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Entry version 59 (11 Dec 2019)
Sequence version 1 (24 Mar 2009)
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Protein

Pterin deaminase

Gene

codAch2

Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
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

Catalyzes the deamination of many pterin metabolites, such as formylpterin, pterin-6-carboxylate, pterin-7-carboxylate, pterin, hydroxymethylpterin, biopterin, D-+-neopterin, isoxanthopterin, sepiapterin, folate, xanthopterin, and 7,8-dihydrohydroxymethylpterin. May be involved in a degradative pathway for catabolizing pterin rings.1 Publication

<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

a divalent metal cationBy 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 is 64 sec(-1) with formylpterin as substrate. kcat is 110 sec(-1) with pterin-6-carboxylate as substrate. kcat is 48 sec(-1) with pterin-7-carboxylate as substrate. kcat is 131 sec(-1) with pterin as substrate. kcat is 28 sec(-1) with hydroxymethylpterin as substrate. kcat is 46 sec(-1) with biopterin as substrate. kcat is 19 sec(-1) with D-+-neopterin as substrate. kcat is 1.6 sec(-1) with isoxanthopterin as substrate. kcat is 2.9 sec(-1) with sepiapterin as substrate. kcat is 6.4 sec(-1) with folate as substrate. kcat is 0.46 sec(-1) with xanthopterin as substrate. kcat is 1.2 sec(-1) with 7,8-dihydro-hydroxymethylpterin as substrate. kcat is 0.036 sec(-1) with 7,8-dihydroneopterin as substrate. kcat is 0.090 sec(-1) with 7,8-dihydrobiopterin as substrate.1 Publication
  1. KM=12 µM for formylpterin1 Publication
  2. KM=27 µM for pterin-6-carboxylate1 Publication
  3. KM=13 µM for pterin-7-carboxylate1 Publication
  4. KM=39 µM for pterin1 Publication
  5. KM=23 µM for hydroxymethylpterin1 Publication
  6. KM=47 µM for biopterin1 Publication
  7. KM=61 µM for D-+-neopterin1 Publication
  8. KM=5.7 µM for isoxanthopterin1 Publication
  9. KM=22 µM for sepiapterin1 Publication
  10. KM=50 µM for folate1 Publication
  11. KM=40 µM for xanthopterin1 Publication
  12. KM=37 µM for 7,8-dihydro-hydroxymethylpterin1 Publication
  13. KM=200 µM for 7,8-dihydroneopterin1 Publication
  14. KM=93 µM for 7,8-dihydrobiopterin1 Publication

    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 bindingi80Divalent metal cation; catalyticBy similarity1
    Metal bindingi82Divalent metal cation; catalyticBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei85Substrate1 Publication1
    Metal bindingi231Divalent metal cation; catalyticBy similarity1
    <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 sitei234Proton donor1 Publication1
    <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>Sitei263Activates the nucleophilic waterBy similarity1
    Metal bindingi331Divalent metal cation; catalyticBy 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

    <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

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    B9J8S0

    <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:
    Pterin deaminase1 Publication (EC:3.5.4.111 Publication)
    Short name:
    PDA1 Publication
    <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:codAch2Imported
    Ordered Locus Names:Arad_3529Imported
    <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>OrganismiAgrobacterium radiobacter (strain K84 / ATCC BAA-868)
    <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 identifieri311403 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000001600 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome 1

    <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_00004319021 – 437Pterin deaminaseAdd BLAST437

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    311403.Arad_3529

    <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
    B9J8S0

    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>Regioni331 – 332Substrate binding1 Publication2

    <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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107TTD Bacteria
    COG0402 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000230085

    KEGG Orthology (KO)

    More...
    KOi
    K01485

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SDNTRDP

    Database of Orthologous Groups

    More...
    OrthoDBi
    1456605at2

    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
    IPR013108 Amidohydro_3
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07969 Amidohydro_3, 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.

    B9J8S0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSYSFMSPPN AARFVLSNAT VPAVTVVGFT GPSSEGLMKA DIVVADGLIK
    60 70 80 90 100
    DILPAGTAPA ELAKADMRDG MVWPTFADMH THLDKGHIWE RRANPDGSFM
    110 120 130 140 150
    GALDAVRSDR EANWSAADVR KRMEFSLRAA YAHGTSLIRT HLDSLAPQHR
    160 170 180 190 200
    ISFEVFSEVR EAWKDKIALQ AVALFPLDFM VDDAFFADLT TVVREAGGLL
    210 220 230 240 250
    GGVTQMNPDI DAQLDKLIRA AAANGLDIDL HVDETEDREV LTLKAIAAAV
    260 270 280 290 300
    LRNGFTGKVT AGHCCSLARQ DENVAAATID LVAKAGISIV ALPMCNMYLQ
    310 320 330 340 350
    DRHPGRTPRW RGVTLLHELA AAGVPTAVAS DNTRDPFYAY GDLDPVEVFR
    360 370 380 390 400
    EAVRILHLDH PLDTAARVVT TSPASILGRP DIGRIAVGGP ADLVLFSARR
    410 420 430
    WSEFLSRPQS DRVVLRKGKV IDRSLPDYRE LDTVIGA
    Length:437
    Mass (Da):47,425
    Last modified:March 24, 2009 - 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:iBC7CA943AEDABB86
    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
    CP000628 Genomic DNA Translation: ACM27458.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012652141.1, NC_011985.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ACM27458; ACM27458; Arad_3529

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ara:Arad_3529

    <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
    CP000628 Genomic DNA Translation: ACM27458.1
    RefSeqiWP_012652141.1, NC_011985.1

    3D structure databases

    SMRiB9J8S0
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi311403.Arad_3529

    Genome annotation databases

    EnsemblBacteriaiACM27458; ACM27458; Arad_3529
    KEGGiara:Arad_3529

    Phylogenomic databases

    eggNOGiENOG4107TTD Bacteria
    COG0402 LUCA
    HOGENOMiHOG000230085
    KOiK01485
    OMAiSDNTRDP
    OrthoDBi1456605at2

    Enzyme and pathway databases

    SABIO-RKiB9J8S0

    Family and domain databases

    Gene3Di2.30.40.10, 1 hit
    InterProiView protein in InterPro
    IPR013108 Amidohydro_3
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF07969 Amidohydro_3, 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 nameiPDA_AGRRK
    <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: B9J8S0
    <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: February 4, 2015
    Last sequence update: March 24, 2009
    Last modified: December 11, 2019
    This is version 59 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

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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