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Database: UniProt
Entry: Q8Y3R3
LinkDB: Q8Y3R3
Original site: Q8Y3R3 
ID   GSHAB_LISMO             Reviewed;         769 AA.
AC   Q8Y3R3;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   13-FEB-2019, entry version 98.
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};
GN   OrderedLocusNames=lmo2770;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=15901709; DOI=10.1128/JB.187.11.3839-3847.2005;
RA   Gopal S., Borovok I., Ofer A., Yanku M., Cohen G., Goebel W.,
RA   Kreft J., Aharonowitz Y.;
RT   "A multidomain fusion protein in Listeria monocytogenes catalyzes the
RT   two primary activities for glutathione biosynthesis.";
RL   J. Bacteriol. 187:3839-3847(2005).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
CC       via gamma-L-glutamyl-L-cysteine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = 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.
CC       {ECO:0000250};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC       from 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00782}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD00983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AL591984; CAD00983.1; ALT_INIT; Genomic_DNA.
DR   PIR; AI1420; AI1420.
DR   RefSeq; NP_466292.1; NC_003210.1.
DR   ProteinModelPortal; Q8Y3R3; -.
DR   SMR; Q8Y3R3; -.
DR   STRING; 169963.lmo2770; -.
DR   PaxDb; Q8Y3R3; -.
DR   EnsemblBacteria; CAD00983; CAD00983; CAD00983.
DR   GeneID; 986798; -.
DR   KEGG; lmo:lmo2770; -.
DR   PATRIC; fig|169963.11.peg.2839; -.
DR   eggNOG; ENOG4105D9M; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   eggNOG; COG2918; LUCA.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IBA:GO_Central.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IBA:GO_Central.
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; 2.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    769       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192555.
FT   DOMAIN      514    768       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00782}.
FT   NP_BIND     541    599       ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   REGION        1    347       Glutamate--cysteine ligase.
FT   METAL       721    721       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       738    738       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       738    738       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       740    740       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
SQ   SEQUENCE   769 AA;  87728 MW;  B60DA05A3D8B43FD CRC64;
     MLDSFKEDPN LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES
     QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN PPILPAEEDI PIAEYKTPDS
     PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYAN ISLPEESKQD FKNRLYLKVA
     KYFMKNRWLL IYLTGASPVY LADFSKTKHE ESLPDGSSAL RDGISLRNSN AGYKNKEALF
     VDYNSFDAYI SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID
     LNPLEPNGIS KDELDFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN GLAQPSIKNC
     DNEDIPLADA GLLELDKMSD FIKSLRPEDT KLRAIIEKQK ERLLHPEKTI AAQVKQQVTK
     EGYVDFHLNQ AKTYMEETEA LAYKLIGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR
     FQKGDHIEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF
     SLFEDKQIVV KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF
     LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI RTGPEETLML
     SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD YFKEIAIRAT QVLDAKICGV
     DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEQKKIG DKILDFLFD
//
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