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Database: UniProt
Entry: Q8DXM9
LinkDB: Q8DXM9
Original site: Q8DXM9 
ID   GSHAB_STRA5             Reviewed;         750 AA.
AC   Q8DXM9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 100.
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=SAG1821;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA   Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA   Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA   Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an
RT   emerging human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=15642737; DOI=10.1074/jbc.M414326200;
RA   Janowiak B.E., Griffith O.W.;
RT   "Glutathione synthesis in Streptococcus agalactiae. One protein
RT   accounts for gamma-glutamylcysteine synthetase and glutathione
RT   synthetase activities.";
RL   J. Biol. Chem. 280:11829-11839(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   -!- ACTIVITY REGULATION: Inhibited by L-buthionine-S-sulfoximine (L-S-
CC       BSO).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22 mM for L-glutamate;
CC         KM=156 uM for L-cysteine;
CC         KM=8.2 mM for alpha-L-aminobutyrate;
CC         KM=64 uM for ATP (in the reaction with gamma-GCS);
CC         KM=5.9 mM for gamma-L-glutamyl-L-cysteine;
CC         KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate;
CC         KM=6.3 mM for glycine;
CC         KM=420 uM for ATP (in the reaction with GS);
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:0000305}.
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; AE009948; AAN00684.1; -; Genomic_DNA.
DR   RefSeq; NP_688811.1; NC_004116.1.
DR   RefSeq; WP_000582678.1; NC_004116.1.
DR   PDB; 3LN6; X-ray; 2.95 A; A=1-750.
DR   PDBsum; 3LN6; -.
DR   ProteinModelPortal; Q8DXM9; -.
DR   SMR; Q8DXM9; -.
DR   EnsemblBacteria; AAN00684; AAN00684; SAG1821.
DR   GeneID; 1014630; -.
DR   KEGG; sag:SAG1821; -.
DR   PATRIC; fig|208435.3.peg.1829; -.
DR   HOGENOM; HOG000156471; -.
DR   KO; K01919; -.
DR   OMA; EANFNPM; -.
DR   BioCyc; SAGA208435:G1FZP-1919-MONOMER; -.
DR   BRENDA; 6.3.2.3; 5917.
DR   SABIO-RK; Q8DXM9; -.
DR   UniPathway; UPA00142; UER00209.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000000821; 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; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   PANTHER; PTHR38761; PTHR38761; 2.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
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   3D-structure; ATP-binding; Complete proteome;
KW   Glutathione biosynthesis; Ligase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    750       Glutathione biosynthesis bifunctional
FT                                protein GshAB.
FT                                /FTId=PRO_0000192559.
FT   DOMAIN      489    747       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00782}.
FT   NP_BIND     516    574       ATP. {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   REGION        1    333       Glutamate--cysteine ligase.
FT   METAL       696    696       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       717    717       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       717    717       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   METAL       719    719       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00782}.
FT   HELIX         7      9       {ECO:0000244|PDB:3LN6}.
FT   STRAND       19     31       {ECO:0000244|PDB:3LN6}.
FT   TURN         32     35       {ECO:0000244|PDB:3LN6}.
FT   STRAND       44     46       {ECO:0000244|PDB:3LN6}.
FT   TURN         49     51       {ECO:0000244|PDB:3LN6}.
FT   STRAND       53     67       {ECO:0000244|PDB:3LN6}.
FT   STRAND       71     73       {ECO:0000244|PDB:3LN6}.
FT   HELIX        74     91       {ECO:0000244|PDB:3LN6}.
FT   STRAND       96     98       {ECO:0000244|PDB:3LN6}.
FT   STRAND      101    103       {ECO:0000244|PDB:3LN6}.
FT   TURN        109    111       {ECO:0000244|PDB:3LN6}.
FT   HELIX       120    133       {ECO:0000244|PDB:3LN6}.
FT   HELIX       136    139       {ECO:0000244|PDB:3LN6}.
FT   STRAND      143    149       {ECO:0000244|PDB:3LN6}.
FT   HELIX       151    161       {ECO:0000244|PDB:3LN6}.
FT   HELIX       166    191       {ECO:0000244|PDB:3LN6}.
FT   STRAND      199    201       {ECO:0000244|PDB:3LN6}.
FT   TURN        206    208       {ECO:0000244|PDB:3LN6}.
FT   STRAND      212    214       {ECO:0000244|PDB:3LN6}.
FT   STRAND      217    221       {ECO:0000244|PDB:3LN6}.
FT   HELIX       234    243       {ECO:0000244|PDB:3LN6}.
FT   TURN        246    248       {ECO:0000244|PDB:3LN6}.
