Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q42521 (DCE1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase 1

Short name=GAD 1
EC=4.1.1.15
Gene names
Name:GAD1
Synonyms:GAD, GDH1
Ordered Locus Names:At5g17330
ORF Names:MKP11.30, MKP11_18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Up-regulatd by calmodulin binding at physiological pH. Ref.10

Subunit structure

Homohexamer. Interacts with clamodulin with a 1:3 stoichiometry. Ref.1 Ref.5 Ref.10

Tissue specificity

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. Ref.5 Ref.6 Ref.7 Ref.8

Induction

Down-regulated by salt treatment. Not induced by hypoxia. Ref.8 Ref.9 Ref.10

Domain

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.

Disruption phenotype

No visible phenotype, but increased glutamate levels and decreased GABA levels in the roots, and loss of GABA accumulation upon heat stress. Ref.7 Ref.8

Sequence similarities

Belongs to the group II decarboxylase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Glutamate decarboxylase 1
PRO_0000146973

Regions

Region469 – 50234Calmodulin-binding

Sites

Site4961Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers
Site4971Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers

Amino acid modifications

Modified residue81Phosphoserine By similarity
Modified residue2771N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis474 – 4752KK → AA: No effect.
Mutagenesis489 – 4902KK → AA: No effect.
Mutagenesis4961K → A: Decreased activity. When associated with A-497; threefold decreased activity, but still pH-dependent. Ref.10
Mutagenesis4971K → A: Decreased activity. When associated with A-496; threefold decreased activity, but still pH-dependent. Ref.10
Mutagenesis5021C → A: No effect. Ref.10
Sequence conflict2081A → D in AAA93132. Ref.1

Secondary structure

........................................................................ 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q42521 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 4E8141FF523E0E22

FASTA50257,066
        10         20         30         40         50         60 
MVLSHAVSES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL 

        70         80         90        100        110        120 
ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLEEAETAVG 

       130        140        150        160        170        180 
VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PVDKPNIVTG ANVQVCWEKF ARYFEVELKE 

       190        200        210        220        230        240 
VKLSEGYYVM DPQQAVDMVD ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP 

       250        260        270        280        290        300 
IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL 

       310        320        330        340        350        360 
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY RNVMENCREN MIVLREGLEK 

       370        380        390        400        410        420 
TERFNIVSKD EGVPLVAFSL KDSSCHTEFE ISDMLRRYGW IVPAYTMPPN AQHITVLRVV 

       430        440        450        460        470        480 
IREDFSRTLA ERLVIDIEKV MRELDELPSR VIHKISLGQE KSESNSDNLM VTVKKSDIDK 

       490        500 
QRDIITGWKK FVADRKKTSG IC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_197235.1. NM_121739.3.
UniGeneAt.25228.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HBXX-ray2.67A/B/C/D/E/F1-502[»]
ProteinModelPortalQ42521.
SMRQ42521. Positions 12-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16875. 1 interaction.
MINTMINT-8062431.
STRING3702.AT5G17330.1-P.

Proteomic databases

PaxDbQ42521.
PRIDEQ42521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G17330.1; AT5G17330.1; AT5G17330.
GeneID831599.
KEGGath:AT5G17330.

Organism-specific databases

TAIRAT5G17330.

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000070228.
InParanoidQ42521.
KOK01580.
OMACVRILAN.
PhylomeDBQ42521.

Enzyme and pathway databases

BioCycARA:AT5G17330-MONOMER.

Gene expression databases

GenevestigatorQ42521.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ42521.

Entry information

Entry nameDCE1_ARATH
AccessionPrimary (citable) accession number: Q42521
Secondary accession number(s): Q9FFH9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 27, 2002
Last modified: June 11, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names