ID A0A1H0MB34_9CLOT Unreviewed; 768 AA.
AC A0A1H0MB34;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, 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=SAMN04488529_101394 {ECO:0000313|EMBL:SDO77669.1};
OS Clostridium gasigenes.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=94869 {ECO:0000313|EMBL:SDO77669.1, ECO:0000313|Proteomes:UP000198597};
RN [1] {ECO:0000313|EMBL:SDO77669.1, ECO:0000313|Proteomes:UP000198597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12272 {ECO:0000313|EMBL:SDO77669.1,
RC ECO:0000313|Proteomes:UP000198597};
RA de Groot N.N.;
RL Submitted (OCT-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=L-cysteine + L-glutamate + ATP = gamma-L-glutamyl-L-cysteine +
CC ADP + phosphate + H(+); 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:ARBA00048819, ECO:0000256|HAMAP-
CC Rule:MF_00782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-L-glutamyl-L-cysteine + glycine + ATP = glutathione +
CC ADP + phosphate + H(+); Xref=Rhea:RHEA:13557, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.3;
CC Evidence={ECO:0000256|HAMAP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNJM01000001; SDO77669.1; -; Genomic_DNA.
DR RefSeq; WP_089965248.1; NZ_FNJM01000001.1.
DR AlphaFoldDB; A0A1H0MB34; -.
DR STRING; 94869.SAMN04488529_101394; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000198597; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
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 NCBIfam; NF002688; PRK02471.1; 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; 1.
DR Pfam; PF08443; RimK; 1.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00782};
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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00782}; Reference proteome {ECO:0000313|Proteomes:UP000198597}.
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 768 AA; 88858 MW; 945675B0722E5F6C CRC64;
MLHVLKTFRE NKEILKGTFG VEREGLRVDL CGNLSETKHP KLFGEKLSNP YITTDFSESQ
VELITPTFNS LEEVYDFLNS LYNITALELE DEYLWPQSMP CNIPDDENIP IADFSGEKEG
EKARDYREKL HKKYGGKKQL ISGIHYNFSF NEKIIRHLYD SENTNESYKA FRDNIYLKVV
RNYLRYRWFL IYILGGTAVI HESYAKECVK KLQEISTGSF TSEGALSYRN SECGYRNHID
LFPNYSTVNE YVNSIKTFVN DDVIESHKEL YSQIRLKARD NNDFLNSLSK DGIDYLEIRS
TDINPFDKAG ISLEDLKFIN IFTIFLLTEE ENNYSPWQEE ALYNQNIIAR FGQQNVMLRN
NGDQILKEKW ALNILNKIEE INKELNLDHE NIIGNVKARV LDPRLTYAYR ISEMVKENGY
INGHLELAKK YKKEAYKDRF KLYGYEDLEL STQILMKEAI KRGIKVELID RSENFISLSA
NNKVEYVKEA TKTSKDNYVS VLMMENKVVT KKILKENNIN VPRGEEYTSF EEGRRNAREF
SGKPIVIKPK STNFGIGISI FSKGADEEDI IDALKIAFKY DNTVLVEEFI KGKEYRFLVI
GDEVVGILHR VPANVLGNGK NTIEELVKIK NQSVLRGKGY KTPLEKIDLD ENAKLFLKQK
GLKFNYIPKL NEVVYLRENS NISTGGDSID YTDEIPKRFF DIAIEAAKAL KVNICGVDMI
IEDYKEENSN YGIIELNFNP AIHIHSYPYK GKERNVAEAL LKVLELIK
//