FT   HELIX       253    255       {ECO:0000244|PDB:3LN6}.
FT   STRAND      259    264       {ECO:0000244|PDB:3LN6}.
FT   TURN        268    274       {ECO:0000244|PDB:3LN6}.
FT   STRAND      278    281       {ECO:0000244|PDB:3LN6}.
FT   HELIX       296    311       {ECO:0000244|PDB:3LN6}.
FT   HELIX       318    334       {ECO:0000244|PDB:3LN6}.
FT   HELIX       347    361       {ECO:0000244|PDB:3LN6}.
FT   HELIX       365    379       {ECO:0000244|PDB:3LN6}.
FT   HELIX       381    383       {ECO:0000244|PDB:3LN6}.
FT   HELIX       385    392       {ECO:0000244|PDB:3LN6}.
FT   HELIX       399    413       {ECO:0000244|PDB:3LN6}.
FT   HELIX       421    423       {ECO:0000244|PDB:3LN6}.
FT   HELIX       428    440       {ECO:0000244|PDB:3LN6}.
FT   STRAND      443    447       {ECO:0000244|PDB:3LN6}.
FT   STRAND      449    451       {ECO:0000244|PDB:3LN6}.
FT   STRAND      453    458       {ECO:0000244|PDB:3LN6}.
FT   STRAND      461    466       {ECO:0000244|PDB:3LN6}.
FT   TURN        467    469       {ECO:0000244|PDB:3LN6}.
FT   HELIX       477    481       {ECO:0000244|PDB:3LN6}.
FT   TURN        482    484       {ECO:0000244|PDB:3LN6}.
FT   HELIX       486    494       {ECO:0000244|PDB:3LN6}.
FT   TURN        507    510       {ECO:0000244|PDB:3LN6}.
FT   HELIX       511    517       {ECO:0000244|PDB:3LN6}.
FT   STRAND      518    521       {ECO:0000244|PDB:3LN6}.
FT   STRAND      523    527       {ECO:0000244|PDB:3LN6}.
FT   STRAND      532    535       {ECO:0000244|PDB:3LN6}.
FT   STRAND      537    541       {ECO:0000244|PDB:3LN6}.
FT   HELIX       545    558       {ECO:0000244|PDB:3LN6}.
FT   STRAND      560    566       {ECO:0000244|PDB:3LN6}.
FT   STRAND      570    578       {ECO:0000244|PDB:3LN6}.
FT   STRAND      581    589       {ECO:0000244|PDB:3LN6}.
FT   STRAND      592    594       {ECO:0000244|PDB:3LN6}.
FT   HELIX       601    608       {ECO:0000244|PDB:3LN6}.
FT   STRAND      614    618       {ECO:0000244|PDB:3LN6}.
FT   STRAND      621    623       {ECO:0000244|PDB:3LN6}.
FT   HELIX       629    637       {ECO:0000244|PDB:3LN6}.
FT   STRAND      651    654       {ECO:0000244|PDB:3LN6}.
FT   TURN        660    663       {ECO:0000244|PDB:3LN6}.
FT   STRAND      665    668       {ECO:0000244|PDB:3LN6}.
FT   TURN        670    672       {ECO:0000244|PDB:3LN6}.
FT   HELIX       675    687       {ECO:0000244|PDB:3LN6}.
FT   STRAND      694    700       {ECO:0000244|PDB:3LN6}.
FT   STRAND      702    704       {ECO:0000244|PDB:3LN6}.
FT   TURN        708    711       {ECO:0000244|PDB:3LN6}.
FT   STRAND      714    721       {ECO:0000244|PDB:3LN6}.
FT   HELIX       725    728       {ECO:0000244|PDB:3LN6}.
FT   STRAND      731    733       {ECO:0000244|PDB:3LN6}.
FT   HELIX       739    746       {ECO:0000244|PDB:3LN6}.
SQ   SEQUENCE   750 AA;  85603 MW;  97829C2C5B44174A CRC64;
     MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN YHPYIQTDYS
     EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP LSMPPKVREE DIQIAQLEDA
     FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG QELLTSLFEL SQADNAIDFQ NQLYMKLSQN
     FLRYRWLLTY LYGASPVAEE DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND
     LENAVKSGQL IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
     TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL VDAMQSVIQH
     FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET FGQRQGQIYH DYAWEAPYAL
     KGYETMELST QLLLFDVIQK GVNFEVLDEQ DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL
     AMANKVVTKK ILDEKHFPTP FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK
     TSANLASYEK AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
     ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT KIELRRNSNI
     STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP NATQAYSKDK KNATCIELNF
     NPLMYMHTYC QEGPGQSITP RILAKLFPEL
//
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