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Q5R7S7

- DCE1_PONAB

UniProt

Q5R7S7 - DCE1_PONAB

Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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)
    Gene namesi
    Name:GAD1
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Glutamate decarboxylase 1PRO_0000231041Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R7S7.
    SMRiQ5R7S7. 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.
    InParanoidiQ5R7S7.
    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.

    Q5R7S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF    50
    LQRTNSLEEK SRLVSAFKER QSSKDLLSCE NSDRDARFRR TETDFSNLFA 100
    RDLLPAKNGE EQTVQFLLEV VDILLNYVRK TFDRSTKVLD FHHPHQLLEG 150
    MEGFNLELSD HPESLEQILV DCRDTLKYGV RTGHPRFFNQ LSTGLDIIGL 200
    AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS SKDGDGIFSP 250
    GGAISNMYSI TAARYKYFLE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA 300
    LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY 350
    GAFDPIQEIA DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT 400
    WNPHKMMGVL LQCSAILVKE KGILQGCNQM CAGYLFQPDK QYDVSYDTGD 450
    KAIQCGRHVD IFKFWLMWKA KGTVGFENQI NKCLELAEYL YAKIKNREEF 500
    EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP KIKALMMESG 550
    TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL 594
    Length:594
    Mass (Da):66,893
    Last modified:December 21, 2004 - v1
    Checksum:iF001AACBCF11D507
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860032 mRNA. Translation: CAH92183.1.
    RefSeqiNP_001126278.1. NM_001132806.1.

    Genome annotation databases

    GeneIDi100173252.
    KEGGipon:100173252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860032 mRNA. Translation: CAH92183.1 .
    RefSeqi NP_001126278.1. NM_001132806.1.

    3D structure databases

    ProteinModelPortali Q5R7S7.
    SMRi Q5R7S7. Positions 93-593.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173252.
    KEGGi pon:100173252.

    Organism-specific databases

    CTDi 2571.

    Phylogenomic databases

    HOVERGENi HBG004980.
    InParanoidi Q5R7S7.
    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiDCE1_PONAB
    AccessioniPrimary (citable) accession number: Q5R7S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 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