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P04425

- GSHB_ECOLI

UniProt

P04425 - GSHB_ECOLI

Protein

Glutathione synthetase

Gene

gshB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi281 – 2811Magnesium or manganeseBy similarity
    Metal bindingi283 – 2831Magnesium or manganeseBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi151 – 20757ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutathione synthase activity Source: EcoCyc
    3. magnesium ion binding Source: EcoCyc
    4. manganese ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. glutathione biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUTATHIONE-SYN-MONOMER.
    ECOL316407:JW2914-MONOMER.
    MetaCyc:GLUTATHIONE-SYN-MONOMER.
    UniPathwayiUPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione synthetase (EC:6.3.2.3)
    Alternative name(s):
    GSH synthetase
    Short name:
    GSH-S
    Short name:
    GSHase
    Glutathione synthase
    Gene namesi
    Name:gshB
    Synonyms:gsh-II
    Ordered Locus Names:b2947, JW2914
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10419. gshB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221C → A: No loss of activity. 1 Publication
    Mutagenesisi195 – 1951C → A: No loss of activity. 1 Publication
    Mutagenesisi222 – 2221C → A: No loss of activity. 1 Publication
    Mutagenesisi227 – 2271P → V: Loss of activity. 2 Publications
    Mutagenesisi233 – 2331R → A or K: Loss of activity. 2 Publications
    Mutagenesisi240 – 2401G → V: Loss of activity. 2 Publications
    Mutagenesisi241 – 2411R → A or K: No loss of activity. 2 Publications
    Mutagenesisi289 – 2891C → A: No loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Glutathione synthetasePRO_0000197465Add
    BLAST

    Proteomic databases

    PaxDbiP04425.
    PRIDEiP04425.

    Expressioni

    Gene expression databases

    GenevestigatoriP04425.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mapP0AE181EBI-909107,EBI-553355
    nadEP188431EBI-909107,EBI-548960

    Protein-protein interaction databases

    DIPiDIP-9840N.
    IntActiP04425. 5 interactions.
    STRINGi511145.b2947.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Helixi11 – 133
    Turni16 – 183
    Helixi20 – 3011
    Beta strandi34 – 385
    Helixi40 – 423
    Beta strandi43 – 464
    Beta strandi49 – 5911
    Beta strandi67 – 7610
    Helixi77 – 793
    Beta strandi80 – 856
    Helixi93 – 10715
    Beta strandi111 – 1144
    Helixi116 – 1216
    Helixi126 – 1316
    Turni132 – 1343
    Beta strandi138 – 1425
    Helixi144 – 15411
    Beta strandi155 – 1606
    Turni166 – 1694
    Beta strandi171 – 1733
    Helixi180 – 1878
    Turni188 – 1925
    Beta strandi195 – 1995
    Helixi202 – 2065
    Beta strandi208 – 2147
    Beta strandi220 – 2267
    Helixi236 – 2383
    Beta strandi241 – 2466
    Helixi249 – 26416
    Beta strandi269 – 2757
    Beta strandi278 – 2836
    Helixi290 – 2967
    Helixi301 – 31212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GLVX-ray2.70A1-316[»]
    1GSAX-ray2.00A1-316[»]
    1GSHX-ray2.00A1-316[»]
    2GLTX-ray2.20A1-316[»]
    ProteinModelPortaliP04425.
    SMRiP04425. Positions 1-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04425.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 310186ATP-graspAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prokaryotic GSH synthase family.Curated
    Contains 1 ATP-grasp domain.Curated

