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Q54VQ5 (GADA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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 A

EC=4.1.1.15
Gene names
Name:gadA
ORF Names:DDB_G0280199
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Generates GABA from glutamate. GABA induces the release of acbA from prespore cells and induces the exposure of tagC on the surface of prestalk cells where it can convert acbA to SDF-2. Glutamate acts as a competitive inhibitor. Ref.3

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homohexamer By similarity.

Tissue specificity

Exclusively expressed in prespore cells late in development. Ref.3

Developmental stage

Expressed only after 10 hours of development and its mRNA accumulates to peak at 18 hours when cells are initiating fruiting body formation. Highly expressed during phagocytosis of non-pathogenic bacteria. Ref.2 Ref.4

Disruption phenotype

Mutant cells grow and develop well, forming normally proportioned fruiting bodies, but the number of viable spores is reduced to about half. Ref.3

Sequence similarities

Belongs to the group II decarboxylase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Glutamate decarboxylase A
PRO_0000391329

Regions

Region124 – 1252Pyridoxal phosphate binding By similarity

Sites

Binding site621Substrate By similarity
Binding site831Substrate By similarity
Binding site2101Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54VQ5 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 5DFE4AB49DD215CB

FASTA46252,621
        10         20         30         40         50         60 
MSLHHVKTNK YKGFYDSYAS PPATKEISKY SLKEESNKPE VIRDLIIDEL LLDGNAKQNL 

        70         80         90        100        110        120 
ATFCQTDLDK EIHVLMDKCI DKNMIDKDEY PQTAEIESRC VHILADLWNS PESSETIGCS 

       130        140        150        160        170        180 
TTGSSEAAML GGMALKWRWR ENRKKQGKPF DKPNIVTGPV QICWHKFALY FDIELREVPM 

       190        200        210        220        230        240 
EHDRYIMTPE EAIKRCDENT IGVIPTLGVT FTLQYEDVKG ISEALDKFEK ETGLDIPIHV 

       250        260        270        280        290        300 
DAASGGFVAP FLQPEIVWDF RLPRVKSING SGHKFGLSPL GVGWVVWRGK NDIHKDLVFD 

       310        320        330        340        350        360 
VNYLGGNMPT FSLNFSRPGG QIVCQYYNFL RHGRSGYTAV HQACLDHGIF ISKQVKKHGI 

       370        380        390        400        410        420 
FDIVYDGTGA LPGACWKLKK DAKVKFNLFD LSDRMRNRGW QIASYTLPNL PDIVVQRVLI 

       430        440        450        460 
RHGFSHDMAM LLIEDFNRSI EYFDKHPMVQ SISKDEGQSF HH 

« Hide

References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"Expression patterns of cell-type-specific genes in Dictyostelium."
Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F.
Mol. Biol. Cell 12:2590-2600(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[3]"GABA induces terminal differentiation of Dictyostelium through a GABAB receptor."
Anjard C., Loomis W.F.
Development 133:2253-2261(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[4]"Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium."
Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B., Skelton J., Ivens A., Bozzaro S.
BMC Genomics 9:291-291(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000035 Genomic DNA. Translation: EAL67326.1.

3D structure databases

ProteinModelPortalQ54VQ5.
SMRQ54VQ5. Positions 18-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0231446.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0231446; DDB0231446; DDB_G0280199.
KEGGddi:DDB_G0280199.

Organism-specific databases

dictyBaseDDB_G0280199. gadA.

Phylogenomic databases

eggNOGCOG0076.
InParanoidQ54VQ5.
KOK01580.
OMANIMENCM.
PhylomeDBQ54VQ5.
ProtClustDBCLSZ2728831.

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 nameGADA_DICDI
AccessionPrimary (citable) accession number: Q54VQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase