SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07346

- DCE_PETHY

UniProt

Q07346 - DCE_PETHY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate decarboxylase

Gene
GAD
Organism
Petunia hybrida (Petunia)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Calmodulin-binding, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase (EC:4.1.1.15)
Short name:
GAD
Gene namesi
Name:GAD
OrganismiPetunia hybrida (Petunia)
Taxonomic identifieri4102 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Glutamate decarboxylasePRO_0000146976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PRIDEiQ07346.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi474 – 49219

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NWDNMR-B/C470-495[»]
ProteinModelPortaliQ07346.
SMRiQ07346. Positions 469-495.

Miscellaneous databases

EvolutionaryTraceiQ07346.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni469 – 50032Calmodulin-bindingAdd
BLAST

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q07346-1 [UniParc]FASTAAdd to Basket

« Hide

MVLSKTVSQS DVSIHSTFAS RYVRTSLPRF KMPDNSIPKE AAYQIINDEL    50
MLDGNPRLNL ASFVTTWMEP ECDKLMMDSI NKNYVDMDEY PVTTELQNRC 100
VNMIAHLFNA PLEDGETAVG VGTVGSSEAI MLAGLAFKRK WQNKMKAQGK 150
PCDKPNIVTG ANVQVCWEKF ARYFEVELKE VKLSEGYYVM DPEKAVEMVD 200
ENTICVAAIL GSTLNGEFED VKRLNDLLVE KNKETGWDTP IHVDAASGGF 250
IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RNKDDLPDEL 300
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY KNVMENCQEN 350
ASVLREGLEK TGRFNIISKE IGVPLVAFSL KDNRQHNEFE ISETLRRFGW 400
IVPAYTMPPN AQHITVLRVV IREDFSRTLA ERLVRDIEKV LHELDTLPAR 450
VNAKLAVAEE QAAANGSEVH KKTDSEVQLE MITAWKKFVE EKKKKTNRVC 500
Length:500
Mass (Da):56,726
Last modified:November 1, 1995 - v1
Checksum:i72A043CB885AE10D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16797 mRNA. Translation: AAA33709.1.
L16977 mRNA. Translation: AAA33710.1.
PIRiA48767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16797 mRNA. Translation: AAA33709.1 .
L16977 mRNA. Translation: AAA33710.1 .
PIRi A48767.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NWD NMR - B/C 470-495 [» ]
ProteinModelPortali Q07346.
SMRi Q07346. Positions 469-495.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q07346.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q07346.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
InterProi IPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 470-495 IN COMPLEX WITH CALMODULIN, DIMERIZATION.

Entry informationi

Entry nameiDCE_PETHY
AccessioniPrimary (citable) accession number: Q07346
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi