Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q07346 (DCE_PETHY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase

Short name=GAD
EC=4.1.1.15
Gene names
Name:GAD
OrganismPetunia hybrida (Petunia)
Taxonomic identifier4102 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Glutamate decarboxylase
PRO_0000146976

Regions

Region469 – 50032Calmodulin-binding

Amino acid modifications

Modified residue2771N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07346 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 72A043CB885AE10D

FASTA50056,726
        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 

« Hide

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] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16797 mRNA. Translation: AAA33709.1.
L16977 mRNA. Translation: AAA33710.1.
PIRA48767.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NWDNMR-B/C470-495[»]
ProteinModelPortalQ07346.
SMRQ07346. Positions 469-495.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ07346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ07346.

Entry information

Entry nameDCE_PETHY
AccessionPrimary (citable) accession number: Q07346
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references