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Q42472

- DCE2_ARATH

UniProt

Q42472 - DCE2_ARATH

Protein

Glutamate decarboxylase 2

Gene

GAD2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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.1 Publication

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.

    Enzyme regulationi

    Up-regulatd by calmodulin binding at physiological pH.1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei488 – 4881Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomersBy similarity
    Sitei489 – 4891Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomersBy similarity

    GO - Molecular functioni

    1. glutamate decarboxylase activity Source: TAIR
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. glutamate metabolic process Source: TAIR
    2. nitrogen compound metabolic process Source: TAIR

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Calmodulin-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciARA:AT1G65960-MONOMER.
    ARA:GQT-2174-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 2 (EC:4.1.1.15)
    Short name:
    GAD 2
    Gene namesi
    Name:GAD2
    Synonyms:GDH2
    Ordered Locus Names:At1g65960
    ORF Names:F12P19.12
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G65960.

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Glutamate decarboxylase 2PRO_0000146974Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PaxDbiQ42472.
    PRIDEiQ42472.

    Expressioni

    Tissue specificityi

    Expressed in roots, inflorescence stems, flowers, siliques and leaves.3 Publications

    Inductioni

    Up-regulated by salt or nitrogen treatments. Down-regulated by hypoxia.3 Publications

    Gene expression databases

    ArrayExpressiQ42472.
    GenevestigatoriQ42472.

    Interactioni

    Subunit structurei

    Homohexamer By similarity. Interacts with calmodulin.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT1G65960.2-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ42472.
    SMRiQ42472. Positions 12-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni463 – 49432Calmodulin-bindingAdd
    BLAST

    Domaini

    The C-terminus (463-494) binds calmodulin in a calcium-dependent fashion.

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000070228.
    InParanoidiQ42472.
    KOiK01580.
    OMAiDEYALAH.
    PhylomeDBiQ42472.

    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.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q42472-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVLTKTATND ESVCTMFGSR YVRTTLPKYE IGENSIPKDA AYQIIKDELM    50
    LDGNPRLNLA SFVTTWMEPE CDKLIMDSIN KNYVDMDEYP VTTELQNRCV 100
    NIIARLFNAP LEESETAVGV GTVGSSEAIM LAGLAFKRKW QNKRKAEGKP 150
    YDKPNIVTGA NVQVCWEKFA RYFEVELKEV NLSEGYYVMD PDKAAEMVDE 200
    NTICVAAILG STLNGEFEDV KRLNDLLVKK NEETGWNTPI HVDAASGGFI 250
    APFIYPELEW DFRLPLVKSI NVSGHKYGLV YAGIGWVVWR AAEDLPEELI 300
    FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ LIRLGFEGYK NVMENCIENM 350
    VVLKEGIEKT ERFNIVSKDQ GVPVVAFSLK DHSFHNEFEI SEMLRRFGWI 400
    VPAYTMPADA QHITVLRVVI REDFSRTLAE RLVADISKVL HELDTLPSKI 450
    SKKMGIEGIA ENVKEKKMEK EILMEVIVGW RKFVKERKKM NGVC 494
    Length:494
    Mass (Da):56,141
    Last modified:November 1, 1997 - v1
    Checksum:i741E83A25DCBC48C
    GO

    Sequence cautioni

    The sequence AAL91148.1 differs from that shown. Reason: Frameshift at position 70.
    The sequence AAL91148.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101A → V in AAL16126. (PubMed:14593172)Curated
    Sequence conflicti461 – 4611E → K in AAL91148. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49937 mRNA. Translation: AAC31617.1.
    U46665 mRNA. Translation: AAC33485.1.
    AC009513 Genomic DNA. Translation: AAF06056.1.
    CP002684 Genomic DNA. Translation: AEE34445.1.
    AF428294 mRNA. Translation: AAL16126.1.
    AF428372 mRNA. Translation: AAL16302.1.
    AY124873 mRNA. Translation: AAM70582.1.
    AY081259 mRNA. Translation: AAL91148.1. Sequence problems.
    PIRiH96683.
    RefSeqiNP_001117556.1. NM_001124084.1. [Q42472-1]
    UniGeneiAt.19149.
    At.20543.
    At.24993.
    At.66846.

    Genome annotation databases

    EnsemblPlantsiAT1G65960.2; AT1G65960.2; AT1G65960. [Q42472-1]
    GeneIDi842908.
    KEGGiath:AT1G65960.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49937 mRNA. Translation: AAC31617.1 .
    U46665 mRNA. Translation: AAC33485.1 .
    AC009513 Genomic DNA. Translation: AAF06056.1 .
    CP002684 Genomic DNA. Translation: AEE34445.1 .
    AF428294 mRNA. Translation: AAL16126.1 .
    AF428372 mRNA. Translation: AAL16302.1 .
    AY124873 mRNA. Translation: AAM70582.1 .
    AY081259 mRNA. Translation: AAL91148.1 . Sequence problems.
    PIRi H96683.
    RefSeqi NP_001117556.1. NM_001124084.1. [Q42472-1 ]
    UniGenei At.19149.
    At.20543.
    At.24993.
    At.66846.

    3D structure databases

    ProteinModelPortali Q42472.
    SMRi Q42472. Positions 12-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G65960.2-P.

    Proteomic databases

    PaxDbi Q42472.
    PRIDEi Q42472.

    Protocols and materials databases

    DNASUi 842908.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G65960.2 ; AT1G65960.2 ; AT1G65960 . [Q42472-1 ]
    GeneIDi 842908.
    KEGGi ath:AT1G65960.

    Organism-specific databases

    TAIRi AT1G65960.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    InParanoidi Q42472.
    KOi K01580.
    OMAi DEYALAH.
    PhylomeDBi Q42472.

    Enzyme and pathway databases

    BioCyci ARA:AT1G65960-MONOMER.
    ARA:GQT-2174-MONOMER.

    Gene expression databases

    ArrayExpressi Q42472.
    Genevestigatori Q42472.

    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. "Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution."
      Zik M., Arazi T., Snedden W.A., Fromm H.
      Plant Mol. Biol. 37:967-975(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CLAMODULIN, TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis."
      Turano F.J., Thakkar S.S., Fang T., Weisemann J.M.
      Plant Physiol. 113:1329-1341(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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.
    6. "Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis."
      Turano F.J., Fang T.K.
      Plant Physiol. 117:1411-1421(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION BY NITROGEN.
    7. "The root-specific glutamate decarboxylase (GAD1) is essential for sustaining GABA levels in Arabidopsis."
      Bouche N., Fait A., Zik M., Fromm H.
      Plant Mol. Biol. 55:315-325(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: cv. Columbia.
    8. "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.
    9. "A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase."
      Gut H., Dominici P., Pilati S., Astegno A., Petoukhov M.V., Svergun D.I., Gruetter M.G., Capitani G.
      J. Mol. Biol. 392:334-351(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    10. "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 nameiDCE2_ARATH
    AccessioniPrimary (citable) accession number: Q42472
    Secondary accession number(s): Q8RXH0, Q944L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 99 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