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Entry version 104 (05 Jun 2019)
Sequence version 1 (20 Dec 2005)
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Protein

Oxalyl-CoA decarboxylase

Gene

oxc

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

Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.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:

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

Activated by ADP.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (with 300 µM ADP at pH 6.5 and 30 degrees Celsius). Kcat is 60.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (at pH 6.5 and 30 degrees Celsius).
  1. KM=3.17 µM for oxalyl-CoA (with 300 µM ADP at pH 6.5 and 30 degrees Celsius)1 Publication
  2. KM=4.8 µM for oxalyl-CoA (at pH 6.5 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is between 5.5 and 7.1 Publication

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

    This protein is involved in step 2 of the subpathway that synthesizes CO(2) and formate from oxalate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Formyl-CoA:oxalate CoA-transferase (frc)
    2. Oxalyl-CoA decarboxylase (oxc)
    This subpathway is part of the pathway oxalate degradation, which is itself part of Metabolic intermediate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and formate from oxalate, the pathway oxalate degradation and in Metabolic intermediate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei32Substrate; via amide nitrogenBy similarity1
    Binding sitei118SubstrateBy similarity1
    Binding sitei158ADP1 Publication1
    Binding sitei220ADP1 Publication1
    Binding sitei280ADP1 Publication1
    Binding sitei302ADP1 Publication1
    Binding sitei322ADP; via amide nitrogen1 Publication1
    Binding sitei355Substrate1
    Binding sitei372Thiamine pyrophosphate1 Publication1
    <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 bindingi447Magnesium1 Publication1
    Metal bindingi474Magnesium1 Publication1
    Metal bindingi476Magnesium; via carbonyl oxygen1 Publication1
    Binding sitei478Thiamine pyrophosphate; via amide nitrogen1 Publication1

    <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 functionDecarboxylase, Lyase
    LigandMagnesium, Metal-binding, Nucleotide-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7236-MONOMER
    ECOL316407:JW2370-MONOMER
    MetaCyc:G7236-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.8 2026

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

    More...
    UniPathwayi
    UPA00540;UER00599

    <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:
    Oxalyl-CoA decarboxylase (EC:4.1.1.8)
    <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:oxc
    Synonyms:yfdU
    Ordered Locus Names:b2373, JW2370
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG14143 oxc

    <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_00000908241 – 564Oxalyl-CoA decarboxylaseAdd BLAST564

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0AFI0

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

    More...
    PaxDbi
    P0AFI0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AFI0

    <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 the acid response regulator EvgA.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

    Homotetramer; dimer of dimers.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-557143,EBI-557143

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260862, 15 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-48075N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AFI0, 6 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0AFI0

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2373

    <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

    1564
    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
    P0AFI0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0AFI0

    <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>Regioni261 – 265Substrate bindingCurated5
    Regioni396 – 398Thiamine pyrophosphate binding3
    Regioni403 – 404Substrate binding2
    Regioni421 – 423Thiamine pyrophosphate binding3
    Regioni448 – 449Thiamine pyrophosphate binding2
    Regioni550 – 552Substrate bindingBy similarity3

    <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 TPP enzyme family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CFN Bacteria
    COG0028 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000053808

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AFI0

    KEGG Orthology (KO)

    More...
    KOi
    K01577

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AFI0

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR017660 Oxalyl-CoA_decarboxylase
    IPR029061 THDP-binding
    IPR012000 Thiamin_PyroP_enz_cen_dom
    IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
    IPR011766 TPP_enzyme-bd_C

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02775 TPP_enzyme_C, 1 hit
    PF00205 TPP_enzyme_M, 1 hit
    PF02776 TPP_enzyme_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52467 SSF52467, 1 hit
    SSF52518 SSF52518, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03254 oxalate_oxc, 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.

