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Protein

Glutamate decarboxylase A

Gene

gadA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateBy similarity
Binding sitei83 – 831SubstrateBy similarity
Binding sitei210 – 2101Pyridoxal phosphateBy similarity
Binding sitei273 – 2731Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: dictyBase
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate catabolic process Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase A (EC:4.1.1.15)
Gene namesi
Name:gadA
ORF Names:DDB_G0280199
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0280199. gadA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: dictyBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutant cells grow and develop well, forming normally proportioned fruiting bodies, but the number of viable spores is reduced to about half.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Glutamate decarboxylase APRO_0000391329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei274 – 2741N6-(pyridoxal phosphate)lysineBy similarity

Expressioni

Tissue specificityi

Exclusively expressed in prespore cells late in development.1 Publication

Developmental stagei

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.2 Publications

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi44689.DDB_0231446.

Structurei

3D structure databases

ProteinModelPortaliQ54VQ5.
SMRiQ54VQ5. Positions 18-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 1252Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
InParanoidiQ54VQ5.
KOiK01580.
OMAiFVGTWMD.
PhylomeDBiQ54VQ5.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q54VQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLHHVKTNK YKGFYDSYAS PPATKEISKY SLKEESNKPE VIRDLIIDEL
60 70 80 90 100
LLDGNAKQNL ATFCQTDLDK EIHVLMDKCI DKNMIDKDEY PQTAEIESRC
110 120 130 140 150
VHILADLWNS PESSETIGCS TTGSSEAAML GGMALKWRWR ENRKKQGKPF
160 170 180 190 200
DKPNIVTGPV QICWHKFALY FDIELREVPM EHDRYIMTPE EAIKRCDENT
210 220 230 240 250
IGVIPTLGVT FTLQYEDVKG ISEALDKFEK ETGLDIPIHV DAASGGFVAP
260 270 280 290 300
FLQPEIVWDF RLPRVKSING SGHKFGLSPL GVGWVVWRGK NDIHKDLVFD
310 320 330 340 350
VNYLGGNMPT FSLNFSRPGG QIVCQYYNFL RHGRSGYTAV HQACLDHGIF
360 370 380 390 400
ISKQVKKHGI FDIVYDGTGA LPGACWKLKK DAKVKFNLFD LSDRMRNRGW
410 420 430 440 450
QIASYTLPNL PDIVVQRVLI RHGFSHDMAM LLIEDFNRSI EYFDKHPMVQ
460
SISKDEGQSF HH
Length:462
Mass (Da):52,621
Last modified:May 24, 2005 - v1
Checksum:i5DFE4AB49DD215CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000035 Genomic DNA. Translation: EAL67326.1.
RefSeqiXP_641300.1. XM_636208.1.

Genome annotation databases

EnsemblProtistsiDDB0231446; DDB0231446; DDB_G0280199.
GeneIDi8622433.
KEGGiddi:DDB_G0280199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000035 Genomic DNA. Translation: EAL67326.1.
RefSeqiXP_641300.1. XM_636208.1.

3D structure databases

ProteinModelPortaliQ54VQ5.
SMRiQ54VQ5. Positions 18-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0231446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0231446; DDB0231446; DDB_G0280199.
GeneIDi8622433.
KEGGiddi:DDB_G0280199.

Organism-specific databases

dictyBaseiDDB_G0280199. gadA.

Phylogenomic databases

eggNOGiCOG0076.
InParanoidiQ54VQ5.
KOiK01580.
OMAiFVGTWMD.
PhylomeDBiQ54VQ5.

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]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(2004) [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(2000) [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(2005) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiGADA_DICDI
AccessioniPrimary (citable) accession number: Q54VQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: May 24, 2005
Last modified: January 7, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.