    Phylogenomic databases

    eggNOGiCOG0189.
    HOGENOMiHOG000265022.
    KOiK01920.
    OMAiDWKIARA.
    OrthoDBiEOG6WMHWB.
    PhylomeDBiP04425.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    HAMAPiMF_00162. GSH_S.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006284. Glut_synth_pro.
    IPR004218. GSHS_ATP-bd.
    IPR004215. GSHS_N.
    IPR016185. PreATP-grasp_dom.
    [Graphical view]
    PfamiPF02955. GSH-S_ATP. 1 hit.
    PF02951. GSH-S_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01380. glut_syn. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04425-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKLGIVMDP IANINIKKDS SFAMLLEAQR RGYELHYMEM GDLYLINGEA    50
    RAHTRTLNVK QNYEEWFSFV GEQDLPLADL DVILMRKDPP FDTEFIYATY 100
    ILERAEEKGT LIVNKPQSLR DCNEKLFTAW FSDLTPETLV TRNKAQLKAF 150
    WEKHSDIILK PLDGMGGASI FRVKEGDPNL GVIAETLTEH GTRYCMAQNY 200
    LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG RGEPRPLTES 250
    DWKIARQIGP TLKEKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPVS 300
    ITGMLMDAIE ARLQQQ 316
    Length:316
    Mass (Da):35,561
    Last modified:August 13, 1987 - v1
    Checksum:iF2E67AB29DE113DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01666 Genomic DNA. Translation: CAA25826.1.
    U28377 Genomic DNA. Translation: AAA69114.1.
    U00096 Genomic DNA. Translation: AAC75984.1.
    AP009048 Genomic DNA. Translation: BAE77010.1.
    PIRiA01194. SYECGS.
    RefSeqiNP_417422.1. NC_000913.3.
    YP_491146.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75984; AAC75984; b2947.
    BAE77010; BAE77010; BAE77010.
    GeneIDi12930412.
    947445.
    KEGGiecj:Y75_p2877.
    eco:b2947.
    PATRICi32121304. VBIEscCol129921_3040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01666 Genomic DNA. Translation: CAA25826.1 .
    U28377 Genomic DNA. Translation: AAA69114.1 .
    U00096 Genomic DNA. Translation: AAC75984.1 .
    AP009048 Genomic DNA. Translation: BAE77010.1 .
    PIRi A01194. SYECGS.
    RefSeqi NP_417422.1. NC_000913.3.
    YP_491146.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GLV X-ray 2.70 A 1-316 [» ]
    1GSA X-ray 2.00 A 1-316 [» ]
    1GSH X-ray 2.00 A 1-316 [» ]
    2GLT X-ray 2.20 A 1-316 [» ]
    ProteinModelPortali P04425.
    SMRi P04425. Positions 1-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9840N.
    IntActi P04425. 5 interactions.
    STRINGi 511145.b2947.

    Proteomic databases

    PaxDbi P04425.
    PRIDEi P04425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75984 ; AAC75984 ; b2947 .
    BAE77010 ; BAE77010 ; BAE77010 .
    GeneIDi 12930412.
    947445.
    KEGGi ecj:Y75_p2877.
    eco:b2947.
    PATRICi 32121304. VBIEscCol129921_3040.

    Organism-specific databases

    EchoBASEi EB0414.
    EcoGenei EG10419. gshB.

    Phylogenomic databases

    eggNOGi COG0189.
    HOGENOMi HOG000265022.
    KOi K01920.
    OMAi DWKIARA.
    OrthoDBi EOG6WMHWB.
    PhylomeDBi P04425.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00210 .
    BioCyci EcoCyc:GLUTATHIONE-SYN-MONOMER.
    ECOL316407:JW2914-MONOMER.
    MetaCyc:GLUTATHIONE-SYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04425.
    PROi P04425.

    Gene expression databases

    Genevestigatori P04425.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    HAMAPi MF_00162. GSH_S.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006284. Glut_synth_pro.
    IPR004218. GSHS_ATP-bd.
    IPR004215. GSHS_N.
    IPR016185. PreATP-grasp_dom.
    [Graphical view ]
    Pfami PF02955. GSH-S_ATP. 1 hit.
    PF02951. GSH-S_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01380. glut_syn. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II."
      Gushima H., Yasuda S., Soeda E., Yokota M., Kondo M., Kimura A.
      Nucleic Acids Res. 12:9299-9307(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0-A resolution."
      Yamaguchi H., Kato H., Hata Y., Nishioka T., Kimura A., Oda J., Katsube Y.
      J. Mol. Biol. 229:1083-1100(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: B.
    5. "Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins."
      Matsuda K., Mizuguchi K., Nishioka T., Kato H., Go N., Oda J.
      Protein Eng. 9:1083-1092(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: B.
    6. "Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase."
      Tanaka T., Yamaguchi H., Kato H., Nishioka T., Katsube Y., Oda J.
      Biochemistry 32:12398-12404(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-227 AND GLY-240.
    7. "Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction."
      Tanaka T., Kato H., Nishioka T., Oda J.
      Biochemistry 31:2259-2265(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 234-242, MUTAGENESIS OF ARG-233 AND ARG-241.
      Strain: B.
    8. "Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis."
      Kato H., Tanaka T., Nishioka T., Kimura A., Oda J.
      J. Biol. Chem. 263:11646-11651(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYSTEINE RESIDUES.
      Strain: B.

    Entry informationi

    Entry nameiGSHB_ECOLI
    AccessioniPrimary (citable) accession number: P04425
    Secondary accession number(s): Q2M9P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3