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Entry version 171 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
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Protein

ATP-dependent dethiobiotin synthetase BioD 1

Gene

bioD1

Organism
Escherichia coli (strain K12)
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 a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid (PubMed:4892372, PubMed:4921568). In another study both CTP and GTP (but not ITP, TTP or UTP) can partially replace ATP (PubMed:25801336).3 Publications

<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 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

Mg2+UniRule annotation4 PublicationsNote: Binds 1 Mg2+ per subunit, in one structure a second Mg2+ was seen.4 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

  1. KM=15.2 µM for DAPA (at pH 7.5, 37 degrees Celsius)1 Publication
  2. KM=600 µM for NaHCO3 (at pH 7.5, 37 degrees Celsius)1 Publication
  3. KM=10.5 µM for ATP (at pH 7.5, 37 degrees Celsius)1 Publication
  4. KM=1.10 mM for CTP (at pH 7.5, 37 degrees Celsius)1 Publication
  5. KM=1.56 mM for GTP (at pH 7.5, 37 degrees Celsius)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: biotin biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. ATP-dependent dethiobiotin synthetase BioD 1 (bioD1), ATP-dependent dethiobiotin synthetase BioD (bioD), ATP-dependent dethiobiotin synthetase BioD (bioD), ATP-dependent dethiobiotin synthetase BioD 2 (bioD2)
    2. Biotin synthase (bioB), Biotin synthase (bioB)
    This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi13Magnesium 1Combined sources1 Publication1
    Metal bindingi17Magnesium 2UniRule annotationCombined sources2 Publications1
    <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 sitei38UniRule annotation1 Publication1
    <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 sitei42SubstrateUniRule annotationCombined sources3 Publications1
    Metal bindingi55Magnesium 2UniRule annotationCombined sources2 Publications1
    Binding sitei55ATPUniRule annotationCombined sources1 Publication1
    Metal bindingi116Magnesium 2UniRule annotationCombined sources2 Publications1
    Binding sitei188SubstrateCombined sources3 Publications1
    Binding sitei212ATPUniRule annotationCombined sources3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi13 – 18ATPUniRule annotationCombined sources3 Publications6
    Nucleotide bindingi116 – 119ATPUniRule annotationCombined sources1 Publication4
    Nucleotide bindingi176 – 177ATPUniRule annotationCombined sources3 Publications2
    Nucleotide bindingi205 – 207ATPUniRule annotationCombined sources3 Publications3

    <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 functionLigase
    Biological processBiotin biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:DETHIOBIOTIN-SYN-MONOMER
    MetaCyc:DETHIOBIOTIN-SYN-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P13000

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

    More...
    UniPathwayi
    UPA00078;UER00161

    <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:
    ATP-dependent dethiobiotin synthetase BioD 1UniRule annotation (EC:6.3.3.3UniRule annotation)
    Alternative name(s):
    DTB synthetase 1UniRule annotation
    Short name:
    DTBS 1UniRule annotation
    Dethiobiotin synthase 1UniRule 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
    Name:bioD1UniRule annotation
    Ordered Locus Names:b0778, JW0761
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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: Chromosome
    • UP000000625 Componenti: Chromosome

    <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

    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%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>Mutagenesisi12T → V: Strong decrease in ATP affinity; essential role for this residue in the steady-state affinity for ATP. 1 Publication1
    Mutagenesisi13E → A or D: Almost no change in activity. 1 Publication1
    Mutagenesisi16K → Q: Complete loss of activity. 1 Publication1
    Mutagenesisi38K → L, Q or R: Complete loss of activity. 1 Publication1
    Mutagenesisi42S → A or C: Almost no change in activity. 1 Publication1
    Mutagenesisi176N → A: Increases affinity for CTP 3-fold, no change for ATP. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02941, 3-(1-Aminoethyl)Nonanedioic Acid
    DB01715, 7,8-Diamino-Nonanoic Acid
    DB03624, 7-(Carboxyamino)-8-Amino-Nonanoic Acid
    DB03775, Dethiobiotin
    DB02927, Mixed Carbamic Phosphoric Acid Anhydride of 7,8-Diaminononanic Acid

    <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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00001879612 – 225ATP-dependent dethiobiotin synthetase BioD 1Add BLAST224

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P13000

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P13000

    <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

    Homodimer.

