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Q83PR1

- DCEA_SHIFL

UniProt

Q83PR1 - DCEA_SHIFL

Protein

Glutamate decarboxylase alpha

Gene

gadA

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria By similarity.By similarity

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621SubstrateBy similarity
    Binding sitei83 – 831SubstrateBy similarity
    Binding sitei212 – 2121Pyridoxal phosphateBy similarity
    Binding sitei275 – 2751Pyridoxal phosphateBy 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase alpha (EC:4.1.1.15)
    Short name:
    GAD-alpha
    Gene namesi
    Name:gadA
    Ordered Locus Names:SF3594, S4173
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 466466Glutamate decarboxylase alphaPRO_0000146981Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiQ83PR1.
    PRIDEiQ83PR1.

    Expressioni

    Inductioni

    By acidic conditions. Expression is regulated by a complex system involving RpoS, cAMP, CRP, EvgAS, H-NS, GadE, GadW and GadX. The level of involvement for each regulator varies depending upon the growth phase and the medium By similarity.By similarity

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    STRINGi198214.SF3594.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83PR1.
    SMRiQ83PR1. Positions 4-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 1272Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000070228.
    KOiK01580.
    OrthoDBiEOG6TFCPW.

    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.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q83PR1-1 [UniParc]FASTAAdd to Basket

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    MDQKLLTDFR SELLDSRFGA KAISTIAESK RFPLHEMRDD VAFQIINDEL    50
    YLDGNARQNL ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC 100
    VNMVADLWHA PAPKNGQAVG TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK 150
    PTDKPNLVCG PVQICWHKFA RYWDVELREI PMRPGQLFMD PKRMIEACDE 200
    NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM HIDAASGGFL 250
    APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV 300
    FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA 350
    AYLADEIAKQ GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR 400
    LRGWQVPAFT LGGEATDIVV MRIMCRRGFE MDFAELLLED YKASLKYLSD 450
    HPKLQGIAQQ NSFKHT 466
    Length:466
    Mass (Da):52,700
    Last modified:January 4, 2005 - v2
    Checksum:i44B04876B2DF1680
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN45045.2.
    AE014073 Genomic DNA. Translation: AAP19142.1.
    RefSeqiNP_709338.2. NC_004337.2.
    NP_839331.1. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN45045; AAN45045; SF3594.
    AAP19142; AAP19142; S4173.
    GeneIDi1026324.
    1080379.
    KEGGisfl:SF3594.
    sfx:S4173.
    PATRICi18710286. VBIShiFle31049_4549.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN45045.2 .
    AE014073 Genomic DNA. Translation: AAP19142.1 .
    RefSeqi NP_709338.2. NC_004337.2.
    NP_839331.1. NC_004741.1.

    3D structure databases

    ProteinModelPortali Q83PR1.
    SMRi Q83PR1. Positions 4-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF3594.

    Proteomic databases

    PaxDbi Q83PR1.
    PRIDEi Q83PR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN45045 ; AAN45045 ; SF3594 .
    AAP19142 ; AAP19142 ; S4173 .
    GeneIDi 1026324.
    1080379.
    KEGGi sfl:SF3594.
    sfx:S4173.
    PATRICi 18710286. VBIShiFle31049_4549.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    KOi K01580.
    OrthoDBi EOG6TFCPW.

    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.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
    PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
      Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
      , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
      Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 301 / Serotype 2a.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiDCEA_SHIFL
    AccessioniPrimary (citable) accession number: Q83PR1
    Secondary accession number(s): Q7UAY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 72 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3