ID B1V4R2_CLOPF Unreviewed; 778 AA.
AC B1V4R2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=CJD_2142 {ECO:0000313|EMBL:EDT71171.1};
OS Clostridium perfringens D str. JGS1721.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT71171.1, ECO:0000313|Proteomes:UP000003188};
RN [1] {ECO:0000313|EMBL:EDT71171.1, ECO:0000313|Proteomes:UP000003188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA Paulsen I., Sebastian Y.;
RL Submitted (MAR-2008) 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:EDT71171.1}.
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DR EMBL; ABOO01000027; EDT71171.1; -; Genomic_DNA.
DR RefSeq; WP_003475387.1; NZ_ABOO01000027.1.
DR AlphaFoldDB; B1V4R2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000003188; 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; 3.30.1490.20; 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; 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 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 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}.
FT DOMAIN 521..777
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..355
FT /note="Glutamate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00782"
SQ SEQUENCE 778 AA; 90537 MW; 65B12AAF75D78353 CRC64;
MVNLDKGLLK IIKDESLEDY FIKANFGLEK ENVRVTERGN LALTPHPKAF GDREKNAYIK
TDFSESQLEI VTPVCNTLEE VYSFICNLNK VVSLEIMKNG EFLWPQSNPP ILPREEEIPI
AKLSNREDEL YRENLSYKYG KKKQVISGIH YNFSFKEEFI KLLYKELKVE KDFREFKDDI
YLRMARNFQK YHWLLIYLTG ASPVFHESYI EEIKEEGEKL GEDSYYIKDD TSLRNSSYGY
KNKKDYYVSY NSIEEYASDI KNLVKDKEIQ SIKEYYNPIR LKSLGSEDML ESLLHKGIDY
LEVRLLDLDP LSIQGVSKET LYLVHLFMIY TLLKENKEIT YKDQEEFFKN HDMVALKGRN
EEVVIHENGV PVLLKDKGRE ILSEMDEIVE ILFSNNEEFK NVIKRALEKI NNPHDTISEK
LIKDIKEEGY INFHMRLAKE YLNNFKNKEF NLVGYEDLEL STQILILDAI KRGIEFNMMD
RLENFISLSD GEKVEYVKQA TKTSKDSYIT ALIMENKLVT KDILRENNIR VPKGKDYDNI
DEAKKDFRLF KDEKIVIKPK STNFGLGISI FPGEYLREDY DKAVEIAFRE DSSILIEEFM
TGKEYRFLVI GEEVVGILHR EPANVIGNGE STIEELVSEK NKDSLRGKGY KTPLEKIKLG
EIEEMFLKNQ GLSFKSIPKN GEKIYLRENS NISTGGDSID FTDKIHPSYK EVALKSAKAV
KALICGVDMV IDNIEEEAKE KNHGIIELNF NPAIHIHCFP YKGENRKAGE KILDLLFN
//
