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Q9LSH2

- DCE5_ARATH

UniProt

Q9LSH2 - DCE5_ARATH

Protein

Glutamate decarboxylase 5

Gene

GAD5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the production of GABA. The calmodulin-binding is calcium-dependent and it is proposed that this may, directly or indirectly, form a calcium regulated control of GABA biosynthesis By similarity.By similarity

    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

    Calmodulin-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciARA:AT3G17760-MONOMER.
    ARA:GQT-2607-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 5 (EC:4.1.1.15)
    Short name:
    GAD 5
    Gene namesi
    Name:GAD5
    Ordered Locus Names:At3g17760
    ORF Names:MIG5.6
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G17760.

    Subcellular locationi

    GO - Cellular componenti

    1. plasmodesma Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Glutamate decarboxylase 5PRO_0000416956Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PRIDEiQ9LSH2.

    Expressioni

    Tissue specificityi

    Expressed in flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9LSH2.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with clamodulin By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9LSH2. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LSH2.
    SMRiQ9LSH2. Positions 13-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    InParanoidiQ9LSH2.
    KOiK01580.
    OMAiPTFQINF.
    PhylomeDBiQ9LSH2.

    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]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9LSH2-1 [UniParc]FASTAAdd to Basket

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    MVLATNSDSD EHLHSTFASR YVRAVVPRFK MPDHCMPKDA AYQVINDELM    50
    LDGNPRLNLA SFVTTWMEPE CDKLIMDSVN KNYVDMDEYP VTTELQNRCV 100
    NMIANLFHAP VGEDEAAIGC GTVGSSEAIM LAGLAFKRKW QHRRKAQGLP 150
    IDKPNIVTGA NVQVCWEKFA RYFEVELKEV KLSEDYYVMD PAKAVEMVDE 200
    NTICVAAILG STLTGEFEDV KQLNDLLAEK NAETGWETPI HVDAASGGFI 250
    APFLYPDLEW DFRLPWVKSI NVSGHKYGLV YAGVGWVVWR TKDDLPEELV 300
    FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ FIRLGFEGYK NIMENCMDNA 350
    RRLREGIEMT GKFNIVSKDI GVPLVAFSLK DSSKHTVFEI AESLRKFGWI 400
    IPAYTMPADA QHIAVLRVVI REDFSRGLAD RLITHIIQVL KEIEGLPSRI 450
    AHLAAAAAVS GDDEEVKVKT AKMSLEDITK YWKRLVEHKR NIVC 494
    Length:494
    Mass (Da):55,770
    Last modified:October 1, 2000 - v1
    Checksum:i7985F175E54DF262
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026646 Genomic DNA. Translation: BAB02870.1.
    CP002686 Genomic DNA. Translation: AEE76003.1.
    CP002686 Genomic DNA. Translation: AEE76004.1.
    RefSeqiNP_001154621.1. NM_001161149.1.
    NP_188403.1. NM_112657.1.
    UniGeneiAt.38660.

    Genome annotation databases

    EnsemblPlantsiAT3G17760.1; AT3G17760.1; AT3G17760.
    AT3G17760.2; AT3G17760.2; AT3G17760.
    GeneIDi821044.
    KEGGiath:AT3G17760.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026646 Genomic DNA. Translation: BAB02870.1 .
    CP002686 Genomic DNA. Translation: AEE76003.1 .
    CP002686 Genomic DNA. Translation: AEE76004.1 .
    RefSeqi NP_001154621.1. NM_001161149.1.
    NP_188403.1. NM_112657.1.
    UniGenei At.38660.

    3D structure databases

    ProteinModelPortali Q9LSH2.
    SMRi Q9LSH2. Positions 13-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9LSH2. 1 interaction.

    Proteomic databases

    PRIDEi Q9LSH2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G17760.1 ; AT3G17760.1 ; AT3G17760 .
    AT3G17760.2 ; AT3G17760.2 ; AT3G17760 .
    GeneIDi 821044.
    KEGGi ath:AT3G17760.

    Organism-specific databases

    TAIRi AT3G17760.

    Phylogenomic databases

    InParanoidi Q9LSH2.
    KOi K01580.
    OMAi PTFQINF.
    PhylomeDBi Q9LSH2.

    Enzyme and pathway databases

    BioCyci ARA:AT3G17760-MONOMER.
    ARA:GQT-2607-MONOMER.

    Gene expression databases

    Genevestigatori Q9LSH2.

    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 ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Metabolism and functions of gamma-aminobutyric acid."
      Shelp B.J., Bown A.W., McLean M.D.
      Trends Plant Sci. 4:446-452(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. "Contribution of the GABA shunt to hypoxia-induced alanine accumulation in roots of Arabidopsis thaliana."
      Miyashita Y., Good A.G.
      Plant Cell Physiol. 49:92-102(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDCE5_ARATH
    AccessioniPrimary (citable) accession number: Q9LSH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2012
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3