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Database: UniProt
Entry: Q6ANW2
LinkDB: Q6ANW2
Original site: Q6ANW2 
ID   GSHAB_DESPS             Reviewed;         779 AA.
AC   Q6ANW2;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   13-FEB-2019, entry version 85.
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=DP1233;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSv54 / DSM 12343;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M.,
RA   Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K.,
RA   Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R.,
RA   Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium
RT   from permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(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; CR522870; CAG35962.1; -; Genomic_DNA.
DR   RefSeq; WP_011188474.1; NC_006138.1.
DR   ProteinModelPortal; Q6ANW2; -.
DR   SMR; Q6ANW2; -.
DR   STRING; 177439.DP1233; -.
DR   PRIDE; Q6ANW2; -.
DR   EnsemblBacteria; CAG35962; CAG35962; DP1233.
DR   KEGG; dps:DP1233; -.
DR   eggNOG; ENOG4105D9M; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   eggNOG; COG2918; LUCA.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   OMA; EANFNPM; -.
DR   OrthoDB; 250578at2; -.
DR   BioCyc; DPSY177439:G1GHX-1246-MONOMER; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000602; 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   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   InterPro; IPR039523; RimK-rel_E_lig_ATP-grasp.
DR   PANTHER; PTHR38761; PTHR38761; 2.
DR   Pfam; PF18419; ATP-grasp_6; 1.
DR   Pfam; PF14397; ATPgrasp_ST; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW   Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    779       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192550.
FT   DOMAIN      512    768       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00782}.
FT   NP_BIND     539    597       ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   REGION        1    346       Glutamate--cysteine ligase.
FT   METAL       719    719       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   779 AA;  89336 MW;  1985FBD93F20889E CRC64;
     MAFSKNILDS LPPLISKQIF EGFFGFEKEN IRVDSRGKLA LTPHPRELGE KTSHPYITTD
     FSESQIEIIT PPLPSIAESL GFLETLHDLV SIELKDEYLW PQSAPPILPE REEDIPIAHF
     GGEFREQEEY RLQLAKIYGR KRQMFSGIHF NISLPERFLE LLHEEGKQEQ PFAEFREDIY
     MKTVRNFLRH RWFLICLLGA SPVIHKSYRK HCIDMLSPFA KDAYHFPYAT SIRNNICGYR
     NTQDFHLNYS TLTDYRESLQ ELVEKKVLRD IRENYAPIRI KTTTDPKRIN HLEIRLLDLN
     PFFKTGVNPL HAEIIHIFLI YCLLCPEETS FTSKEQETAN RNQEQAATEG LNPGAIICDA
     DGNEQRLDKQ LAHCLQEIQQ TVSPHLPPEY RAGMEELERL VQNQASRPTD TLLKEIKQEG
     FTEWHMKQAL KFLKKSHDEQ FIFHGLRDME LSTQLLLRRA ALRGVSFEIM DRQENFVCLE
     QAGKREYVMQ ASRTSLDNYI SVLSMENKVI TKKILDQAGI NTPKGRSYSS PSEALADYPY
     YRGRAIVIKP KSTNFGIGIT IIKENNRHDF FAQGIAQAFK HEATVLIENF SSGKEYRFFI
     VNDQVVGILH RVPANVTGDG TSSVQVLVTE KNKNPLRGRG YRTPLEKIKL EETEEMFLAS
     QGYSFATVPA KDQRIYLREN SNISTGGDSI DFTDKVPQSY KDIAVRAAQA LQVKITGLDM
     MIDSLEEDAA EDNFSIIELN FNPAIHIHCH PYIGKNRHLD DKILDALGFT GAEEAGEKA
//
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