Reviewed, UniProtKB/Swiss-Prot Q42472 (DCE2_ARATH)

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 By similarity.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate.
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	Glutamate decarboxylase 2		PRO_0000146974
Regions
	Region	461 – 494	34	Calmodulin-binding By similarity
Amino acid modifications
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 741E83A25DCBC48C	FASTA	494	56,141
	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

References

	« Hide 'large scale' referencesShow '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: 9700069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9112779] [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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49937 mRNA. Translation: AAC31617.1. U46665 mRNA. Translation: AAC33485.1. AC009513 Genomic DNA. Translation: AAF06056.1. AF428372 mRNA. Translation: AAL16302.1. AY124873 mRNA. Translation: AAM70582.1.
IPI	IPI00534442.
PIR	H96683.
RefSeq	NP_001117556.1.
UniGene	At.19149 At.24993 At.66846
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q42472.
ProMEX	Q42472.
Genome annotation databases
GeneID	842908.
GenomeReviews	Gene locus AT1G65960 in contig CT485782_GR.
KEGG	ath:AT1G65960.
NMPDR	fig|3702.1.peg.6017.
Organism-specific databases
TAIR	At1g65960.
Enzyme and pathway databases
BRENDA	4.1.1.15. 302.
Gene expression databases
Genevestigator	Q42472.
GermOnline	AT1G65960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11999:SF1. Glu_decarb_GAD. 1 hit. PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCE2_ARATH

Accession

Primary (citable) accession number: Q42472

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	October 13, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)