    UniRule annotation6 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4259956, 20 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P13000, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0778

    <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

    1225
    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
    P13000

    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
    P13000

    <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 dethiobiotin synthetase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0132, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_072551_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P13000

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P13000

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00336, BioD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004472, DTB_synth_BioD
    IPR027417, P-loop_NTPase

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43210, PTHR43210, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF006755, DTB_synth, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540, SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00347, bioD, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P13000-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKRYFVTGT DTEVGKTVAS CALLQAAKAA GYRTAGYKPV ASGSEKTPEG
    60 70 80 90 100
    LRNSDALALQ RNSSLQLDYA TVNPYTFAEP TSPHIISAQE GRPIESLVMS
    110 120 130 140 150
    AGLRALEQQA DWVLVEGAGG WFTPLSDTFT FADWVTQEQL PVILVVGVKL
    160 170 180 190 200
    GCINHAMLTA QVIQHAGLTL AGWVANDVTP PGKRHAEYMT TLTRMIPAPL
    210 220
    LGEIPWLAEN PENAATGKYI NLALL
    Length:225
    Mass (Da):24,140
    Last modified:January 23, 2007 - v3
    <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:i9AE76F3BE6565780
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29A → R in AAA23518 (PubMed:3058702).Curated1
    Sequence conflicti108 – 109QQ → HK in CAA00967 (Ref. 3) Curated2
    Sequence conflicti198 – 225APLLG…NLALL → RRCWERSPGLQKIQKMRQPE ST in AAA23518 (PubMed:3058702).CuratedAdd BLAST28

    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
    J04423 Genomic DNA Translation: AAA23518.1
    S68059 Genomic DNA Translation: AAB29683.2
    A11538 Unassigned DNA Translation: CAA00967.1
    U00096 Genomic DNA Translation: AAC73865.1
    AP009048 Genomic DNA Translation: BAE76365.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B64814, SYECDB

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415299.1, NC_000913.3
    WP_000044843.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73865; AAC73865; b0778
    BAE76365; BAE76365; BAE76365

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    57728427
    945387

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0761
    eco:b0778

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1500

    <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
    J04423 Genomic DNA Translation: AAA23518.1
    S68059 Genomic DNA Translation: AAB29683.2
    A11538 Unassigned DNA Translation: CAA00967.1
    U00096 Genomic DNA Translation: AAC73865.1
    AP009048 Genomic DNA Translation: BAE76365.1
    PIRiB64814, SYECDB
    RefSeqiNP_415299.1, NC_000913.3
    WP_000044843.1, NZ_LN832404.1

    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
    1A82X-ray1.80A2-225[»]
    1BS1X-ray1.80A2-225[»]
    1BYIX-ray0.97A2-225[»]
    1DADX-ray1.60A2-225[»]
    1DAEX-ray1.70A2-225[»]
    1DAFX-ray1.70A2-225[»]
    1DAGX-ray1.64A2-225[»]
    1DAHX-ray1.64A2-225[»]
    1DAIX-ray1.64A2-225[»]
    1DAKX-ray1.60A2-225[»]
    1DAMX-ray1.80A2-225[»]
    1DBSX-ray1.80A2-225[»]
    1DTSX-ray1.65A1-224[»]
    SMRiP13000
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4259956, 20 interactors
    IntActiP13000, 3 interactors
    STRINGi511145.b0778

    Chemistry databases

    DrugBankiDB02941, 3-(1-Aminoethyl)Nonanedioic Acid
    DB01715, 7,8-Diamino-Nonanoic Acid
    DB03624, 7-(Carboxyamino)-8-Amino-Nonanoic Acid
    DB03775, Dethiobiotin
    DB02927, Mixed Carbamic Phosphoric Acid Anhydride of 7,8-Diaminononanic Acid

    Proteomic databases

    PaxDbiP13000
    PRIDEiP13000

    Genome annotation databases

    EnsemblBacteriaiAAC73865; AAC73865; b0778
    BAE76365; BAE76365; BAE76365
    GeneIDi57728427
    945387
    KEGGiecj:JW0761
    eco:b0778
    PATRICifig|1411691.4.peg.1500

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0118

    Phylogenomic databases

    eggNOGiCOG0132, Bacteria
    HOGENOMiCLU_072551_0_0_6
    InParanoidiP13000
    PhylomeDBiP13000

    Enzyme and pathway databases

    UniPathwayiUPA00078;UER00161
    BioCyciEcoCyc:DETHIOBIOTIN-SYN-MONOMER
    MetaCyc:DETHIOBIOTIN-SYN-MONOMER
    SABIO-RKiP13000

    Miscellaneous databases

    EvolutionaryTraceiP13000

    Protein Ontology

    More...
    PROi
    PR:P13000

    Family and domain databases

    HAMAPiMF_00336, BioD, 1 hit
    InterProiView protein in InterPro
    IPR004472, DTB_synth_BioD
    IPR027417, P-loop_NTPase
    PANTHERiPTHR43210, PTHR43210, 1 hit
    PIRSFiPIRSF006755, DTB_synth, 1 hit
    SUPFAMiSSF52540, SSF52540, 1 hit
    TIGRFAMsiTIGR00347, bioD, 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 nameiBIOD1_ECOLI
    <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: P13000
    Secondary accession number(s): Q2MBJ1
    <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: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: April 7, 2021
    This is version 171 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

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