GSHAB_LISIN
ID GSHAB_LISIN Reviewed; 769 AA.
AC Q926X7;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00782};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00782};
GN Name=gshAB {ECO:0000255|HAMAP-Rule:MF_00782};
GN Synonyms=gshF {ECO:0000255|HAMAP-Rule:MF_00782}; OrderedLocusNames=lin2913;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via
CC gamma-L-glutamyl-L-cysteine. {ECO:0000255|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:0000255|HAMAP-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:0000255|HAMAP-
CC Rule:MF_00782};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00782}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC98138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL596174; CAC98138.1; ALT_INIT; Genomic_DNA.
DR PIR; AB1796; AB1796.
DR RefSeq; WP_010991443.1; NC_003212.1.
DR AlphaFoldDB; Q926X7; -.
DR SMR; Q926X7; -.
DR STRING; 272626.lin2913; -.
DR EnsemblBacteria; CAC98138; CAC98138; CAC98138.
DR KEGG; lin:lin2913; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_1_0_9; -.
DR OrthoDB; 250578at2; -.
DR UniPathway; UPA00142; UER00209.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000002513; 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; 3.30.1490.20; -; 1.
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 InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding.
FT CHAIN 1..769
FT /note="Glutathione biosynthesis bifunctional protein GshAB"
FT /id="PRO_0000192553"
FT DOMAIN 514..768
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT REGION 1..347
FT /note="Glutamate--cysteine ligase"
FT BINDING 541..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 721
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 740
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 740
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
SQ SEQUENCE 769 AA; 87659 MW; 70EBC5926351E309 CRC64;
MLDSFKENEA LRKYLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES
QIEMITPVTD SIDAVYEWLE NLHNIVSLRA ENELLWPSSN PPILPAEEDI PIAEYKTPDS
PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYAE ISHPNESKRD FKNRLYLKVA
KYFMKNRWLL IYLTGASPVY LADFTKTNSE EVLNDGSKAL HRGISLRNSN AGYKNKESLF
VDYNSFDAYI SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAKHG VEYLEIRSID
LNPLEPNGIS KDELIFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN GLAQPAIKNC
DNEEMSLADA GLLELDKMSD FIQSLIPNDN HFQAIIEKQK ERLLHPEKTI AAQVQAQSAK
EGYVEFHLNQ AKTYMEETEA LAYKLVGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR
FQKGDHVEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH GIRVPFGDSF SDQALALEAF
SLFEDKQIVV KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF
LVINDKVEAV LKRVPANVTG DGIHTVRQLV EEKNTDPLRG TDHLKPLEKI RTGPEETLML
SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD YFKEIAIRAT QVLDAKICGV
DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEKKKIG DKILDFLFE
