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Reviewed, UniProtKB/Swiss-Prot Q07346 (DCE_PETHY)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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
Q07346-1 [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: 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

L16797 mRNA. Translation: AAA33709.1.
L16977 mRNA. Translation: AAA33710.1.
PIRA48767.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NWDNMR-B/C470-495[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.15. 2263.

Family and domain databases

InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11999:SF1. Glu_decarb_GAD. 1 hit.
PTHR11999. Pyridoxal_deC. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. False negative.
[Graphical view]
ProtoNetSearch...

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 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents