ID A0A089LRD5_9BACL Unreviewed; 775 AA.
AC A0A089LRD5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=PSTEL_14510 {ECO:0000313|EMBL:AIQ64116.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ64116.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ64116.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ64116.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009286; AIQ64116.1; -; Genomic_DNA.
DR RefSeq; WP_038696150.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LRD5; -.
DR STRING; 169760.PSTEL_14510; -.
DR KEGG; pste:PSTEL_14510; -.
DR HOGENOM; CLU_020728_1_0_9; -.
DR OrthoDB; 9803907at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000029507; 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; 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; 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|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:UP000029507}.
FT DOMAIN 518..774
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..353
FT /note="Glutamate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00782"
SQ SEQUENCE 775 AA; 89468 MW; 712F29C34E7FDFF8 CRC64;
MNWLNRELVQ IVIDNALQDD LIRGRFGLEK ENVRVDQEGK LALTPHPKAF GSKTENPYIQ
TDFSESQIEM ITPALDSIEE TYHFMEALQD IVSLELEGEF LWPSSNPPML PEEEEIPIAK
MSDPVADDYR KELADKYGRK RQLLSGIHYN FSFDEKLLVR LYETQGHYKD FKEFKDTVYF
KVARNLLRYR WLLIYLTGAS PVFDNTYIEK CVNLADSLDK KSYYFPMMNS LRNSMCGYRN
EKLYYVSFNS ATEYVHDLNR LIQQNELLSV KEYYSPVRIK TSKGTNPVQD LVEEGVAYLE
LRFIDINPLH KIGISMEMMS FIHLFILFML LKVDESYNKE DQRIAAVNQD QVIMEGIKGF
LNESEYCQLT MEEMALSFIN EMKEMVELLF PGNEDYRKII DGEKQKILHS ELNAASIVKK
EIQESSFLTY HLDKAKKYAE ESIHNGYRFT GYEDLELSTQ LLLKAAVKRG IRFELMDREE
NFVLLSQGDH KEYVKQATKT ALDSYSTVLI MENKVVTKDI LNQHGIRVPS GETFQNLDEA
MSSYDTYRST PIVIKPKSTN FGLGITIFNR DYSREDMEKA FKIAFTHDKT VLLEEFITGK
EYRFLIMGDQ VVGVLHRVPA NVIGDGIHTI EQLVHEKNKN PLRGKGYKTP LEKIQLGEAE
EMFLKNHAMS WNDIPQLGEI IYLRENSNIS TGGDSIDFTD EIPNSYKDLA IQSAKAAGAT
ICGVDMMIDS IEEAANDTNY SIIELNFNPA IHIHCYPYIG KNRKADEKIL DLLFC
//
