ID B0BR08_ACTPJ Unreviewed; 757 AA.
AC B0BR08;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=gshA {ECO:0000313|EMBL:ABY69993.1};
GN Synonyms=gshAB {ECO:0000256|HAMAP-Rule:MF_00782}, gshF
GN {ECO:0000256|HAMAP-Rule:MF_00782};
GN OrderedLocusNames=APJL_1439 {ECO:0000313|EMBL:ABY69993.1};
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271 {ECO:0000313|EMBL:ABY69993.1, ECO:0000313|Proteomes:UP000008547};
RN [1] {ECO:0000313|EMBL:ABY69993.1, ECO:0000313|Proteomes:UP000008547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03 {ECO:0000313|EMBL:ABY69993.1,
RC ECO:0000313|Proteomes:UP000008547};
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00008772}.
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}.
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DR EMBL; CP000687; ABY69993.1; -; Genomic_DNA.
DR RefSeq; WP_012263222.1; NC_010278.1.
DR AlphaFoldDB; B0BR08; -.
DR SMR; B0BR08; -.
DR KEGG; apj:APJL_1439; -.
DR HOGENOM; CLU_020728_1_0_6; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000008547; Chromosome.
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; 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 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}; Ligase {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 494..753
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..337
FT /note="Glutamate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00782"
SQ SEQUENCE 757 AA; 85384 MW; C13B124E7E70A8D0 CRC64;
MKLQQLIKTH HLGLLFQQGK FGIEKESQRI DNKGNIVTTA HPSVFGNRSY HPYIQTDFAE
SQLELITPPN DKLENTYRWL SAIHEVTLRS LPDDEYIFPF SMPAGLPPES EIKEAQLDNE
WDVKYREHLS AIYGKYKQMV SGIHYNFQIS DEFVESAFAL QTEYPNKIAF RNALYMKLAN
NFLRYQWILV YLLAATPTVE AQYFGENRPL AEGQLVRSLR SGPYGYVNAP HIVINHDSLQ
QYVESLEHFV ATGDLLAEKE FYSNVRLRGA KKARELLEKG VKYAEFRLFD LNPFSPYGIE
LADAKFIHLF LLAMLWMDET SGQREVEIGT QKLYQVALED PRSHTAFQAE GEAILNLMLA
MLDDLSVPQN EKDLLQQKLA QFADPSQTVN GRLLAAIEQA GSYKALGAQL AQQYKAQAFE
RFYAISAFDN MELSTQALLF DAIQQGLQIE LLDENDQFLA LKFGDHLEYV KNGNMTSHDQ
YISPLIMENK VVTKKVLAKA GFNVPKSIEF TSVEQAVAHY PLFEGKAMVI KPKSTNYGLG
ITIFQQGVTD KADFAKAIEI AFREDKEVMV EDYLVGTEYR FFVLGDETLA VLLRVPANVK
GDGIHTVREL VEAKNSDPLR GDGSRSPLKK IALGDIELLQ LKEQGLTPDS IPADGQIVQL
RANSNISTGG DSIDMTDQMH DSYKQLAVGI AKEMGAKVCG VDLIIPDLTK AAEPSLRSWG
VIEANFNPMM MMHIFPYQGK SRRLTKAVLK MLFPELP
//