    P0AFI0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSDQLQMTDG MHIIVEALKQ NNIDTIYGVV GIPVTDMARH AQAEGIRYIG
    60 70 80 90 100
    FRHEQSAGYA AAASGFLTQK PGICLTVSAP GFLNGLTALA NATVNGFPMI
    110 120 130 140 150
    MISGSSDRAI VDLQQGDYEE LDQMNAAKPY AKAAFRVNQP QDLGIALARA
    160 170 180 190 200
    IRVSVSGRPG GVYLDLPANV LAATMEKDEA LTTIVKVENP SPALLPCPKS
    210 220 230 240 250
    VTSAISLLAK AERPLIILGK GAAYSQADEQ LREFIESAQI PFLPMSMAKG
    260 270 280 290 300
    ILEDTHPLSA AAARSFALAN ADVVMLVGAR LNWLLAHGKK GWAADTQFIQ
    310 320 330 340 350
    LDIEPQEIDS NRPIAVPVVG DIASSMQGML AELKQNTFTT PLVWRDILNI
    360 370 380 390 400
    HKQQNAQKMH EKLSTDTQPL NYFNALSAVR DVLRENQDIY LVNEGANTLD
    410 420 430 440 450
    NARNIIDMYK PRRRLDCGTW GVMGIGMGYA IGASVTSGSP VVAIEGDSAF
    460 470 480 490 500
    GFSGMEIETI CRYNLPVTIV IFNNGGIYRG DGVDLSGAGA PSPTDLLHHA
    510 520 530 540 550
    RYDKLMDAFR GVGYNVTTTD ELRHALTTGI QSRKPTIINV VIDPAAGTES
    560
    GHITKLNPKQ VAGN
    Length:564
    Mass (Da):60,581
    Last modified:December 20, 2005 - 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:i94418B2BE7D40C17
    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
    U00096 Genomic DNA Translation: AAC75432.1
    AP009048 Genomic DNA Translation: BAA16245.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B65011

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416874.1, NC_000913.3
    WP_001283490.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75432; AAC75432; b2373
    BAA16245; BAA16245; BAA16245

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946845

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2370
    eco:b2373

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4356

    <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
    U00096 Genomic DNA Translation: AAC75432.1
    AP009048 Genomic DNA Translation: BAA16245.1
    PIRiB65011
    RefSeqiNP_416874.1, NC_000913.3
    WP_001283490.1, 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
    2Q27X-ray2.12A/B1-564[»]
    2Q28X-ray1.74A/B1-564[»]
    2Q29X-ray1.82A/B1-564[»]
    SMRiP0AFI0
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4260862, 15 interactors
    DIPiDIP-48075N
    IntActiP0AFI0, 6 interactors
    MINTiP0AFI0
    STRINGi511145.b2373

    Proteomic databases

    jPOSTiP0AFI0
    PaxDbiP0AFI0
    PRIDEiP0AFI0

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75432; AAC75432; b2373
    BAA16245; BAA16245; BAA16245
    GeneIDi946845
    KEGGiecj:JW2370
    eco:b2373
    PATRICifig|1411691.4.peg.4356

    Organism-specific databases

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

    More...
    EchoBASEi
    EB3895
    EcoGeneiEG14143 oxc

    Phylogenomic databases

    eggNOGiENOG4105CFN Bacteria
    COG0028 LUCA
    HOGENOMiHOG000053808
    InParanoidiP0AFI0
    KOiK01577
    PhylomeDBiP0AFI0

    Enzyme and pathway databases

    UniPathwayiUPA00540;UER00599
    BioCyciEcoCyc:G7236-MONOMER
    ECOL316407:JW2370-MONOMER
    MetaCyc:G7236-MONOMER
    BRENDAi4.1.1.8 2026

    Miscellaneous databases

    EvolutionaryTraceiP0AFI0

    Protein Ontology

    More...
    PROi
    PR:P0AFI0

    Family and domain databases

    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR017660 Oxalyl-CoA_decarboxylase
    IPR029061 THDP-binding
    IPR012000 Thiamin_PyroP_enz_cen_dom
    IPR012001 Thiamin_PyroP_enz_TPP-bd_dom
    IPR011766 TPP_enzyme-bd_C
    PfamiView protein in Pfam
    PF02775 TPP_enzyme_C, 1 hit
    PF00205 TPP_enzyme_M, 1 hit
    PF02776 TPP_enzyme_N, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    SSF52518 SSF52518, 2 hits
    TIGRFAMsiTIGR03254 oxalate_oxc, 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 nameiOXC_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: P0AFI0
    Secondary accession number(s): P78093, P78194, P78195
    <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: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: June 5, 2019
    This is version 104 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    UniProt is an ELIXIR core data resource
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