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Q9ZPS3

- DCE4_ARATH

UniProt

Q9ZPS3 - DCE4_ARATH

Protein

Glutamate decarboxylase 4

Gene

GAD4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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:AT2G02010-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 4 (EC:4.1.1.15)
    Short name:
    GAD 4
    Gene namesi
    Name:GAD4
    Ordered Locus Names:At2g02010
    ORF Names:F14H20.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G02010.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. nucleus Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493Glutamate decarboxylase 4PRO_0000416955Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine1 Publication
    Modified residuei277 – 2771N6-(pyridoxal phosphate)lysineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9ZPS3.
    PRIDEiQ9ZPS3.

    Expressioni

    Tissue specificityi

    Expressed in flowers and shoots. Detected at low levels in siliques, stems, leaves and roots.1 Publication

    Inductioni

    Up-regulated by salt treatment and hypoxia.2 Publications

    Gene expression databases

    GenevestigatoriQ9ZPS3.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with clamodulin By similarity.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT2G02010.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZPS3.
    SMRiQ9ZPS3. Positions 12-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000070228.
    InParanoidiQ9ZPS3.
    KOiK01580.
    OMAiNAPKEMS.
    PhylomeDBiQ9ZPS3.

    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.

    Q9ZPS3-1 [UniParc]FASTAAdd to Basket

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    MVLSKTVSES DVSIHSTFAS RYVRNSLPRF EMPENSIPKE AAYQIINDEL    50
    MLDGNPRLNL ASFVTTWMEP ECDKLMMESI NKNYVDMDEY PVTTELQNRC 100
    VNMIARLFNA PLGDGEAAVG VGTVGSSEAI MLAGLAFKRQ WQNKRKAQGL 150
    PYDKPNIVTG ANVQVCWEKF ARYFEVELKE VNLREDYYVM DPVKAVEMVD 200
    ENTICVAAIL GSTLTGEFED VKLLNDLLVE KNKQTGWDTP IHVDAASGGF 250
    IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RTKTDLPDEL 300
    IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMDNCREN 350
    MMVLRQGLEK TGRFKIVSKE NGVPLVAFSL KDSSRHNEFE VAHTLRRFGW 400
    IVPAYTMPAD AQHVTVLRVV IREDFSRTLA ERLVADFEKV LHELDTLPAR 450
    VHAKMANGKV NGVKKTPEET QREVTAYWKK LLETKKTNKN TIC 493
    Length:493
    Mass (Da):56,005
    Last modified:May 1, 1999 - v1
    Checksum:i36B3FC93F2978168
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006532 Genomic DNA. Translation: AAD20099.1.
    CP002685 Genomic DNA. Translation: AEC05532.1.
    AF361836 mRNA. Translation: AAK32848.1.
    AY124860 mRNA. Translation: AAM70569.1.
    PIRiH84431.
    RefSeqiNP_178310.1. NM_126262.1.
    UniGeneiAt.28718.

    Genome annotation databases

    EnsemblPlantsiAT2G02010.1; AT2G02010.1; AT2G02010.
    GeneIDi814732.
    KEGGiath:AT2G02010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006532 Genomic DNA. Translation: AAD20099.1 .
    CP002685 Genomic DNA. Translation: AEC05532.1 .
    AF361836 mRNA. Translation: AAK32848.1 .
    AY124860 mRNA. Translation: AAM70569.1 .
    PIRi H84431.
    RefSeqi NP_178310.1. NM_126262.1.
    UniGenei At.28718.

    3D structure databases

    ProteinModelPortali Q9ZPS3.
    SMRi Q9ZPS3. Positions 12-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT2G02010.1-P.

    Proteomic databases

    PaxDbi Q9ZPS3.
    PRIDEi Q9ZPS3.

    Protocols and materials databases

    DNASUi 814732.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G02010.1 ; AT2G02010.1 ; AT2G02010 .
    GeneIDi 814732.
    KEGGi ath:AT2G02010.

    Organism-specific databases

    TAIRi AT2G02010.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    InParanoidi Q9ZPS3.
    KOi K01580.
    OMAi NAPKEMS.
    PhylomeDBi Q9ZPS3.

    Enzyme and pathway databases

    BioCyci ARA:AT2G02010-MONOMER.

    Gene expression databases

    Genevestigatori Q9ZPS3.

    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. 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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "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.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    6. "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, INDUCTION BY HYPOXIA.
    7. "The Arabidopsis pop2-1 mutant reveals the involvement of GABA transaminase in salt stress tolerance."
      Renault H., Roussel V., El Amrani A., Arzel M., Renault D., Bouchereau A., Deleu C.
      BMC Plant Biol. 10:20-20(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY SALT.

    Entry informationi

    Entry nameiDCE4_ARATH
    AccessioniPrimary (citable) accession number: Q9ZPS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2012
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 95 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