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Entry version 99 (05 Dec 2018)
Sequence version 1 (01 Feb 1995)
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Protein

Oxalyl-CoA decarboxylase

Gene

oxc

Organism
Oxalobacter formigenes
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). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.2 Publications

<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 ‘Function’ 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

Inhibited by CoA and activated by ADP.

<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 88 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (at pH 6.7 and 30 degrees Celsius).
  1. KM=23 µM for oxalyl-CoA (at pH 6.7 and 30 degrees Celsius)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: 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 ‘Function’ 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 sitei34Substrate; via amide nitrogen1
    Binding sitei120Substrate1
    Binding sitei160ADP2 Publications1
    Binding sitei222ADP2 Publications1
    Binding sitei282ADP2 Publications1
    Binding sitei306ADP2 Publications1
    Binding sitei326ADP; via amide nitrogen2 Publications1
    Binding sitei358SubstrateBy similarity1
    Binding sitei377Thiamine pyrophosphate2 Publications1
    <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 bindingi452Magnesium2 Publications1
    Metal bindingi479Magnesium2 Publications1
    Metal bindingi481Magnesium; via carbonyl oxygen2 Publications1
    Binding sitei483Thiamine pyrophosphate2 Publications1

    <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
    MetaCyc:MONOMER-16180

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.1.8 4478

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P40149

    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
    <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>OrganismiOxalobacter formigenes
    <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 identifieri847 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeOxalobacter

    <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>Mutagenesisi56E → A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer. 1 Publication1
    Mutagenesisi120Y → A: 3-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi120Y → F: 2 and 12-fold reduction in the affinity binding and in the catalytic efficiency for oxalyl-CoA, respectively. 1 Publication1
    Mutagenesisi121E → A: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi121E → Q: Slight increase of the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi483Y → A: Does not affect oxalyl-CoA binding, but it strongly reduces the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi483Y → F: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi553S → A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA. 1 Publication1
    Mutagenesisi555R → A: 3-fold reduction in the affinity binding for oxalyl-CoA, but it does not affect the catalytic efficiency. 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_00000908231 – 568Oxalyl-CoA decarboxylaseAdd BLAST568

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P40149

    <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.2 Publications

    <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
    itself2EBI-15648203,EBI-15648203

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-29437N

    <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

    1568
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2C31X-ray1.73A/B1-568[»]
    2JI6X-ray2.06A/B1-568[»]
    2JI7X-ray1.82A/B1-568[»]
    2JI8X-ray2.15A/B1-568[»]
    2JI9X-ray2.20A/B1-568[»]
    2JIBX-ray2.20A/B1-568[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P40149

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P40149

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P40149

    <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>Regioni263 – 267Substrate binding5
    Regioni401 – 403Thiamine pyrophosphate binding3
    Regioni408 – 409Substrate binding2
    Regioni426 – 428Thiamine pyrophosphate binding3
    Regioni453 – 454Thiamine pyrophosphate binding2
    Regioni553 – 555Substrate binding3

    <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

    KEGG Orthology (KO)

    More...
    KOi
    K01577

    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>.<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.

    P40149-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSNDDNVELT DGFHVLIDAL KMNDIDTMYG VVGIPITNLA RMWQDDGQRF
    60 70 80 90 100
    YSFRHEQHAG YAASIAGYIE GKPGVCLTVS APGFLNGVTS LAHATTNCFP
    110 120 130 140 150
    MILLSGSSER EIVDLQQGDY EEMDQMNVAR PHCKASFRIN SIKDIPIGIA
    160 170 180 190 200
    RAVRTAVSGR PGGVYVDLPA KLFGQTISVE EANKLLFKPI DPAPAQIPAE
    210 220 230 240 250
    DAIARAADLI KNAKRPVIML GKGAAYAQCD DEIRALVEET GIPFLPMGMA
    260 270 280 290 300
    KGLLPDNHPQ SAAATRAFAL AQCDVCVLIG ARLNWLMQHG KGKTWGDELK
    310 320 330 340 350
    KYVQIDIQAN EMDSNQPIAA PVVGDIKSAV SLLRKALKGA PKADAEWTGA
    360 370 380 390 400
    LKAKVDGNKA KLAGKMTAET PSGMMNYSNS LGVVRDFMLA NPDISLVNEG
    410 420 430 440 450
    ANALDNTRMI VDMLKPRKRL DSGTWGVMGI GMGYCVAAAA VTGKPVIAVE
    460 470 480 490 500
    GDSAFGFSGM ELETICRYNL PVTVIIMNNG GIYKGNEADP QPGVISCTRL
    510 520 530 540 550
    TRGRYDMMME AFGGKGYVAN TPAELKAALE EAVASGKPCL INAMIDPDAG
    560
    VESGRIKSLN VVSKVGKK
    Length:568
    Mass (Da):60,684
    Last modified:February 1, 1995 - 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:iE33DB2E0064497D1
    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
    M77128 Genomic DNA Translation: AAA53683.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A55219

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_005881708.1, NZ_CP018787.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ofo:BRW83_0575

    <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
    M77128 Genomic DNA Translation: AAA53683.1
    PIRiA55219
    RefSeqiWP_005881708.1, NZ_CP018787.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2C31X-ray1.73A/B1-568[»]
    2JI6X-ray2.06A/B1-568[»]
    2JI7X-ray1.82A/B1-568[»]
    2JI8X-ray2.15A/B1-568[»]
    2JI9X-ray2.20A/B1-568[»]
    2JIBX-ray2.20A/B1-568[»]
    ProteinModelPortaliP40149
    SMRiP40149
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-29437N

    Proteomic databases

    PRIDEiP40149

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiofo:BRW83_0575

    Phylogenomic databases

    eggNOGiENOG4105CFN Bacteria
    COG0028 LUCA
    KOiK01577

    Enzyme and pathway databases

    UniPathwayi
    UPA00540;UER00599

    BioCyciMetaCyc:MONOMER-16180
    BRENDAi4.1.1.8 4478
    SABIO-RKiP40149

    Miscellaneous databases

    EvolutionaryTraceiP40149

    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...

    <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_OXAFO
    <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: P40149
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: December 5, 2018
    This is version 99 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, Direct protein sequencing

    Documents

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