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Q9LSH2 (DCE5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase 5

Short name=GAD 5
EC=4.1.1.15
Gene names
Name:GAD5
Ordered Locus Names:At3g17760
ORF Names:MIG5.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homohexamer. Interacts with clamodulin By similarity.

Tissue specificity

Expressed in flowers. Ref.4

Sequence similarities

Belongs to the group II decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Glutamate decarboxylase 5
PRO_0000416956

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LSH2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7985F175E54DF262

FASTA49455,770
        10         20         30         40         50         60 
MVLATNSDSD EHLHSTFASR YVRAVVPRFK MPDHCMPKDA AYQVINDELM LDGNPRLNLA 

        70         80         90        100        110        120 
SFVTTWMEPE CDKLIMDSVN KNYVDMDEYP VTTELQNRCV NMIANLFHAP VGEDEAAIGC 

       130        140        150        160        170        180 
GTVGSSEAIM LAGLAFKRKW QHRRKAQGLP IDKPNIVTGA NVQVCWEKFA RYFEVELKEV 

       190        200        210        220        230        240 
KLSEDYYVMD PAKAVEMVDE NTICVAAILG STLTGEFEDV KQLNDLLAEK NAETGWETPI 

       250        260        270        280        290        300 
HVDAASGGFI APFLYPDLEW DFRLPWVKSI NVSGHKYGLV YAGVGWVVWR TKDDLPEELV 

       310        320        330        340        350        360 
FHINYLGADQ PTFTLNFSKG SSQIIAQYYQ FIRLGFEGYK NIMENCMDNA RRLREGIEMT 

       370        380        390        400        410        420 
GKFNIVSKDI GVPLVAFSLK DSSKHTVFEI AESLRKFGWI IPAYTMPADA QHIAVLRVVI 

       430        440        450        460        470        480 
REDFSRGLAD RLITHIIQVL KEIEGLPSRI AHLAAAAAVS GDDEEVKVKT AKMSLEDITK 

       490 
YWKRLVEHKR NIVC 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Metabolism and functions of gamma-aminobutyric acid."
Shelp B.J., Bown A.W., McLean M.D.
Trends Plant Sci. 4:446-452(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026646 Genomic DNA. Translation: BAB02870.1.
CP002686 Genomic DNA. Translation: AEE76003.1.
CP002686 Genomic DNA. Translation: AEE76004.1.
RefSeqNP_001154621.1. NM_001161149.1.
NP_188403.1. NM_112657.1.
UniGeneAt.38660.

3D structure databases

ProteinModelPortalQ9LSH2.
SMRQ9LSH2. Positions 13-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9LSH2. 1 interaction.

Proteomic databases

PRIDEQ9LSH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G17760.1; AT3G17760.1; AT3G17760.
AT3G17760.2; AT3G17760.2; AT3G17760.
GeneID821044.
KEGGath:AT3G17760.

Organism-specific databases

TAIRAT3G17760.

Phylogenomic databases

InParanoidQ9LSH2.
KOK01580.
OMAPTFQINF.
PhylomeDBQ9LSH2.

Enzyme and pathway databases

BioCycARA:AT3G17760-MONOMER.
ARA:GQT-2607-MONOMER.

Gene expression databases

GenevestigatorQ9LSH2.

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...

Entry information

Entry nameDCE5_ARATH
AccessionPrimary (citable) accession number: Q9LSH2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 88 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