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Database: UniProt
Entry: Q5LYY5
LinkDB: Q5LYY5
Original site: Q5LYY5 
ID   GSHAB_STRT1             Reviewed;         754 AA.
AC   Q5LYY5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   13-FEB-2019, entry version 90.
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=str1413;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D.,
RA   Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D.,
RA   Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J.,
RA   Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy
RT   bacterium Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
CC   -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine
CC       via gamma-L-glutamyl-L-cysteine. {ECO:0000255|HAMAP-
CC       Rule:MF_00782}.
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}.
DR   EMBL; CP000024; AAV62950.1; -; Genomic_DNA.
DR   RefSeq; WP_011227399.1; NC_006449.1.
DR   ProteinModelPortal; Q5LYY5; -.
DR   SMR; Q5LYY5; -.
DR   PRIDE; Q5LYY5; -.
DR   EnsemblBacteria; AAV62950; AAV62950; str1413.
DR   GeneID; 31940331; -.
DR   KEGG; stc:str1413; -.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   OMA; EANFNPM; -.
DR   BioCyc; STHE299768:G1G42-1355-MONOMER; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
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   HAMAP; MF_00782; Glut_biosynth; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003806; ATP-grasp_PylC-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   PANTHER; PTHR38761; PTHR38761; 2.
DR   Pfam; PF02655; ATP-grasp_3; 1.
DR   Pfam; PF18419; ATP-grasp_6; 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    754       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192561.
FT   DOMAIN      488    746       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00782}.
FT   NP_BIND     515    573       ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   REGION        1    332       Glutamate--cysteine ligase.
FT   METAL       695    695       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       716    716       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       716    716       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       718    718       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
SQ   SEQUENCE   754 AA;  85137 MW;  83C856B2641FA2E3 CRC64;
     MTLNQLLQKL EATSPILQAN FGIERESLRV DRQGQLVHTP HPSCLGARSF HPYIQTDFCE
     FQMELITPVA KSTTEARRFL GAITDVAGRS IATDEVLWPL SMPPRLKAEE IQVAQLENDF
     ERHYRNYLAE KYGTKLQAIS GIHYNMELGK DLVEALFQES DQTDMIAFKN ALYLKLAQNY
     LRYRWVITYL FGASPIAEQG FFDQEVPEPM RSFRNSDHGY VNKEEIQVSF VSLEDYVSAI
     ETYIEQGDLI AEKEFYSAVR FRGQKVNRSF LDKGITYLEF RNFDLNPFER IGISQTTMDT
     VHLLILAFLW LDSPENVDQA LAQGHALNEK IALSHPLEPL PSEAKTQDIV TALDQLVQHF
     GLGDYHQDLV KQVKAAFADP NQTLSAQLLP YIKDKSLAEF ALNKALAYHD YDWTAHYALK
     GYEEMELSTQ MLLFDAIQKG IHFEILDEQD QFLKLWHQDH VEYVKNGNMT SKDNYVVPLA
     MANKTVTKKI LADAGFPVPS GDEFTSLEEG LAYYPLIKDK QIVVKPKSTN FGLGISIFQE
     PASLDNYQKA LEIAFAEDTS VLVEEFIPGT EYRFFILDGR CEAVLLRVAA NVIGDGKHTI
     RELVAQKNAN PLRGRDHRSP LEIIELGDIE QLMLAQQGYT PDDILPEGKK VNLRRNSNIS
     TGGDSIDVTE TMDSSYQELA AAMATSMGAW ACGVDLIIPD ETQIATKENP HCTCIELNFN
     PSMYMHTYCA EGPGQAITTK ILDKLFPEIV AGQT
//
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