Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q42521

- DCE1_ARATH

UniProt

Q42521 - DCE1_ARATH

Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    Sitei496 – 4961Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers
    Sitei497 – 4971Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamate metabolic process Source: InterPro
    2. response to cadmium ion Source: TAIR

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Calmodulin-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciARA:AT5G17330-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 1 (EC:4.1.1.15)
    Short name:
    GAD 1
    Gene namesi
    Name:GAD1
    Synonyms:GAD, GDH1
    Ordered Locus Names:At5g17330
    ORF Names:MKP11.30, MKP11_18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G17330.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype, but increased glutamate levels and decreased GABA levels in the roots, and loss of GABA accumulation upon heat stress.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi474 – 4752KK → AA: No effect.
    Mutagenesisi489 – 4902KK → AA: No effect.
    Mutagenesisi496 – 4961K → A: Decreased activity. When associated with A-497; threefold decreased activity, but still pH-dependent. 1 Publication
    Mutagenesisi497 – 4971K → A: Decreased activity. When associated with A-496; threefold decreased activity, but still pH-dependent. 1 Publication
    Mutagenesisi502 – 5021C → A: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 502502Glutamate decarboxylase 1PRO_0000146973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei277 – 2771N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ42521.
    PRIDEiQ42521.

    Expressioni

    Tissue specificityi

    Expressed in roots. Detected at low levels in shoots of young seedlings. Not detected in the root tips or in the central vascular bundle in the elongating region of mature roots.4 Publications

    Inductioni

    Down-regulated by salt treatment. Not induced by hypoxia.2 Publications

    Gene expression databases

    GenevestigatoriQ42521.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with clamodulin with a 1:3 stoichiometry.3 Publications

    Protein-protein interaction databases

    BioGridi16875. 1 interaction.
    MINTiMINT-8062431.
    STRINGi3702.AT5G17330.1-P.

    Structurei

    Secondary structure

    1
    502
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni17 – 193
    Helixi22 – 243
    Beta strandi29 – 313
    Helixi39 – 4911
    Helixi50 – 523
    Helixi56 – 583
    Helixi70 – 789
    Turni79 – 813
    Turni87 – 893
    Helixi91 – 10717
    Beta strandi119 – 1257
    Helixi126 – 14722
    Beta strandi156 – 1605
    Helixi165 – 1739
    Beta strandi177 – 1815
    Helixi192 – 1987
    Beta strandi203 – 2119
    Turni213 – 2153
    Helixi221 – 23515
    Beta strandi241 – 2444
    Helixi248 – 2503
    Helixi252 – 2554
    Beta strandi268 – 2747
    Turni275 – 2795
    Beta strandi286 – 2927
    Helixi293 – 2953
    Helixi298 – 3003
    Beta strandi302 – 3043
    Beta strandi306 – 3094
    Beta strandi311 – 3133
    Helixi323 – 35937
    Turni360 – 3623
    Beta strandi364 – 3663
    Beta strandi370 – 38213
    Helixi388 – 3969
    Turni397 – 3993
    Beta strandi404 – 4063
    Beta strandi415 – 4206
    Helixi427 – 44519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HBXX-ray2.67A/B/C/D/E/F1-502[»]
    ProteinModelPortaliQ42521.
    SMRiQ42521. Positions 12-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ42521.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni469 – 50234Calmodulin-bindingAdd
    BLAST

    Domaini

    The N-terminus (1-57) is involved in the formation of the multimer. The C-terminus (471-502) binds calmodulin in a calcium-dependent fashion and contains probably an autoinhibitory domain.

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000070228.
    InParanoidiQ42521.
    KOiK01580.
    OMAiCVRILAN.
    PhylomeDBiQ42521.

    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.

    Q42521-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLSHAVSES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL    50
    MLDGNPRLNL ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC 100
    VNMIAHLFNA PLEEAETAVG VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK 150
    PVDKPNIVTG ANVQVCWEKF ARYFEVELKE VKLSEGYYVM DPQQAVDMVD 200
    ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP IHVDAASGGF 250
    IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL 300
    IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY RNVMENCREN 350
    MIVLREGLEK TERFNIVSKD EGVPLVAFSL KDSSCHTEFE ISDMLRRYGW 400
    IVPAYTMPPN AQHITVLRVV IREDFSRTLA ERLVIDIEKV MRELDELPSR 450
    VIHKISLGQE KSESNSDNLM VTVKKSDIDK QRDIITGWKK FVADRKKTSG 500
    IC 502
    Length:502
    Mass (Da):57,066
    Last modified:May 27, 2002 - v2
    Checksum:i4E8141FF523E0E22
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081A → D in AAA93132. (PubMed:7610159)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10034 mRNA. Translation: AAA93132.1.
    AB005238 Genomic DNA. Translation: BAB10520.1.
    CP002688 Genomic DNA. Translation: AED92414.1.
    AY094464 mRNA. Translation: AAM19834.1.
    BT001047 mRNA. Translation: AAN46801.1.
    RefSeqiNP_197235.1. NM_121739.3.
    UniGeneiAt.25228.

    Genome annotation databases

    EnsemblPlantsiAT5G17330.1; AT5G17330.1; AT5G17330.
    GeneIDi831599.
    KEGGiath:AT5G17330.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10034 mRNA. Translation: AAA93132.1 .
    AB005238 Genomic DNA. Translation: BAB10520.1 .
    CP002688 Genomic DNA. Translation: AED92414.1 .
    AY094464 mRNA. Translation: AAM19834.1 .
    BT001047 mRNA. Translation: AAN46801.1 .
    RefSeqi NP_197235.1. NM_121739.3.
    UniGenei At.25228.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HBX X-ray 2.67 A/B/C/D/E/F 1-502 [» ]
    ProteinModelPortali Q42521.
    SMRi Q42521. Positions 12-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16875. 1 interaction.
    MINTi MINT-8062431.
    STRINGi 3702.AT5G17330.1-P.

    Proteomic databases

    PaxDbi Q42521.
    PRIDEi Q42521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G17330.1 ; AT5G17330.1 ; AT5G17330 .
    GeneIDi 831599.
    KEGGi ath:AT5G17330.

    Organism-specific databases

    TAIRi AT5G17330.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    InParanoidi Q42521.
    KOi K01580.
    OMAi CVRILAN.
    PhylomeDBi Q42521.

    Enzyme and pathway databases

    BioCyci ARA:AT5G17330-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q42521.

    Gene expression databases

    Genevestigatori Q42521.

    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. "Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase."
      Arazi T., Baum G., Snedden W.A., Shelp B.J., Fromm H.
      Plant Physiol. 108:551-561(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CALMODULIN.
      Strain: cv. Columbia.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
      Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
      DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.
    5. "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: FUNCTION, INTERACTION WITH CLAMODULIN, TISSUE SPECIFICITY.
      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.
    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: TISSUE SPECIFICITY, 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, DISRUPTION PHENOTYPE.
    9. "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.
    10. "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: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS), SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF 474-LYS-LYS-475; 489-LYS-LYS-490; LYS-496; LYS-497 AND CYS-502.

    Entry informationi

    Entry nameiDCE1_ARATH
    AccessioniPrimary (citable) accession number: Q42521
    Secondary accession number(s): Q9FFH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3