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Protein

Tyrosine ammonia-lyase

Gene

Rmet_0231

Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Has ammonia-lyase and, to a lesser extent, aminomutase activity. Catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine and S-beta-tyrosine. Does not accept L-histidine or L-phenylalanine as substrates.1 Publication

Catalytic activityi

L-tyrosine = trans-p-hydroxycinnamate + ammonia.1 Publication
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate.1 Publication

Kineticsi

  1. KM=348 µM for L-tyrosine (tyrosine 2,3-aminomutase activity)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei57Proton donor/acceptorBy similarity1
    Binding sitei87SubstrateBy similarity1
    Binding sitei200SubstrateBy similarity1
    Binding sitei305SubstrateBy similarity1

    GO - Molecular functioni

    • ammonia-lyase activity Source: UniProtKB
    • tyrosine 2,3-aminomutase activity Source: UniProtKB
    • tyrosine ammonia-lyase activity Source: UniProtKB-EC

    Keywordsi

    Molecular functionIsomerase, Lyase

    Enzyme and pathway databases

    BioCyciCMET266264:GJ5G-235-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine ammonia-lyase1 Publication (EC:4.3.1.23)
    Short name:
    CmTAL1 Publication
    Alternative name(s):
    Tyrosine 2,3-aminomutase1 Publication (EC:5.4.3.6)
    Gene namesi
    Ordered Locus Names:Rmet_0231
    OrganismiCupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
    Taxonomic identifieri266264 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000002429 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004073741 – 533Tyrosine ammonia-lyaseAdd BLAST533

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki146 ↔ 1485-imidazolinone (Ala-Gly)By similarity
    Modified residuei1472,3-didehydroalanine (Ser)PROSITE-ProRule annotationBy similarity1

    Post-translational modificationi

    Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.By similarity

    Proteomic databases

    PRIDEiQ1LRV9

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers.By similarity

    Protein-protein interaction databases

    STRINGi266264.Rmet_0231

    Structurei

    3D structure databases

    ProteinModelPortaliQ1LRV9
    SMRiQ1LRV9
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TAL/TAM family.1 Publication

    Phylogenomic databases

    eggNOGiENOG4105C84 Bacteria
    COG2986 LUCA
    HOGENOMiHOG000237620
    KOiK10774
    OMAiMLTRCNS
    OrthoDBiPOG091H04Z2

    Family and domain databases

    CDDicd00332 PAL-HAL, 1 hit
    Gene3Di1.10.275.10, 1 hit
    InterProiView protein in InterPro
    IPR001106 Aromatic_Lyase
    IPR024083 Fumarase/histidase_N
    IPR008948 L-Aspartase-like
    IPR022313 Phe/His_NH3-lyase_AS
    IPR022314 Tyr_aminomutase
    PANTHERiPTHR10362 PTHR10362, 1 hit
    PfamiView protein in Pfam
    PF00221 Lyase_aromatic, 1 hit
    SUPFAMiSSF48557 SSF48557, 1 hit
    TIGRFAMsiTIGR03832 Tyr_2_3_mutase, 1 hit
    PROSITEiView protein in PROSITE
    PS00488 PAL_HISTIDASE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q1LRV9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPHAHPADID GHHLTPDTVA AIARGQRAAI VPEPVLGKVA DARARFEQVA
    60 70 80 90 100
    AANVPIYGVS TGFGELVHNW VDIEHGRALQ ENLLRSHCAG VGPLFSRDEV
    110 120 130 140 150
    RAMMVARANA LARGYSAVRP AVIEQLLKYL EAGITPAVPQ VGSLGASGDL
    160 170 180 190 200
    APLSHVAITL IGEGKVLTED GGTAPTAEVL RERGITPLAL AYKEGLALIN
    210 220 230 240 250
    GTSAMTGVSC LLLETLRAQV QQAEIIAALA LEGLSASADA FMAHGHDIAK
    260 270 280 290 300
    PHPGQIRSAA NMRALLADSA RLSGHGELSA EMKTRAGEAK NTGTGVFIQK
    310 320 330 340 350
    AYTLRCIPQV LGAVRDTLDH CATVVERELN SSNDNPLFFE DGELFHGGNF
    360 370 380 390 400
    HGQQVAFAMD FLAIAATQLG VVSERRLNRL LSPHLNNNLP AFLAAANEGL
    410 420 430 440 450
    SCGFAGAQYP ATALIAENRT ICSPASIQSV PSNGDNQDVV SMGLIAARNA
    460 470 480 490 500
    RRILDNNQYI LALELLASCQ AAELAGAVEQ LAPAGRAVFA FVRERVPFLS
    510 520 530
    IDRYMTDDIE AMAALLRQGA LVEVVRGAGI ELA
    Length:533
    Mass (Da):56,163
    Last modified:May 30, 2006 - v1
    Checksum:i37618DC17B19CC44
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000352 Genomic DNA Translation: ABF07117.1
    RefSeqiWP_011515131.1, NC_007973.1

    Genome annotation databases

    EnsemblBacteriaiABF07117; ABF07117; Rmet_0231
    GeneIDi24150735
    KEGGirme:Rmet_0231

    Similar proteinsi

    Entry informationi

    Entry nameiTALY_CUPMC
    AccessioniPrimary (citable) accession number: Q1LRV9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: May 30, 2006
    Last modified: May 23, 2018
    This is version 86 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. SIMILARITY comments
      Index of protein domains and families

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