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P54767 (DCE_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Alternative name(s):
ERT D1
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length502 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 By similarity.

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate.

Sequence similarities

Belongs to the group II decarboxylase family.

Ontologies

Keywords
   LigandCalmodulin-binding
Pyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionglutamate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Glutamate decarboxylase
PRO_0000146975

Regions

Region471 – 50232Calmodulin-binding By similarity

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P54767 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1C5F9BD0084272A6

FASTA50256,785
        10         20         30         40         50         60 
MVLTTTSIRD SEESLHCTFA SRYVQEPLPK FKMPKKSMPK EAAYQIVNDE LMLDGNPRLN 

        70         80         90        100        110        120 
LASFVSTWME PECDKLIMSS INKNYVDMDE YPVTTELQNR CVNMLAHLFH APVGDDETAV 

       130        140        150        160        170        180 
GVGTVGSSEA IMLAGLAFKR KWQSKRKAEG KPFDKPNIVT GANVQVCWEK FARYFEVELK 

       190        200        210        220        230        240 
EVKLKEGYYV MDPAKAVEIV DENTICVAAI LGSTLTGEFE DVKLLNELLT KKNKETGWET 

       250        260        270        280        290        300 
PIHVDAASGG FIAPFLWPDL EWDFRLPLVK SINVSGHKYG LVYAGVGWVI WRSKEDLPDE 

       310        320        330        340        350        360 
LVFHINYLGS DQPTFTLNFS KGSYQIIAQY YQLIRLGFEG YKNVMKNCLS NAKVLTEGIT 

       370        380        390        400        410        420 
KMGRFDIVSK DVGVPVVAFS LRDSSKYTVF EVSEHLRRFG WIVPAYTMPP DAEHIAVLRV 

       430        440        450        460        470        480 
VIREDFSHSL AERLVSDIEK ILSELDTQPP RLPTKAVRVT AEEVRDDKGD GLHHFHMDTV 

       490        500 
ETQKDIIKHW RKIAGKKTSG VC 

« Hide

References

[1]"A role for glutamate decarboxylase during tomato ripening: the characterisation of a cDNA encoding a putative glutamate decarboxylase with a calmodulin-binding site."
Gallego P.P., Whotton L., Picton S., Grierson D., Gray J.E.
Plant Mol. Biol. 27:1143-1151(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Ailsa Craig.
Tissue: Pericarp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80840 mRNA. Translation: CAA56812.1.
PIRS56177.
RefSeqNP_001234041.1. NM_001247112.1.
UniGeneLes.21402.
Les.249.

3D structure databases

ProteinModelPortalP54767.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXP54767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID544313.
KEGGsly:544313.

Phylogenomic databases

KOK01580.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15560.

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]
PANTHERPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCE_SOLLC
AccessionPrimary (citable) accession number: P54767
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 73 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