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Q42472 (DCE2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase 2

Short name=GAD 2
EC=4.1.1.15
Gene names
Name:GAD2
Synonyms:GDH2
Ordered Locus Names:At1g65960
ORF Names:F12P19.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length494 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.1

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Up-regulatd by calmodulin binding at physiological pH. Ref.9

Subunit structure

Homohexamer By similarity. Interacts with calmodulin. Ref.1

Tissue specificity

Expressed in roots, inflorescence stems, flowers, siliques and leaves. Ref.1 Ref.6 Ref.8

Induction

Up-regulated by salt or nitrogen treatments. Down-regulated by hypoxia. Ref.6 Ref.8 Ref.9 Ref.10

Domain

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

Disruption phenotype

No visible phenotype. Ref.7

Sequence similarities

Belongs to the group II decarboxylase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.9

Sequence caution

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

The sequence AAL91148.1 differs from that shown. Reason: Frameshift at position 70.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q42472-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Glutamate decarboxylase 2
PRO_0000146974

Regions

Region463 – 49432Calmodulin-binding

Sites

Site4881Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers By similarity
Site4891Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers By similarity

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict4101A → V in AAL16126. Ref.5
Sequence conflict4611E → K in AAL91148. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 741E83A25DCBC48C

FASTA49456,141
        10         20         30         40         50         60 
MVLTKTATND ESVCTMFGSR YVRTTLPKYE IGENSIPKDA AYQIIKDELM LDGNPRLNLA 

        70         80         90        100        110        120 
SFVTTWMEPE CDKLIMDSIN KNYVDMDEYP VTTELQNRCV NIIARLFNAP LEESETAVGV 

       130        140        150        160        170        180 
GTVGSSEAIM LAGLAFKRKW QNKRKAEGKP YDKPNIVTGA NVQVCWEKFA RYFEVELKEV 

       190        200        210        220        230        240 
NLSEGYYVMD PDKAAEMVDE NTICVAAILG STLNGEFEDV KRLNDLLVKK NEETGWNTPI 

       250        260        270        280        290        300 
HVDAASGGFI APFIYPELEW DFRLPLVKSI NVSGHKYGLV YAGIGWVVWR AAEDLPEELI 

       310        320        330        340        350        360 
FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ LIRLGFEGYK NVMENCIENM VVLKEGIEKT 

       370        380        390        400        410        420 
ERFNIVSKDQ GVPVVAFSLK DHSFHNEFEI SEMLRRFGWI VPAYTMPADA QHITVLRVVI 

       430        440        450        460        470        480 
REDFSRTLAE RLVADISKVL HELDTLPSKI SKKMGIEGIA ENVKEKKMEK EILMEVIVGW 

       490 
RKFVKERKKM NGVC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRH96683.
RefSeqNP_001117556.1. NM_001124084.1.
UniGeneAt.19149.
At.20543.
At.24993.
At.66846.

3D structure databases

ProteinModelPortalQ42472.
SMRQ42472. Positions 12-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G65960.2-P.

Proteomic databases

PaxDbQ42472.
PRIDEQ42472.

Protocols and materials databases

DNASU842908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65960.2; AT1G65960.2; AT1G65960. [Q42472-1]
GeneID842908.
KEGGath:AT1G65960.

Organism-specific databases

TAIRAT1G65960.

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000070228.
InParanoidQ42472.
KOK01580.
OMAMENCIEN.
PhylomeDBQ42472.
ProtClustDBCLSN2683665.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ42472.
GenevestigatorQ42472.

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]
PANTHERPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCE2_ARATH
AccessionPrimary (citable) accession number: Q42472
Secondary accession number(s): Q8RXH0, Q944L6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 96 of the entry and version 1 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names