Reviewed, UniProtKB/Swiss-Prot Q07346 (DCE_PETHY)

Names and origin

Protein names

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

Gene names

Name:

GAD

Organism

Petunia hybrida (Petunia)

Taxonomic identifier

4102 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Petunioideae › Petunia

Protein attributes

Sequence length	500 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.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Calmodulin-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	3D-structure
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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 500

500

Glutamate decarboxylase

PRO_0000146976

Regions

Region

469 – 500

32

Calmodulin-binding

Amino acid modifications

Modified residue

277

1

N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

1

.

.

.

500

Helix Strand Turn

Details...

Helix

474 – 492

19

Sequences

	Sequence		Length	Mass (Da)
	Q07346-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 72A043CB885AE10D	FASTA	500	56,726
	10 20 30 40 50 60 MVLSKTVSQS DVSIHSTFAS RYVRTSLPRF KMPDNSIPKE AAYQIINDEL MLDGNPRLNL 70 80 90 100 110 120 ASFVTTWMEP ECDKLMMDSI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLEDGETAVG 130 140 150 160 170 180 VGTVGSSEAI MLAGLAFKRK WQNKMKAQGK PCDKPNIVTG ANVQVCWEKF ARYFEVELKE 190 200 210 220 230 240 VKLSEGYYVM DPEKAVEMVD ENTICVAAIL GSTLNGEFED VKRLNDLLVE KNKETGWDTP 250 260 270 280 290 300 IHVDAASGGF IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RNKDDLPDEL 310 320 330 340 350 360 IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY KNVMENCQEN ASVLREGLEK 370 380 390 400 410 420 TGRFNIISKE IGVPLVAFSL KDNRQHNEFE ISETLRRFGW IVPAYTMPPN AQHITVLRVV 430 440 450 460 470 480 IREDFSRTLA ERLVRDIEKV LHELDTLPAR VNAKLAVAEE QAAANGSEVH KKTDSEVQLE 490 500 MITAWKKFVE EKKKKTNRVC

References

[1]	"A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis." Baum G., Chen Y., Arazi T., Takatsuji H., Fromm H. J. Biol. Chem. 268:19610-19617(1993) [PubMed: 8366104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Petal.
[2]	"Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin." Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M. J. Mol. Biol. 328:193-204(2003) [PubMed: 12684008] [Abstract] Cited for: STRUCTURE BY NMR OF 470-495 IN COMPLEX WITH CALMODULIN, DIMERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L16797 mRNA. Translation: AAA33709.1.
L16977 mRNA. Translation: AAA33710.1.

PIR

A48767.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NWD	NMR	-	B/C	470-495	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.1.1.15. 2263.

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

DCE_PETHY

Accession

Primary (citable) accession number: Q07346

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)