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Entry version 25 (07 Oct 2020)
Sequence version 1 (22 Feb 2012)
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Protein

Cyanuric acid amidohydrolase

Gene

BRAO375_2640015

Organism
Bradyrhizobium sp. (strain ORS 375)
Status
Reviewed-Annotation score:

Annotation score:3 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

Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.

UniRule annotation1 Publication

<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 <a href="http://www.uniprot.org/help/function%5Fsection">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 barbituric acid.UniRule annotationBy similarity

<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/KM is with cyanuric acid as substrate.1 Publication

      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 1 of the subpathway that synthesizes biuret from cyanurate.UniRule annotation 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 biuret from cyanurate, 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%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 sitei56SubstrateUniRule annotation1
      <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 sitei165UniRule annotation1
      Binding sitei197SubstrateUniRule annotation1
      Active sitei235NucleophileUniRule annotation1
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi305Magnesium; structuralUniRule annotation1
      <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei328Important for substrate specificityUniRule annotation1
      Binding sitei332SubstrateUniRule annotation1
      Metal bindingi354Magnesium; via carbonyl oxygen; structuralUniRule annotation1
      Metal bindingi357Magnesium; via carbonyl oxygen; structuralUniRule annotation1
      Metal bindingi358Magnesium; via carbonyl oxygen; structuralUniRule annotation1
      Metal bindingi359Magnesium; via carbonyl oxygen; structuralUniRule annotation1
      Metal bindingi362Magnesium; via carbonyl oxygen; structuralUniRule annotation1

      <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
      LigandMagnesium, Metal-binding

      Enzyme and pathway databases

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

      More...
      UniPathwayi
      UPA00008;UER00502

      <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:
      Cyanuric acid amidohydrolaseUniRule annotation (EC:3.5.2.15UniRule annotation1 Publication)
      Short name:
      CAHUniRule annotation
      <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
      ORF Names:BRAO375_2640015
      <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>OrganismiBradyrhizobium sp. (strain ORS 375)
      <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 identifieri566679 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobiumunclassified Bradyrhizobium
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000003055 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

      <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_00004399131 – 372Cyanuric acid amidohydrolaseAdd BLAST372

      <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.

      UniRule annotationBy 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
      H0SH23

      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

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 105RU AUniRule annotationAdd BLAST105
      Regioni84 – 85Substrate bindingUniRule annotation2
      Regioni115 – 252RU BUniRule annotationAdd BLAST138
      Regioni235 – 236Substrate bindingUniRule annotation2
      Regioni258 – 372RU CUniRule annotationAdd BLAST115
      Regioni351 – 352Substrate bindingUniRule annotation2

      <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).UniRule annotation

      <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 cyclic amide hydrolase (CyAH) family.UniRule annotationCurated

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      3.30.1330.160, 1 hit
      3.30.1330.170, 1 hit
      3.30.1330.180, 1 hit

      HAMAP database of protein families

      More...
      HAMAPi
      MF_01989, Cyc_amidohydrol, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR014086, AtzD/Barbiturase
      IPR043008, AtzD/Barbiturase_RUA
      IPR043006, AtzD/Barbiturase_RUB
      IPR043007, AtzD/Barbiturase_RUC

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF09663, Amido_AtzD_TrzD, 1 hit

      TIGRFAMs; a protein family database

      More...
      TIGRFAMsi
      TIGR02714, amido_AtzD_TrzD, 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.

      H0SH23-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MPTTLRRAHV HRLPMRSPDD VAALEAAITQ GTIDPAGIVA ILGKTEGNGC
      60 70 80 90 100
      VNDFTRAFAV RSLEALLGRH LATEAVRQIA MVMSGGTEGA LSPHMIVFEA
      110 120 130 140 150
      REVDEGHAPR AFAASLALGR ARTPVLPSEH LGRMQQVAQV AAGVRAAMND
      160 170 180 190 200
      AGITDAGDVH YVQVKCPLLT MERIEAAEAR GVRTAVRDTL KSMGFSRGAS
      210 220 230 240 250
      ALGVAVALGE LAMDELSDTE ICTDYARYSE RAATSGGVEL LDHEIMVAGM
      260 270 280 290 300
      SRDWTGPLAI DHGVMRDAID IEPARAALAR LGLDVPGQLP AAARGRIAAV
      310 320 330 340 350
      LAKAEAAQSG KVRDVRHTML DDSDVSSTRH ARAFVGGALA GLFGFTDLFV
      360 370
      SGGAEHQGPD GGGPVAIIVE RT
      Length:372
      Mass (Da):38,930
      Last modified:February 22, 2012 - 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:i1C303D8DDFEAD90D
      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
      CAFI01000184 Genomic DNA Translation: CCD93500.1

      NCBI Reference Sequences

      More...
      RefSeqi
      WP_009028459.1, NZ_CAFI01000184.1

      Genome annotation databases

      Ensembl bacterial and archaeal genome annotation project

      More...
      EnsemblBacteriai
      CCD93500; CCD93500; BRAO375_2640015

      <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
      CAFI01000184 Genomic DNA Translation: CCD93500.1
      RefSeqiWP_009028459.1, NZ_CAFI01000184.1

      3D structure databases

      SMRiH0SH23
      ModBaseiSearch...

      Genome annotation databases

      EnsemblBacteriaiCCD93500; CCD93500; BRAO375_2640015

      Enzyme and pathway databases

      UniPathwayiUPA00008;UER00502

      Family and domain databases

      Gene3Di3.30.1330.160, 1 hit
      3.30.1330.170, 1 hit
      3.30.1330.180, 1 hit
      HAMAPiMF_01989, Cyc_amidohydrol, 1 hit
      InterProiView protein in InterPro
      IPR014086, AtzD/Barbiturase
      IPR043008, AtzD/Barbiturase_RUA
      IPR043006, AtzD/Barbiturase_RUB
      IPR043007, AtzD/Barbiturase_RUC
      PfamiView protein in Pfam
      PF09663, Amido_AtzD_TrzD, 1 hit
      TIGRFAMsiTIGR02714, amido_AtzD_TrzD, 1 hit

      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 nameiCAH_BRAS3
      <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: H0SH23
      <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 10, 2017
      Last sequence update: February 22, 2012
      Last modified: October 7, 2020
      This is version 25 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. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      2. SIMILARITY comments
        Index of protein domains and families
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