Q9ZPS3 (DCE4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate decarboxylase 4
Short name=GAD 4
EC=4.1.1.15

Gene names

Name:	GAD4
Ordered Locus Names:	At2g02010
ORF Names:	F14H20.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence 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 and shoots. Detected at low levels in siliques, stems, leaves and roots. Ref.5
Induction	Up-regulated by salt treatment and hypoxia. Ref.5 Ref.6
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Calmodulin-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 18433157. Source: TAIR nucleus Inferred from direct assay PubMed 18433157. Source: TAIR
Molecular_function	glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	Glutamate decarboxylase 4		PRO_0000416955
Amino acid modifications
	Modified residue	277	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZPS3 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 36B3FC93F2978168	FASTA	493	56,005
	10 20 30 40 50 60 MVLSKTVSES DVSIHSTFAS RYVRNSLPRF EMPENSIPKE AAYQIINDEL MLDGNPRLNL 70 80 90 100 110 120 ASFVTTWMEP ECDKLMMESI NKNYVDMDEY PVTTELQNRC VNMIARLFNA PLGDGEAAVG 130 140 150 160 170 180 VGTVGSSEAI MLAGLAFKRQ WQNKRKAQGL PYDKPNIVTG ANVQVCWEKF ARYFEVELKE 190 200 210 220 230 240 VNLREDYYVM DPVKAVEMVD ENTICVAAIL GSTLTGEFED VKLLNDLLVE KNKQTGWDTP 250 260 270 280 290 300 IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RTKTDLPDEL 310 320 330 340 350 360 IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMDNCREN MMVLRQGLEK 370 380 390 400 410 420 TGRFKIVSKE NGVPLVAFSL KDSSRHNEFE VAHTLRRFGW IVPAYTMPAD AQHVTVLRVV 430 440 450 460 470 480 IREDFSRTLA ERLVADFEKV LHELDTLPAR VHAKMANGKV NGVKKTPEET QREVTAYWKK 490 LLETKKTNKN TIC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [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]	"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.
[4]	"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.
[5]	"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.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC006532 Genomic DNA. Translation: AAD20099.1. CP002685 Genomic DNA. Translation: AEC05532.1. AF361836 mRNA. Translation: AAK32848.1. AY124860 mRNA. Translation: AAM70569.1.
IPI	IPI00518622.
PIR	H84431.
RefSeq	NP_178310.1. NM_126262.1.
UniGene	At.28718.
3D structure databases
HSSP	HSSP built from PDB template 1PMM based on UniProtKB P28302.
ProteinModelPortal	Q9ZPS3.
SMR	Q9ZPS3. Positions 12-448.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G02010.1-P.
Proteomic databases
PaxDb	Q9ZPS3.
PRIDE	Q9ZPS3.
Protocols and materials databases
DNASU	814732.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G02010.1; AT2G02010.1; AT2G02010.
GeneID	814732.
KEGG	ath:AT2G02010.
Organism-specific databases
TAIR	At2g02010.
Phylogenomic databases
eggNOG	COG0076.
HOGENOM	HOG000070228.
InParanoid	Q9ZPS3.
KO	K01580.
OMA	FRWRNNA.
PhylomeDB	Q9ZPS3.
ProtClustDB	CLSN2683665.
Gene expression databases
Genevestigator	Q9ZPS3.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11999:SF1. PTHR11999:SF1. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DCE4_ARATH

Accession

Primary (citable) accession number: Q9ZPS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program