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Entry version 60 (11 Dec 2019)
Sequence version 1 (05 Sep 2006)
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Protein

Tyrosine 2,3-aminomutase

Gene

cmdF

Organism
Chondromyces crocatus
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Has aminomutase and, to a lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine, which is incorporated into secondary metabolites called chondramides. The aminomutase activity mainly produces R-beta-tyrosine but also S-beta tyrosine in smaller amounts. Does not accept D-tyrosine, L-histidine or L-phenylalanine as substrates.3 Publications

Miscellaneous

Chondramides are secondary metabolites with antifungal and cytotoxic activity. They are non-ribosomally produced depsipeptides consisting of a polyketide chain and 3 amino acids (alanine, N-methyltryptophan and beta-tyrosine or alpha-methoxy-beta-tyrosine).

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=377 µM for L-tyrosine (tyrosine 2,3-aminomutase activity)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei51Proton donor/acceptorBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei81SubstrateBy similarity1
    Binding sitei193SubstrateBy similarity1
    Binding sitei298SubstrateBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    • toxin biosynthetic process Source: UniProtKB

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase, Lyase

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.3.6 11879

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Tyrosine 2,3-aminomutase1 Publication (EC:5.4.3.6)
    Alternative name(s):
    Tyrosine ammonia-lyase1 Publication (EC:4.3.1.23)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:cmdFImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiChondromyces crocatus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri52 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeChondromyces

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi57F → Y: Loss of aminomutase activity. 1 Publication1
    Mutagenesisi60 – 65LVPVMI → MIYMLV: Shift towards ammonia lyase activity. 1 Publication6
    Mutagenesisi79 – 83RSHAA → YHLAT: Total loss of aminomutase activity. 1 Publication5
    Mutagenesisi79 – 82RSHA → TFLS: Total loss of aminomutase activity. 1 Publication4
    Mutagenesisi184G → R: Gain of aminomutase activity. 1 Publication1
    Mutagenesisi242K → R: Gain of aminomutase activity. 1 Publication1
    Mutagenesisi275 – 288Missing : Total loss of aminomutase activity. 1 PublicationAdd BLAST14
    Mutagenesisi377P → R: No effect. 1 Publication1
    Mutagenesisi396C → S: No effect. 1 Publication1
    Mutagenesisi399 – 406EGGQYLAT → MIAQVTSA: Residual aminomutase activity. 1 Publication8
    Mutagenesisi399E → A: Loss of aminomutase activity and increased product racemization. Gain of ammonia-lyase activity. 1 Publication1
    Mutagenesisi399E → K: Loss of aminomutase and ammonia-lyase activity. Higher enantiomeric excess of (R)-beta-tyrosine. 1 Publication1
    Mutagenesisi399E → M: Loss of aminomutase and ammonia-lyase activity. 1 Publication1
    Mutagenesisi427 – 433NGSNQDV → SAGREDH: Total loss of aminomutase activity. 1 Publication7
    Mutagenesisi427 – 433NGSNQDV → SANQEDH: Total loss of aminomutase activity. 1 Publication7

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004073751 – 531Tyrosine 2,3-aminomutaseAdd BLAST531

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki140 ↔ 1425-imidazolinone (Ala-Gly)By similarity
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1412,3-didehydroalanine (Ser)PROSITE-ProRule annotationBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer; dimer of dimers.

    By similarity

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q0VZ68

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the TAL/TAM family.1 Publication

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    715502at2

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00332 PAL-HAL, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.275.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001106 Aromatic_Lyase
    IPR024083 Fumarase/histidase_N
    IPR008948 L-Aspartase-like
    IPR022313 Phe/His_NH3-lyase_AS
    IPR022314 Tyr_aminomutase

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10362 PTHR10362, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00221 Lyase_aromatic, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48557 SSF48557, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03832 Tyr_2_3_mutase, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00488 PAL_HISTIDASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q0VZ68-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKITGSNLSI YDVADVCMKR ATVELDPSQL ERVAVAHERT QAWGEAQHPI
    60 70 80 90 100
    YGVNTGFGEL VPVMIPRQHK RELQENLIRS HAAGGGEPFA DDVVRAIMLA
    110 120 130 140 150
    RLNCLMKGYS GASVETVKLL AEFINRGIHP VIPQQGSLGA SGDLSPLSHI
    160 170 180 190 200
    ALALIGEGTV SFKGQVRKTG DVLREEGLKP LELGFKGGLT LINGTSAMTG
    210 220 230 240 250
    AACVALGRAY HLFRLALLAT ADFVQCLGGS TGPFEERGHL PKNHSGQVIV
    260 270 280 290 300
    AREIRKLLAG SQLTSDHQDL MKEMVARSGV GNDVVDTGVY LQDAYTLRAV
    310 320 330 340 350
    PQILGPVLDT LDFARKLIEE ELNSTNDNPL IFDVPEQTFH GANFHGQYVA
    360 370 380 390 400
    MACDYLNIAV TEIGVLAERQ LNRLVDPNIN GKLPPFLASA HSGLLCGFEG
    410 420 430 440 450
    GQYLATSIAS ENLDLAAPSS IKSLPSNGSN QDVVSMGTTS ARKSLRLCEN
    460 470 480 490 500
    VGTIVSTLIA ACNQAGHILG NERFSPPIRE LHGELSRSVP LYQDDSPIFE
    510 520 530
    LFQTVRAFVG GDGFRAHLVT HLDLAATTAS S
    Length:531
    Mass (Da):56,901
    Last modified:September 5, 2006 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i07A542D37EA339E0
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AM179409 Genomic DNA Translation: CAJ46694.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_050432503.1, NZ_CP012159.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM179409 Genomic DNA Translation: CAJ46694.1
    RefSeqiWP_050432503.1, NZ_CP012159.1

    3D structure databases

    SMRiQ0VZ68
    ModBaseiSearch...

    Phylogenomic databases

    OrthoDBi715502at2

    Enzyme and pathway databases

    BRENDAi5.4.3.6 11879

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTAM_CHOCO
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q0VZ68
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: September 5, 2006
    Last modified: December 11, 2019
    This is version 60 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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