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Q42521

- DCE1_ARATH

UniProt

Q42521 - DCE1_ARATH

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi489 – 4902KK → AA: No effect. 1 Publication
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

        10         20         30         40         50
MVLSHAVSES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL
60 70 80 90 100
MLDGNPRLNL ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC
110 120 130 140 150
VNMIAHLFNA PLEEAETAVG VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK
160 170 180 190 200
PVDKPNIVTG ANVQVCWEKF ARYFEVELKE VKLSEGYYVM DPQQAVDMVD
210 220 230 240 250
ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP IHVDAASGGF
260 270 280 290 300
IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL
310 320 330 340 350
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY RNVMENCREN
360 370 380 390 400
MIVLREGLEK TERFNIVSKD EGVPLVAFSL KDSSCHTEFE ISDMLRRYGW
410 420 430 440 450
IVPAYTMPPN AQHITVLRVV IREDFSRTLA ERLVIDIEKV MRELDELPSR
460 470 480 490 500
VIHKISLGQE KSESNSDNLM VTVKKSDIDK QRDIITGWKK FVADRKKTSG

IC
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

« Hide 'large scale' publications
  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 29, 2014
This is version 112 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