SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q42472

- DCE2_ARATH

UniProt

Q42472 - DCE2_ARATH

(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)

Protein
Glutamate decarboxylase 2
Gene
GAD2, GDH2, At1g65960, F12P19.12
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
Sitei488 – 4881Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers By similarity
Sitei489 – 4891Anchoring site for calmodulin binding; modulates the equilibrium between pyridoxal phosphate tautomers By similarity

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: TAIR
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glutamate metabolic process Source: TAIR
  2. nitrogen compound metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Calmodulin-binding, Pyridoxal phosphate

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase 2 (EC:4.1.1.15)
Short name:
GAD 2
Gene namesi
Name:GAD2
Synonyms:GDH2
Ordered Locus Names:At1g65960
ORF Names:F12P19.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G65960.

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Glutamate decarboxylase 2
PRO_0000146974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PaxDbiQ42472.
PRIDEiQ42472.

Expressioni

Tissue specificityi

Expressed in roots, inflorescence stems, flowers, siliques and leaves.3 Publications

Inductioni

Up-regulated by salt or nitrogen treatments. Down-regulated by hypoxia.4 Publications

Gene expression databases

ArrayExpressiQ42472.
GenevestigatoriQ42472.

Interactioni

Subunit structurei

Homohexamer By similarity. Interacts with calmodulin.1 Publication

Protein-protein interaction databases

STRINGi3702.AT1G65960.2-P.

Structurei

3D structure databases

ProteinModelPortaliQ42472.
SMRiQ42472. Positions 12-447.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni463 – 49432Calmodulin-binding
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
InParanoidiQ42472.
KOiK01580.
OMAiDEYALAH.
PhylomeDBiQ42472.

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.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q42472-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVLTKTATND ESVCTMFGSR YVRTTLPKYE IGENSIPKDA AYQIIKDELM    50
LDGNPRLNLA SFVTTWMEPE CDKLIMDSIN KNYVDMDEYP VTTELQNRCV 100
NIIARLFNAP LEESETAVGV GTVGSSEAIM LAGLAFKRKW QNKRKAEGKP 150
YDKPNIVTGA NVQVCWEKFA RYFEVELKEV NLSEGYYVMD PDKAAEMVDE 200
NTICVAAILG STLNGEFEDV KRLNDLLVKK NEETGWNTPI HVDAASGGFI 250
APFIYPELEW DFRLPLVKSI NVSGHKYGLV YAGIGWVVWR AAEDLPEELI 300
FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ LIRLGFEGYK NVMENCIENM 350
VVLKEGIEKT ERFNIVSKDQ GVPVVAFSLK DHSFHNEFEI SEMLRRFGWI 400
VPAYTMPADA QHITVLRVVI REDFSRTLAE RLVADISKVL HELDTLPSKI 450
SKKMGIEGIA ENVKEKKMEK EILMEVIVGW RKFVKERKKM NGVC 494
Length:494
Mass (Da):56,141
Last modified:November 1, 1997 - v1
Checksum:i741E83A25DCBC48C
GO

Sequence cautioni

The sequence AAL91148.1 differs from that shown. Reason: Frameshift at position 70.
The sequence AAL91148.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101A → V in AAL16126. 1 Publication
Sequence conflicti461 – 4611E → K in AAL91148. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiH96683.
RefSeqiNP_001117556.1. NM_001124084.1. [Q42472-1]
UniGeneiAt.19149.
At.20543.
At.24993.
At.66846.

Genome annotation databases

EnsemblPlantsiAT1G65960.2; AT1G65960.2; AT1G65960. [Q42472-1]
GeneIDi842908.
KEGGiath:AT1G65960.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi H96683.
RefSeqi NP_001117556.1. NM_001124084.1. [Q42472-1 ]
UniGenei At.19149.
At.20543.
At.24993.
At.66846.

3D structure databases

ProteinModelPortali Q42472.
SMRi Q42472. Positions 12-447.
ModBasei Search...

Protein-protein interaction databases

STRINGi 3702.AT1G65960.2-P.

Proteomic databases

PaxDbi Q42472.
PRIDEi Q42472.

Protocols and materials databases

DNASUi 842908.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G65960.2 ; AT1G65960.2 ; AT1G65960 . [Q42472-1 ]
GeneIDi 842908.
KEGGi ath:AT1G65960.

Organism-specific databases

TAIRi AT1G65960.

Phylogenomic databases

eggNOGi COG0076.
HOGENOMi HOG000070228.
InParanoidi Q42472.
KOi K01580.
OMAi DEYALAH.
PhylomeDBi Q42472.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressi Q42472.
Genevestigatori Q42472.

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. "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.
    , 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.
    , 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.

Entry informationi

Entry nameiDCE2_ARATH
AccessioniPrimary (citable) accession number: Q42472
Secondary accession number(s): Q8RXH0, Q944L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi