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Protein

Aspartate 1-decarboxylase

Gene

panP

Organism
Vibrio fischeri (strain ATCC 700601 / ES114)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the pyridoxal-dependent decarboxylation of aspartate to produce beta-alanine. Has weak activity with glutamate.1 Publication

Catalytic activityi

L-aspartate = beta-alanine + CO2.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

kcat is 0.075 sec(-1) at 28 degrees Celsius. kcat is 0.008 sec(-1) at 37 degrees Celsius.1 Publication
  1. KM=1.44 mM for aspartate (at 28 degrees Celsius)1 Publication
  2. KM=1.70 mM for aspartate (at 37 degrees Celsius)1 Publication

    Pathwayi: (R)-pantothenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes beta-alanine from L-aspartate.Curated
    Proteins known to be involved in this subpathway in this organism are:
    1. Aspartate 1-decarboxylase (panP)
    This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes beta-alanine from L-aspartate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    • aspartate 1-decarboxylase activity Source: UniProtKB
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    Keywordsi

    Molecular functionDecarboxylase, Lyase
    Biological processPantothenate biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyciVFIS312309:G12Y8-939-MONOMER.
    UniPathwayiUPA00028; UER00002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate 1-decarboxylase1 Publication (EC:4.1.1.111 Publication)
    Gene namesi
    Name:panP1 Publication
    Ordered Locus Names:VF_0892Imported
    OrganismiVibrio fischeri (strain ATCC 700601 / ES114)
    Taxonomic identifieri312309 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
    Proteomesi
    • UP000000537 Componenti: Chromosome I

    Pathology & Biotechi

    Disruption phenotypei

    Deletion mutant cannot grow in minimal medium.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004408741 – 547Aspartate 1-decarboxylaseAdd BLAST547

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei338N6-(pyridoxal phosphate)lysineBy similarity1

    Interactioni

    Protein-protein interaction databases

    STRINGi312309.VF_0892.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5E6F9.
    SMRiQ5E6F9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105DY8. Bacteria.
    COG0076. LUCA.
    HOGENOMiHOG000282553.
    KOiK01580.
    OMAiLECTKEM.
    OrthoDBiPOG091H05DC.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiView protein in InterPro
    IPR022517. Asp_decarboxylase_pyridox.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_sub2.
    PfamiView protein in Pfam
    PF00282. Pyridoxal_deC. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03799. NOD_PanD_pyr. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5E6F9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVTDNKTADA SFESLLRIFT VPEAPDSTLG IIEKELSQNL NQFLREHIVA
    60 70 80 90 100
    EEKPLTEIEK DFTDSSMPES PTYVSEHTEH LLDTLVSQSV HTSAPSFIGH
    110 120 130 140 150
    MTSALPYFLM PLSKIMIALN QNLVKIETSK AFTPLERQVL GMLHRLIFGQ
    160 170 180 190 200
    KDSFYQHWMH SADHSLGAFC SGGTIANITA LWVARNRLLK PEGDFEGIAK
    210 220 230 240 250
    QGLFAALMHY KCNGLAIFVS ERGHYSLKKA ADVLGIGQDG VIAVKTDNNN
    260 270 280 290 300
    RVCLDDLELK IAQAKAKNIK PLAIVGVAGT TETGSIDPLR ELANVAQREG
    310 320 330 340 350
    CHFHVDAAWG GATLMSNTYR HLLDGIDLAD SVTIDAHKQL YVPMGAGMVI
    360 370 380 390 400
    FKDPELMSSI QHHAEYILRK GSKDLGRHTL EGSRSGMAML LYSCFNVISR
    410 420 430 440 450
    PGYELLINQS IEKAHYFADL IQQQDDFELI TEPELCLLTY RYVPSNVKAA
    460 470 480 490 500
    LAIATDEQKI EIYEHLDNLT KYIQKTQRET GKSFVSRTRL TPEAYQHQPT
    510 520 530 540
    IVFRVVLANP LTTKEILQNV LIEQREIASS SEISLPLLNQ IVGNILH
    Length:547
    Mass (Da):60,953
    Last modified:March 15, 2005 - v1
    Checksum:iB089F65FD9D6844C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000020 Genomic DNA. Translation: AAW85387.1.
    RefSeqiWP_011261555.1. NC_006840.2.
    YP_204275.1. NC_006840.2.

    Genome annotation databases

    EnsemblBacteriaiAAW85387; AAW85387; VF_0892.
    GeneIDi3277990.
    KEGGivfi:VF_0892.
    PATRICifig|312309.11.peg.888.

    Similar proteinsi

    Entry informationi

    Entry nameiPANP_VIBF1
    AccessioniPrimary (citable) accession number: Q5E6F9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2017
    Last sequence update: March 15, 2005
    Last modified: October 25, 2017
    This is version 80 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families