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Q9EYW9

- DCEB_LISMO

UniProt

Q9EYW9 - DCEB_LISMO

Protein

Glutamate decarboxylase beta

Gene

gadB

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (21 Feb 2002)
      Previous versions | rss
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    Functioni

    Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance in gastric fluid.

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.By similarity

    GO - Molecular functioni

    1. glutamate decarboxylase activity Source: UniProtKB-EC
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. glutamate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciLMON169963:LMO2363-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase beta (EC:4.1.1.15)
    Short name:
    GAD-beta
    Gene namesi
    Name:gadB
    Ordered Locus Names:lmo2363
    OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
    Taxonomic identifieri169963 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000817: Chromosome

    Organism-specific databases

    GenoListiLMO2363.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Glutamate decarboxylase betaPRO_0000146990Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei275 – 2751N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Protein-protein interaction databases

    STRINGi169963.lmo2363.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EYW9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000070228.
    KOiK01580.
    OMAiPTFQINF.
    OrthoDBiEOG6TFCPW.
    PhylomeDBiQ9EYW9.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR010107. Glutamate_decarboxylase.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9EYW9-1 [UniParc]FASTAAdd to Basket

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    MLYSKENKES YLEPVFGSSA EDRDIPKYTL GKEPLEPRIA YRLVKDELLD    50
    EGSARQNLAT FCQTYMEDEA TKLMSETLEK NAIDKSEYPR TAELENRCVN 100
    IIADLWHAPK DQKFMGTSTI GSSEACMLGG MAMKFAWRKR AEKLGLDIYA 150
    KKPNLVISSG YQVCWEKFCV YWDIDMRVVP MDKEHMQLNT DQVLDYVDEY 200
    TIGVVGILGI TYTGRYDDIY ALNEKLEEYN SKTDYKVYIH VDAASGGFFT 250
    PFVEPDIIWD FRLKNVISIN TSGHKYGLVY PGIGWVLWKD ESYLPEELIF 300
    KVSYLGGEMP TMQINFSRSA SHIIGQYYNF LRYGFEGYRT IHQKTSDVAQ 350
    YLAHAVEQTG YFDIFNDGSH LPIVCYKLKD DANVNWTLYD LADRLQMRGW 400
    QVPAYPLPKS LENIIIQRYV CRADLGFNMA EEFIQDFQAS IQELNNAHIL 450
    FHDTQQSGVH GFTH 464
    Length:464
    Mass (Da):53,543
    Last modified:February 21, 2002 - v2
    Checksum:iF2E2778CFD1E2C36
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921A → P in strain: LO28.
    Natural varianti124 – 1241E → D in strain: LO28.
    Natural varianti261 – 2611F → L in strain: EGD5.
    Natural varianti375 – 3751C → R in strain: EGD5.
    Natural varianti380 – 3812DD → TT in strain: LO28.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309077 Genomic DNA. Translation: AAG22562.1.
    AF329447 Genomic DNA. Translation: AAK17187.1.
    AL591983 Genomic DNA. Translation: CAD00441.1.
    PIRiAC1370.
    RefSeqiNP_465886.1. NC_003210.1.

    Genome annotation databases

    EnsemblBacteriaiCAD00441; CAD00441; CAD00441.
    GeneIDi985123.
    KEGGilmo:lmo2363.
    PATRICi20313958. VBILisMon69206_2421.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309077 Genomic DNA. Translation: AAG22562.1 .
    AF329447 Genomic DNA. Translation: AAK17187.1 .
    AL591983 Genomic DNA. Translation: CAD00441.1 .
    PIRi AC1370.
    RefSeqi NP_465886.1. NC_003210.1.

    3D structure databases

    ProteinModelPortali Q9EYW9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 169963.lmo2363.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD00441 ; CAD00441 ; CAD00441 .
    GeneIDi 985123.
    KEGGi lmo:lmo2363.
    PATRICi 20313958. VBILisMon69206_2421.

    Organism-specific databases

    GenoListi LMO2363.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    KOi K01580.
    OMAi PTFQINF.
    OrthoDBi EOG6TFCPW.
    PhylomeDBi Q9EYW9.

    Enzyme and pathway databases

    BioCyci LMON169963:LMO2363-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR010107. Glutamate_decarboxylase.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11999:SF1. PTHR11999:SF1. 1 hit.
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid."
      Cotter P.D., Gahan C.G.M., Hill C.
      Mol. Microbiol. 40:465-475(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: EGD5 and LO28 / Serovar 1/2c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-679 / EGD-e.

    Entry informationi

    Entry nameiDCEB_LISMO
    AccessioniPrimary (citable) accession number: Q9EYW9
    Secondary accession number(s): Q8Y4S0, Q9AGQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2002
    Last sequence update: February 21, 2002
    Last modified: October 1, 2014
    This is version 78 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3