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Entry version 87 (18 Sep 2019)
Sequence version 1 (01 Jun 1998)
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Protein

N-isopropylammelide isopropyl amidohydrolase

Gene

atzC

Organism
Pseudomonas sp. (strain ADP)
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

Transforms N-isopropylammelide to cyanuric acid and isopropylamine.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+3 PublicationsNote: Binds 1 Zn2+ ion per subunit.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N-ethylammeline, N-hydroxyethylammeline, N-isopropylammeline, ammeline and 2-amino-4hydroxy-1,3,5-s-triazine.1 Publication

<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

kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1) for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide. kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1) for N-cyclopropylammelide. kcat is 0.07 sec(-1) for N-t-butylammelide. kcat is 10.7 sec(-1) for N-dimethylammelide. kcat is 1.65 sec(-1) for ammelide.1 Publication
  1. KM=817 µM for N-methylammelide1 Publication
  2. KM=308 µM for N-ethylammelide1 Publication
  3. KM=3860 µM for N-hydroxyethylammelide1 Publication
  4. KM=406 µM for N-isopropylammelide1 Publication
  5. KM=580 µM for N-cyclopropylammelide1 Publication
  6. KM=299 µM for N-t-butylammelide1 Publication
  7. KM=155 µM for N-dimethylammelide1 Publication
  8. KM=1320 µM for ammelide1 Publication

    pH dependencei

    Optimum pH is 7.25.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: atrazine degradation

    This protein is involved in step 3 of the subpathway that synthesizes cyanurate from atrazine.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Atrazine chlorohydrolase (atzA)
    2. Hydroxydechloroatrazine ethylaminohydrolase (atzB)
    3. N-isopropylammelide isopropyl amidohydrolase (atzC)
    This subpathway is part of the pathway atrazine degradation, which is itself part of Xenobiotic degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes cyanurate from atrazine, the pathway atrazine degradation and in Xenobiotic degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi60Zinc; via tele nitrogen; catalytic2 Publications1
    Metal bindingi62Zinc; via tele nitrogen; catalytic2 Publications1
    Metal bindingi217Zinc; via tele nitrogen; catalytic2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei249Proton donor/acceptor1 Publication1
    Metal bindingi303Zinc; catalytic2 Publications1

    <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

    GO - Biological processi

    <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 functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-921

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.99.4 5085

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00008;UER00501

    <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_and_taxonomy_section">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:
    N-isopropylammelide isopropyl amidohydrolase (EC:3.5.4.422 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:atzC
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pADP-10 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiPseudomonas sp. (strain ADP)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri47660 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteria

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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_and_biotech_section">'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>Mutagenesisi65K → A: 30-fold increase in kcat with ammelide as substrate. 1 Publication1
    Mutagenesisi65K → R: 12-fold increase in kcat with ammelide as substrate. 1 Publication1
    Mutagenesisi160Q → A or E: Almost no effect. 1 Publication1
    Mutagenesisi188D → A: 5-fold increase in kcat with ammelide as substrate. 1 Publication1
    Mutagenesisi188D → N: No effect. 1 Publication1
    Mutagenesisi219H → A: Almost no effect. 1 Publication1
    Mutagenesisi249H → A: No activity. 1 Publication1
    Mutagenesisi303D → A or N: Almost no effect. 1 Publication1
    Mutagenesisi304N → A: Almost no effect. 1 Publication1
    Mutagenesisi304N → D: 7-fold increase in kcat with ammelide as substrate. 1 Publication1
    Mutagenesisi309W → A or F: Almost no effect. 1 Publication1

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001827071 – 403N-isopropylammelide isopropyl amidohydrolaseAdd BLAST403

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O52063

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.

    2 Publications

    <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

    Secondary structure

    1403
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    O52063

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    O52063

    <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

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K08710

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006680 Amidohydro-rel
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01979 Amidohydro_1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    O52063-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKDFDLIIR NAYLSEKDSV YDIGIVGDRI IKIEAKIEGT VKDEIDAKGN
    60 70 80 90 100
    LVSPGFVDAH THMDKSFTST GERLPKFWSR PYTRDAAIED GLKYYKNATH
    110 120 130 140 150
    EEIKRHVIEH AHMQVLHGTL YTRTHVDVDS VAKTKAVEAV LEAKEELKDL
    160 170 180 190 200
    IDIQVVAFAQ SGFFVDLESE SLIRKSLDMG CDLVGGVDPA TRENNVEGSL
    210 220 230 240 250
    DLCFKLAKEY DVDIDYHIHD IGTVGVYSIN RLAQKTIENG YKGRVTTSHA
    260 270 280 290 300
    WCFADAPSEW LDEAIPLYKD SGMKFVTCFS STPPTMPVIK LLEAGINLGC
    310 320 330 340 350
    ASDNIRDFWV PFGNGDMVQG ALIETQRLEL KTNRDLGLIW KMITSEGARV
    360 370 380 390 400
    LGIEKNYGIE VGKKADLVVL NSLSPQWAII DQAKRLCVIK NGRIIVKDEV

    IVA
    Length:403
    Mass (Da):44,938
    Last modified:June 1, 1998 - 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:i0B91206B436EEC64
    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
    U66917 Genomic DNA Translation: AAB96621.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_862508.1, NC_004956.1
    WP_011117177.1, NZ_CM003636.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1440605

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAB96621

    <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
    U66917 Genomic DNA Translation: AAB96621.1
    RefSeqiNP_862508.1, NC_004956.1
    WP_011117177.1, NZ_CM003636.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QT3X-ray2.24A/B1-403[»]
    4CQBX-ray1.84A/B1-403[»]
    4CQCX-ray2.20A/B1-403[»]
    4CQDX-ray2.25A/B1-403[»]
    5AKQX-ray2.60A/B1-403[»]
    SMRiO52063
    ModBaseiSearch...
    PDBe-KBiSearch...

    Proteomic databases

    PRIDEiO52063

    Genome annotation databases

    GeneIDi1440605
    KEGGiag:AAB96621

    Phylogenomic databases

    KOiK08710

    Enzyme and pathway databases

    UniPathwayiUPA00008;UER00501
    BioCyciMetaCyc:MONOMER-921
    BRENDAi3.5.99.4 5085

    Miscellaneous databases

    EvolutionaryTraceiO52063

    Family and domain databases

    Gene3Di2.30.40.10, 1 hit
    InterProiView protein in InterPro
    IPR006680 Amidohydro-rel
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF01979 Amidohydro_1, 1 hit
    SUPFAMiSSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 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 nameiATZC_PSESD
    <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: O52063
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 1, 1998
    Last modified: September 18, 2019
    This is version 87 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

    Keywords - Technical termi

    3D-structure, Plasmid

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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