKAYD NDDLLNSLKE KGINYLELRS
IDINPFDKTG IKKVDLDFLS VFNLFLLLKE ETEYKNYLVE ASENQYQIAK YGFYDMDLIK
DGEGIKKSAW AEEILSEVQK INSFLNLNQG VALLHQMEKI TNHKKTYAHM IFSQVKQHGY
IKAHMNLAKS YKKDAYNNRY LFKGYTDLEL STQQILKESV KRGINVQVID KEDNFIRLKD
ENHVEYIKQA TKTSQDTYIS MLIMENKIVT KKVLDENNIC TPSGDNITRT DNLQHILDKY
KNTAVVIKPK STNFGTGISI FKEPTTKEDI LNAINIAFKY DSSVLIEEFI SGKEYRLLVI
GQEVAAIVHR VPANVIGDGK RSIAELVEIK NTDPLRGVGY KTPLEKIKLD ANSALFLKQQ
QMTFESIPTD GQTVYLRENS NVSTGGDSID YTEQIANYFK EIAVKAAQSV GANICGVDMM
IEDVTAKNKS YSIIELNFNP AIHMHHYPYK GREINVAAKV LDLLGYECKN C
//
