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UniProtKB - P0AFI0 (OXC_ECOLI)

Entry version 115 (07 Apr 2021)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
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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%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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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%5Fsection">'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), 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%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 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%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 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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
    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%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:
    Oxalyl-CoA decarboxylase (EC:4.1.1.8)
    <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:oxc
    Synonyms:yfdU
    Ordered Locus Names:b2373, JW2370
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000908241 – 564Oxalyl-CoA decarboxylaseAdd BLAST564

    Proteomic databases

    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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer; dimer of dimers.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P0AFI0
    With#Exp.IntAct
    itself4EBI-557143,EBI-557143

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260862, 15 interactors
    851186, 1 interactor

    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...

    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    		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    		COG0028, Bacteria

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AFI0

    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%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.

    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...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260862, 15 interactors
    851186, 1 interactor
    DIPiDIP-48075N
    IntActiP0AFI0, 6 interactors
    MINTiP0AFI0
    STRINGi511145.b2373

    Proteomic databases

    PaxDbiP0AFI0
    PRIDEiP0AFI0

    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

    Phylogenomic databases

    eggNOGiCOG0028, Bacteria
    InParanoidiP0AFI0
    PhylomeDBiP0AFI0

    Enzyme and pathway databases

    UniPathwayiUPA00540;UER00599
    BioCyciEcoCyc:G7236-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%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: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: April 7, 2021
    This is version 115 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, 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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