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P20228

- DCE_DROME

UniProt

P20228 - DCE_DROME

Protein

Glutamate decarboxylase

Gene

Gad1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the production of GABA.

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei483 – 4831SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. gamma-aminobutyric acid biosynthetic process Source: FlyBase
    2. glutamate catabolic process Source: FlyBase
    3. larval locomotory behavior Source: FlyBase
    4. neuromuscular junction development Source: FlyBase
    5. neurotransmitter biosynthetic process Source: UniProtKB-KW
    6. neurotransmitter receptor metabolic process Source: FlyBase
    7. olfactory learning Source: FlyBase
    8. response to mechanical stimulus Source: FlyBase
    9. synapse assembly Source: FlyBase

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Neurotransmitter biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_180252. GABA synthesis.
    REACT_180323. GABA synthesis, release, reuptake and degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase (EC:4.1.1.15)
    Short name:
    GAD
    Gene namesi
    Name:Gad1
    Synonyms:Gad, Glb
    ORF Names:CG14994
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0004516. Gad1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 510510Glutamate decarboxylasePRO_0000146972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei322 – 3221N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP20228.

    Expressioni

    Gene expression databases

    BgeeiP20228.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi63964. 2 interactions.
    IntActiP20228. 1 interaction.
    MINTiMINT-917310.
    STRINGi7227.FBpp0073133.

    Structurei

    3D structure databases

    ProteinModelPortaliP20228.
    SMRiP20228. Positions 17-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni107 – 1093Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    GeneTreeiENSGT00730000110441.
    InParanoidiP20228.
    KOiK01580.
    OMAiEYLYTKI.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiP20228.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20228-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLNPNGYKL SERTGKLTAY DLMPTTVTAG PETREFLLKV IDVLLDFVKA    50
    TNDRNEKVLD FHHPEDMKRL LDLDVPDRAL PLQQLIEDCA TTLKYQVKTG 100
    HPHFFNQLSN GLDLISMAGE WLTATANTNM FTYEIAPVFI LMENVVLTKM 150
    REIIGWSGGD SILAPGGSIS NLYAFLAARH KMFPNYKEHG SVGLPGTLVM 200
    FTSDQCHYSI KSCAAVCGLG TDHCIVVPSD EHGKMITSEL ERLILERKAK 250
    GDIPFFVNAT AGTTVLGAFD DINTIADICQ KYNCWMHIDA AWGGGLLMSR 300
    KHRHPRFTGV ERADSVTWNP HKLMGALLQC STIHFKEDGL LISCNQMSAE 350
    YLFMTDKQYD ISYDTGDKVI QCGRHNDIFK LWLQWRAKGT EGFEQQQDRL 400
    MELVQYQLKR IREQSDRFHL ILEPECVNVS FWYVPKRLRG VPHDAKKEVE 450
    LGKICPIIKG RMMQKGTLMV GYQPDDRRPN FFRSIISSAA VNEADVDFML 500
    DEIHRLGDDL 510
    Length:510
    Mass (Da):57,819
    Last modified:June 21, 2005 - v2
    Checksum:iAAEBFC6FDC662001
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011F → L in CAA53791. (PubMed:1689376)Curated
    Sequence conflicti301 – 3011K → T in CAA53791. (PubMed:1689376)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76198 mRNA. Translation: CAA53791.1.
    AE014296 Genomic DNA. Translation: AAF47834.1.
    AE014296 Genomic DNA. Translation: AAN11581.1.
    AE014296 Genomic DNA. Translation: AAN11582.1.
    AY089526 mRNA. Translation: AAL90264.1.
    PIRiJH0192. A30999.
    RefSeqiNP_001261396.1. NM_001274467.1.
    NP_523914.2. NM_079190.3.
    NP_728930.1. NM_168055.2.
    NP_728931.1. NM_168056.2.
    UniGeneiDm.4963.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073275; FBpp0073131; FBgn0004516.
    FBtr0073276; FBpp0073132; FBgn0004516.
    FBtr0073277; FBpp0073133; FBgn0004516.
    FBtr0332980; FBpp0305196; FBgn0004516.
    GeneIDi38484.
    KEGGidme:Dmel_CG14994.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76198 mRNA. Translation: CAA53791.1 .
    AE014296 Genomic DNA. Translation: AAF47834.1 .
    AE014296 Genomic DNA. Translation: AAN11581.1 .
    AE014296 Genomic DNA. Translation: AAN11582.1 .
    AY089526 mRNA. Translation: AAL90264.1 .
    PIRi JH0192. A30999.
    RefSeqi NP_001261396.1. NM_001274467.1.
    NP_523914.2. NM_079190.3.
    NP_728930.1. NM_168055.2.
    NP_728931.1. NM_168056.2.
    UniGenei Dm.4963.

    3D structure databases

    ProteinModelPortali P20228.
    SMRi P20228. Positions 17-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63964. 2 interactions.
    IntActi P20228. 1 interaction.
    MINTi MINT-917310.
    STRINGi 7227.FBpp0073133.

    Proteomic databases

    PaxDbi P20228.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073275 ; FBpp0073131 ; FBgn0004516 .
    FBtr0073276 ; FBpp0073132 ; FBgn0004516 .
    FBtr0073277 ; FBpp0073133 ; FBgn0004516 .
    FBtr0332980 ; FBpp0305196 ; FBgn0004516 .
    GeneIDi 38484.
    KEGGi dme:Dmel_CG14994.

    Organism-specific databases

    CTDi 2571.
    FlyBasei FBgn0004516. Gad1.

    Phylogenomic databases

    eggNOGi COG0076.
    GeneTreei ENSGT00730000110441.
    InParanoidi P20228.
    KOi K01580.
    OMAi EYLYTKI.
    OrthoDBi EOG7H1JM3.
    PhylomeDBi P20228.

    Enzyme and pathway databases

    Reactomei REACT_180252. GABA synthesis.
    REACT_180323. GABA synthesis, release, reuptake and degradation.

    Miscellaneous databases

    GenomeRNAii 38484.
    NextBioi 808870.
    PROi P20228.

    Gene expression databases

    Bgeei P20228.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drosophila GABAergic systems: sequence and expression of glutamic acid decarboxylase."
      Jackson F.R., Newby L.M., Kulkarni S.J.
      J. Neurochem. 54:1068-1078(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiDCE_DROME
    AccessioniPrimary (citable) accession number: P20228
    Secondary accession number(s): A4V1G1, Q9VZI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3