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Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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

Enzyme regulationi

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

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei496Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers1
Sitei497Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers1

GO - Molecular functioni

  • calmodulin binding Source: TAIR
  • glutamate decarboxylase activity Source: TAIR
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • glutamate metabolic process Source: InterPro
  • response to cadmium ion Source: TAIR

Keywordsi

Molecular functionCalmodulin-binding, Decarboxylase, Lyase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT5G17330-MONOMER
BRENDAi4.1.1.15 399

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
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

AraportiAT5G17330
TAIRilocus:2167240 AT5G17330

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi474 – 475KK → AA: No effect. 1 Publication2
Mutagenesisi489 – 490KK → AA: No effect. 1 Publication2
Mutagenesisi496K → A: Decreased activity. When associated with A-497; threefold decreased activity, but still pH-dependent. 1 Publication1
Mutagenesisi497K → A: Decreased activity. When associated with A-496; threefold decreased activity, but still pH-dependent. 1 Publication1
Mutagenesisi502C → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469731 – 502Glutamate decarboxylase 1Add BLAST502

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphoserineBy similarity1
Modified residuei277N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ42521
PRIDEiQ42521

PTM databases

iPTMnetiQ42521

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

ExpressionAtlasiQ42521 baseline and differential
GenevisibleiQ42521 AT

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • calmodulin binding Source: TAIR

Protein-protein interaction databases

BioGridi16875, 4 interactors
STRINGi3702.AT5G17330.1

Structurei

Secondary structure

1502
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni17 – 19Combined sources3
Helixi22 – 24Combined sources3
Beta strandi29 – 31Combined sources3
Helixi39 – 49Combined sources11
Helixi50 – 52Combined sources3
Helixi56 – 58Combined sources3
Helixi70 – 78Combined sources9
Turni79 – 81Combined sources3
Turni87 – 89Combined sources3
Helixi91 – 107Combined sources17
Beta strandi119 – 125Combined sources7
Helixi126 – 147Combined sources22
Beta strandi156 – 160Combined sources5
Helixi165 – 173Combined sources9
Beta strandi177 – 181Combined sources5
Helixi192 – 198Combined sources7
Beta strandi203 – 211Combined sources9
Turni213 – 215Combined sources3
Helixi221 – 235Combined sources15
Beta strandi241 – 244Combined sources4
Helixi248 – 250Combined sources3
Helixi252 – 255Combined sources4
Beta strandi268 – 274Combined sources7
Beta strandi286 – 292Combined sources7
Helixi293 – 295Combined sources3
Helixi298 – 300Combined sources3
Beta strandi302 – 304Combined sources3
Beta strandi306 – 309Combined sources4
Beta strandi311 – 313Combined sources3
Helixi323 – 359Combined sources37
Turni360 – 362Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi370 – 382Combined sources13
Helixi388 – 396Combined sources9
Turni397 – 399Combined sources3
Beta strandi404 – 406Combined sources3
Beta strandi415 – 420Combined sources6
Helixi427 – 445Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HBXX-ray2.67A/B/C/D/E/F1-502[»]
ProteinModelPortaliQ42521
SMRiQ42521
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ42521

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni469 – 502Calmodulin-bindingAdd BLAST34

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

eggNOGiKOG1383 Eukaryota
COG0076 LUCA
HOGENOMiHOG000070228
InParanoidiQ42521
KOiK01580
OMAiPVIAQYF
OrthoDBiEOG093607ZR
PhylomeDBiQ42521

Family and domain databases

Gene3Di3.40.640.10, 1 hit
InterProiView protein in InterPro
IPR010107 Glutamate_decarboxylase
IPR002129 PyrdxlP-dep_de-COase
IPR015424 PyrdxlP-dep_Trfase
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR43321 PTHR43321, 1 hit
PfamiView protein in Pfam
PF00282 Pyridoxal_deC, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti208A → D in AAA93132 (PubMed:7610159).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_121739.4
UniGeneiAt.25228

Genome annotation databases

EnsemblPlantsiAT5G17330.1; AT5G17330.1; AT5G17330
GeneIDi831599
GrameneiAT5G17330.1; AT5G17330.1; AT5G17330
KEGGiath:AT5G17330

Similar proteinsi

Entry informationi

Entry nameiDCE1_ARATH
AccessioniPrimary (citable) accession number: Q42521
Secondary accession number(s): Q9FFH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 27, 2002
Last modified: April 25, 2018
This is version 135 of the entry and version 2 of the sequence. See 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

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