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Protein

Anthranilate 1,2-dioxygenase large subunit

Gene

antA

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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

Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol.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

Protein has several cofactor binding sites:

Redox potential

E0 is -86 +/-10 mV for Rieske center at pH 7.0.2 Publications

<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

KM values measured using the AntAB complex.
  1. KM=1 µM for anthranilate2 Publications
  2. KM=12 µM for benzoate2 Publications

    pH dependencei

    Optimum pH is 6.3 for the reverse reaction.2 Publications

    <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: anthranilate degradation via hydroxylation

    This protein is involved in step 1 of the subpathway that synthesizes catechol from anthranilate.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Anthranilate 1,2-dioxygenase large subunit (antA), Anthranilate 1,2-dioxygenase electron transfer component (antC), Anthranilate 1,2-dioxygenase small subunit (antB)
    This subpathway is part of the pathway anthranilate degradation via hydroxylation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes catechol from anthranilate, the pathway anthranilate degradation via hydroxylation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi93Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity1
    Metal bindingi95Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity1
    Metal bindingi113Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity1
    Metal bindingi116Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity1
    Metal bindingi220IronBy similarity1
    Metal bindingi225IronBy similarity1
    Metal bindingi379IronBy 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

    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 functionDioxygenase, Oxidoreductase
    Biological processAromatic hydrocarbons catabolism
    Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    ASP62977:ACIAD_RS12135-MONOMER
    MetaCyc:MONOMER-7505

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

    More...
    UniPathwayi
    UPA01016;UER01026

    <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:
    Anthranilate 1,2-dioxygenase large subunit1 Publication (EC:1.14.12.11 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:antAImported
    Ordered Locus Names:ACIAD2669
    <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>OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    <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 identifieri62977 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    <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
    • UP000000430 <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

    <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>Mutagenesisi43M → K: Prevents anthranilate degradation. 1 Publication1
    Mutagenesisi217D → A in ACN476; loss of dioxygenase activity and 2-fold lower redox potential. 1 Publication1
    Mutagenesisi217D → E: Loss of dioxygenase activity and lack of iron at the mononuclear site. 1 Publication1
    Mutagenesisi217D → N: Loss of dioxygenase activity. 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_00004151571 – 471Anthranilate 1,2-dioxygenase large subunitAdd BLAST471

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O85673

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By anthranilate.1 Publication

    <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

    The anthranilate dioxygenase (AntDO) multicomponent enzyme system is composed of an oxygenase component and a NADH:acceptor reductase component (AntC). The oxygenase component is a heterohexamer of 3 large (AntA) and 3 small (AntB) subunits.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    62977.ACIAD2669

    <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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O85673

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini52 – 160RieskePROSITE-ProRule annotationAdd BLAST109

    <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
    ENOG4108Q89 Bacteria
    COG4638 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000140938

    KEGG Orthology (KO)

    More...
    KOi
    K05599

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GEYCEDF

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG091H0936

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.102.10.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017638 Anthranilate_1-2-diOase_lsu
    IPR017941 Rieske_2Fe-2S
    IPR036922 Rieske_2Fe-2S_sf
    IPR015881 Ring-hydroxy_dOase_2Fe2S_BS
    IPR015879 Ring_hydroxy_dOase_asu_C_dom
    IPR001663 Rng_hydr_dOase-A

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00355 Rieske, 1 hit
    PF00848 Ring_hydroxyl_A, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00090 RNGDIOXGNASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50022 SSF50022, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03228 anthran_1_2_A, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51296 RIESKE, 1 hit
    PS00570 RING_HYDROXYL_ALPHA, 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>.<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.

    O85673-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTARNLAEWQ NFVQGCIDFR PNDGVYRIAR DMFTEPELFE LEMELIFEKV
    60 70 80 90 100
    WIYACHESEI PNNNDFVTVQ IGRQPMIVSR DGKGELHAMV NACEHRGATL
    110 120 130 140 150
    TRVAKGNQSV FTCPFHAWCY KSDGRLVKVK APGEYCEDFD KSSRGLKQGR
    160 170 180 190 200
    IASYRGFVFV SLDTQATDSL EDFLGDAKVF LDLMVDQSPT GELEVLQGKS
    210 220 230 240 250
    AYTFAGNWKL QNENGLDGYH VSTVHYNYVS TVQHRQQVNA AKGDELDTLD
    260 270 280 290 300
    YSKLGAGDSE TDDGWFSFKN GHSVLFSDMP NPTVRPGYNT VMPYLVEKFG
    310 320 330 340 350
    EKRAEWAMHR LRNLNLYPSL FFMDQISSQL RIIRPVAWNK TEVISQCIGV
    360 370 380 390 400
    KGESSEARRN RIRQFEDFFN VSGLGTPDDL VEFREQQKGF QGRIERWSDI
    410 420 430 440 450
    SRGYHQWTYG PTQNSQDLGI EPVITGREFT HEGLYVNQHG QWQRLILDGL
    460 470
    NKKALKMHDV TFDNQSVMDE V
    Length:471
    Mass (Da):53,936
    Last modified:November 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:i2DB8F0BA56CBED4A
    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
    AF071556 Genomic DNA Translation: AAC34813.1
    CR543861 Genomic DNA Translation: CAG69424.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_004928945.1, NC_005966.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAG69424; CAG69424; ACIAD2669

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    aci:ACIAD2669

    <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
    AF071556 Genomic DNA Translation: AAC34813.1
    CR543861 Genomic DNA Translation: CAG69424.1
    RefSeqiWP_004928945.1, NC_005966.1

    3D structure databases

    ProteinModelPortaliO85673
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi62977.ACIAD2669

    Proteomic databases

    PRIDEiO85673

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAG69424; CAG69424; ACIAD2669
    KEGGiaci:ACIAD2669

    Phylogenomic databases

    eggNOGiENOG4108Q89 Bacteria
    COG4638 LUCA
    HOGENOMiHOG000140938
    KOiK05599
    OMAiGEYCEDF
    OrthoDBiPOG091H0936

    Enzyme and pathway databases

    UniPathwayi
    UPA01016;UER01026

    BioCyciASP62977:ACIAD_RS12135-MONOMER
    MetaCyc:MONOMER-7505

    Family and domain databases

    Gene3Di2.102.10.10, 1 hit
    InterProiView protein in InterPro
    IPR017638 Anthranilate_1-2-diOase_lsu
    IPR017941 Rieske_2Fe-2S
    IPR036922 Rieske_2Fe-2S_sf
    IPR015881 Ring-hydroxy_dOase_2Fe2S_BS
    IPR015879 Ring_hydroxy_dOase_asu_C_dom
    IPR001663 Rng_hydr_dOase-A
    PfamiView protein in Pfam
    PF00355 Rieske, 1 hit
    PF00848 Ring_hydroxyl_A, 1 hit
    PRINTSiPR00090 RNGDIOXGNASE
    SUPFAMiSSF50022 SSF50022, 1 hit
    TIGRFAMsiTIGR03228 anthran_1_2_A, 1 hit
    PROSITEiView protein in PROSITE
    PS51296 RIESKE, 1 hit
    PS00570 RING_HYDROXYL_ALPHA, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiANTDA_ACIAD
    <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: O85673
    <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: January 25, 2012
    Last sequence update: November 1, 1998
    Last modified: December 5, 2018
    This is version 113 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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