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P14748

- DCE1_FELCA

UniProt

P14748 - DCE1_FELCA

Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 3 (01 Oct 1993)
      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 sitei567 – 5671SubstrateBy similarity

    GO - Molecular functioni

    1. glutamate decarboxylase activity Source: UniProtKB-EC
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. carboxylic acid metabolic process Source: InterPro
    2. neurotransmitter biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Neurotransmitter biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 1 (EC:4.1.1.15)
    Alternative name(s):
    67 kDa glutamic acid decarboxylase
    Short name:
    GAD-67
    Glutamate decarboxylase 67 kDa isoform
    Gene namesi
    Name:GAD1
    Synonyms:GAD67
    OrganismiFelis catus (Cat) (Felis silvestris catus)
    Taxonomic identifieri9685 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
    ProteomesiUP000011712: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Glutamate decarboxylase 1PRO_0000146962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei405 – 4051N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP14748.
    SMRiP14748. Positions 93-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 1923Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    HOVERGENiHBG004980.
    KOiK01580.

    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.

    P14748-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF    50
    LQRTNSLEEK SRLVSAFKER QSSKNLLSCE NSDRDGRFRR TETDFSNLFA 100
    RDLLPAKNGE EQTVQFLLEV VDILLNYVRK TFDRSTKVLD FHHPHQLLEG 150
    MEGFNLELSD HPESLEQILV DCRDTLKYGV RTGHPRFFNQ LSTGLDIIGL 200
    AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS SKDGDGIFSP 250
    GGAISNMYSI MAARYKFFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA 300
    LGFGTDNVIL IKCNERGKII PADLEAKILE AKQKGYVPLY VNATAGTTVY 350
    GAFDPIQEIA DICEKYNLWL HVDAAWGGGL LMSRKHRHKL SGIERANSVT 400
    WNPHKMMGVL LQCSAILVKE KGILQGCNQM CAGYLFQPDK QYDVSYDTGD 450
    KAIQCGRHVD IFKFWLMWKA KGTVGFENQI NKCLELAEYL YAKIKNREEF 500
    EMVFDGEPEH TNVCFWYIPQ SLRGIPDSPE RREKLHRVAP KIKALMMESG 550
    TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL 594
    Length:594
    Mass (Da):66,825
    Last modified:October 1, 1993 - v3
    Checksum:iEE1C8D928BC0BD02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18629 mRNA. Translation: AAA51430.1.
    PIRiA46758.
    RefSeqiNP_001009225.1. NM_001009225.1.

    Genome annotation databases

    GeneIDi493699.
    KEGGifca:493699.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18629 mRNA. Translation: AAA51430.1 .
    PIRi A46758.
    RefSeqi NP_001009225.1. NM_001009225.1.

    3D structure databases

    ProteinModelPortali P14748.
    SMRi P14748. Positions 93-593.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 493699.
    KEGGi fca:493699.

    Organism-specific databases

    CTDi 2571.

    Phylogenomic databases

    HOVERGENi HBG004980.
    KOi K01580.

    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. "Glutamic acid decarboxylase cDNA: nucleotide sequence encoding an enzymatically active fusion protein."
      Kobayashi Y., Kaufman D.L., Tobin A.J.
      J. Neurosci. 7:2768-2772(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Occipital cortex.

    Entry informationi

    Entry nameiDCE1_FELCA
    AccessioniPrimary (citable) accession number: P14748
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 79 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3