Reviewed, UniProtKB/Swiss-Prot Q42521 (DCE1_ARATH)

Names and origin

Protein names

Recommended name:
    Glutamate decarboxylase 1
      Short name=GAD 1
    EC=4.1.1.15

Gene names

Name:	GAD1
Synonyms:	GAD, GDH1
Ordered Locus Names:	At5g17330
ORF Names:	MKP11.30, MKP11_18

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 › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
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.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate.
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Calmodulin-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern. Source: TAIR
Molecular function	calmodulin binding Inferred from direct assay. Source: TAIR glutamate decarboxylase activity Inferred from direct assay. Source: TAIR 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 – 502

502

Glutamate decarboxylase 1

PRO_0000146973

Regions

Region

469 – 502

34

Calmodulin-binding

Amino acid modifications

Modified residue

277

1

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

208

1

A → D in AAA93132. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

502

Helix Strand Turn

Details...

Turn

17 – 19

3

Helix

22 – 24

3

Beta strand

29 – 31

3

Helix

39 – 49

11

Helix

50 – 52

3

Helix

56 – 58

3

Helix

70 – 78

9

Turn

79 – 81

3

Turn

87 – 89

3

Helix

91 – 107

17

Helix

127 – 132

6

Helix

136 – 147

12

Beta strand

156 – 159

4

Helix

165 – 173

9

Beta strand

177 – 180

4

Helix

192 – 198

7

Beta strand

203 – 209

7

Helix

221 – 234

14

Beta strand

241 – 244

4

Helix

252 – 255

4

Beta strand

268 – 272

5

Beta strand

288 – 292

5

Helix

293 – 295

3

Helix

298 – 300

3

Beta strand

302 – 304

3

Beta strand

311 – 313

3

Helix

323 – 334

12

Helix

341 – 355

15

Turn

359 – 362

4

Beta strand

364 – 366

3

Beta strand

375 – 382

8

Helix

388 – 396

9

Beta strand

404 – 406

3

Beta strand

415 – 420

6

Helix

427 – 445

19

Sequences

	Sequence		Length	Mass (Da)
	Q42521-1 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: 4E8141FF523E0E22	FASTA	502	57,066
	10 20 30 40 50 60 MVLSHAVSES DVSVHSTFAS RYVRTSLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL 70 80 90 100 110 120 ASFVTTWMEP ECDKLIMSSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLEEAETAVG 130 140 150 160 170 180 VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PVDKPNIVTG ANVQVCWEKF ARYFEVELKE 190 200 210 220 230 240 VKLSEGYYVM DPQQAVDMVD ENTICVAAIL GSTLNGEFED VKLLNDLLVE KNKETGWDTP 250 260 270 280 290 300 IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKEDLPEEL 310 320 330 340 350 360 IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGHEGY RNVMENCREN MIVLREGLEK 370 380 390 400 410 420 TERFNIVSKD EGVPLVAFSL KDSSCHTEFE ISDMLRRYGW IVPAYTMPPN AQHITVLRVV 430 440 450 460 470 480 IREDFSRTLA ERLVIDIEKV MRELDELPSR VIHKISLGQE KSESNSDNLM VTVKKSDIDK 490 500 QRDIITGWKK FVADRKKTSG IC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase." Arazi T., Baum G., Snedden W.A., Shelp B.J., Fromm H. Plant Physiol. 108:551-561(1995) [PubMed: 7610159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed: 9330910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10034 mRNA. Translation: AAA93132.1.
AB005238 Genomic DNA. Translation: BAB10520.1.
AY094464 mRNA. Translation: AAM19834.1.
BT001047 mRNA. Translation: AAN46801.1.

IPI

IPI00530557.

RefSeq

NP_197235.1.

UniGene

At.25228
Rra.3677

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HBX	X-ray	2.67	A/B/C/D/E/F	1-502	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q42521.

Proteomic databases

PRIDE

Q42521.

Genome annotation databases

GeneID

831599.

GenomeReviews

Gene locus AT5G17330 in contig BA000015_GR.

KEGG

ath:AT5G17330.

NMPDR

fig|3702.1.peg.23899.

Organism-specific databases

TAIR

At5g17330.

Phylogenomic databases

HOGENOM

HBG365574.

InParanoid

Q42521.

OMA

HQLVIHI.

PhylomeDB

Q42521.

Enzyme and pathway databases

BRENDA

4.1.1.15. 302.

Gene expression databases

ArrayExpress

Q42521.

Genevestigator

Q42521.

GermOnline

AT5G17330. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
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

DCE1_ARATH

Accession

Primary (citable) accession number: Q42521
Secondary accession number(s): Q9FFH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 27, 2002
Last modified:	February 9, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)