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Q54VQ5

- GADA_DICDI

UniProt

Q54VQ5 - GADA_DICDI

Protein

Glutamate decarboxylase A

Gene

gadA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    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

    Pyridoxal phosphate.By similarity

    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

    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: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0280199. gadA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: dictyBase

    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.
    OMAiKIHERTR.
    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

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    MSLHHVKTNK YKGFYDSYAS PPATKEISKY SLKEESNKPE VIRDLIIDEL    50
    LLDGNAKQNL ATFCQTDLDK EIHVLMDKCI DKNMIDKDEY PQTAEIESRC 100
    VHILADLWNS PESSETIGCS TTGSSEAAML GGMALKWRWR ENRKKQGKPF 150
    DKPNIVTGPV QICWHKFALY FDIELREVPM EHDRYIMTPE EAIKRCDENT 200
    IGVIPTLGVT FTLQYEDVKG ISEALDKFEK ETGLDIPIHV DAASGGFVAP 250
    FLQPEIVWDF RLPRVKSING SGHKFGLSPL GVGWVVWRGK NDIHKDLVFD 300
    VNYLGGNMPT FSLNFSRPGG QIVCQYYNFL RHGRSGYTAV HQACLDHGIF 350
    ISKQVKKHGI FDIVYDGTGA LPGACWKLKK DAKVKFNLFD LSDRMRNRGW 400
    QIASYTLPNL PDIVVQRVLI RHGFSHDMAM LLIEDFNRSI EYFDKHPMVQ 450
    SISKDEGQSF HH 462
    Length:462
    Mass (Da):52,621
    Last modified:May 24, 2005 - v1
    Checksum:i5DFE4AB49DD215CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000035 Genomic DNA. Translation: EAL67326.1 .
    RefSeqi XP_641300.1. XM_636208.1.

    3D structure databases

    ProteinModelPortali Q54VQ5.
    SMRi Q54VQ5. Positions 18-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0231446.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0231446 ; DDB0231446 ; DDB_G0280199 .
    GeneIDi 8622433.
    KEGGi ddi:DDB_G0280199.

    Organism-specific databases

    dictyBasei DDB_G0280199. gadA.

    Phylogenomic databases

    eggNOGi COG0076.
    InParanoidi Q54VQ5.
    KOi K01580.
    OMAi KIHERTR.
    PhylomeDBi Q54VQ5.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR010107. Glutamate_decarboxylase.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11999:SF1. PTHR11999:SF1. 1 hit.
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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(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.

    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: October 1, 2014
    This is version 63 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