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Protein

Quinate/shikimate dehydrogenase (NAD(+))

Gene

aroE

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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 biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD+-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. It can only use NAD.2 Publications

Miscellaneous

Has a different substrate and cosubstrate specificities relative to all other known bacterial shikimate/quinate dehydrogenases.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 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

The catalytic efficiency with quinate is 3.3-fold higher than that with shikimate. With NADP+ instead of NAD+ as cosubstrate, activity decreases by more than 300-fold with either shikimate or quinate as a substrate.2 Publications
  1. KM=0.13 mM for NAD (with 16 mM quinate at pH 7.5)1 Publication
  2. KM=0.28 mM for NAD (with 16 mM quinate at pH 9)1 Publication
  3. KM=0.46 mM for NAD (with 60 mM shikimate at pH 9)1 Publication
  4. KM=0.87 mM for NAD (with 60 mM shikimate at pH 7.5)1 Publication
  5. KM=1.56 mM for quinate (at pH 7.5)1 Publication
  6. KM=2.37 mM for quinate (at pH 9)1 Publication
  7. KM=10.16 mM for shikimate(at pH 7.5)1 Publication
  8. KM=10.2 mM for quinate1 Publication
  9. KM=46.6 mM for shikimate1 Publication
  10. KM=53.8 mM for shikimate(at pH 10)1 Publication

    pH dependencei

    Optimum pH is 9-10.2 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: chorismate biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.Curated
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase (Cgl2178), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. Quinate/shikimate dehydrogenase (NAD(+)) (aroE)
    5. Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC)
    This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

    Pathwayi: 3,4-dihydroxybenzoate biosynthesis

    This protein is involved in the subpathway that synthesizes 3-dehydroquinate from D-quinate (NAD(+) route).Curated This subpathway is part of the pathway 3,4-dihydroxybenzoate biosynthesis, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway 3,4-dihydroxybenzoate biosynthesis and in Aromatic compound metabolism.

    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 sitei69Quinate/shikimateUniRule annotation1 Publication1
    <p>This subsection of the ‘Function’ 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 sitei73Proton acceptorUniRule annotation1 Publication1
    Binding sitei85NADPUniRule annotation1
    Binding sitei94Quinate/shikimateUniRule annotation1 Publication1
    Binding sitei110Quinate/shikimateUniRule annotation1 Publication1
    Binding sitei158NAD1 Publication1
    Binding sitei163NAD1 Publication1
    Binding sitei213NAD; via carbonyl oxygen1 Publication1
    Binding sitei228NAD; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei230ShikimateUniRule annotation1
    Binding sitei251NAD; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei258Quinate/shikimate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi137 – 138NADUniRule annotation1 Publication2
    Nucleotide bindingi203 – 206NAD1 Publication4

    <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 functionOxidoreductase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CORYNE:G18NG-9981-MONOMER
    MetaCyc:MONOMER-15330

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.24 960
    1.1.1.25 960

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

    More...
    UniPathwayi
    UPA00053;UER00087

    <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:
    Quinate/shikimate dehydrogenase (NAD(+))1 Publication (EC:1.1.1.-2 Publications, EC:1.1.1.242 Publications)
    Short name:
    QSDH1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:aroEUniRule annotation
    Synonyms:qsuD1 Publication
    <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>OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    <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 identifieri196627 [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 lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    <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
    • UP000000582 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section 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_00001360011 – 283Quinate/shikimate dehydrogenase (NAD(+))Add BLAST283

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9X5C9

    <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 shikimate, quinate and QsuR.By similarity

    <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

    Homodimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    196627.cg0504

    <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

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9X5C9

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

    More...
    SMRi
    Q9X5C9

    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
    Q9X5C9

    <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>Regioni17 – 19Quinate/shikimate bindingUniRule annotation1 Publication3

    <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 shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0169 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000237875

    KEGG Orthology (KO)

    More...
    KOi
    K00014

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HEHEGDA

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00222 Shikimate_DH_AroE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR013708 Shikimate_DH-bd_N
    IPR022893 Shikimate_DH_fam

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08501 Shikimate_dh_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 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.

    Q9X5C9-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD
    60 70 80 90 100
    LKTLLDAALY LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA
    110 120 130 140 150
    TGHTTGHNTD VSGFGRGMEE GLPNAKLDSV VQVGAGGVGN AVAYALVTHG
    160 170 180 190 200
    VQKLQVADLD TSRAQALADV INNAVGREAV VGVDARGIED VIAAADGVVN
    210 220 230 240 250
    ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA ARALGCETLD
    260 270 280
    GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL
    Length:283
    Mass (Da):29,697
    Last modified:July 26, 2002 - v2
    <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:i2DBCE25D186DAF74
    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 → P in AAD30993 (Ref. 1) Curated1
    Sequence conflicti135 – 143AGGVGNAVA → RRRRKRSR in AAD30993 (Ref. 1) Curated9
    Sequence conflicti211Missing in AAD30993 (Ref. 1) Curated1
    Sequence conflicti272 – 273DV → T in AAD30993 (Ref. 1) Curated2

    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
    AF124518 Genomic DNA Translation: AAD30993.1
    BA000036 Genomic DNA Translation: BAB97817.1
    BX927149 Genomic DNA Translation: CAF19140.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_599671.1, NC_003450.3
    WP_011013640.1, NC_006958.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAB97817; BAB97817; BAB97817
    CAF19140; CAF19140; cg0504

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1021203

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cgb:cg0504
    cgl:NCgl0409

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|196627.13.peg.423

    <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
    AF124518 Genomic DNA Translation: AAD30993.1
    BA000036 Genomic DNA Translation: BAB97817.1
    BX927149 Genomic DNA Translation: CAF19140.1
    RefSeqiNP_599671.1, NC_003450.3
    WP_011013640.1, NC_006958.1

    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
    2NLOX-ray1.64A1-283[»]
    3JYOX-ray1.00A1-283[»]
    3JYPX-ray1.16A1-283[»]
    3JYQX-ray1.16A1-283[»]
    ProteinModelPortaliQ9X5C9
    SMRiQ9X5C9
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi196627.cg0504

    Proteomic databases

    PRIDEiQ9X5C9

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB97817; BAB97817; BAB97817
    CAF19140; CAF19140; cg0504
    GeneIDi1021203
    KEGGicgb:cg0504
    cgl:NCgl0409
    PATRICifig|196627.13.peg.423

    Phylogenomic databases

    eggNOGiCOG0169 LUCA
    HOGENOMiHOG000237875
    KOiK00014
    OMAiHEHEGDA

    Enzyme and pathway databases

    UniPathwayi
    UPA00053;UER00087

    BioCyciCORYNE:G18NG-9981-MONOMER
    MetaCyc:MONOMER-15330
    BRENDAi1.1.1.24 960
    1.1.1.25 960

    Miscellaneous databases

    EvolutionaryTraceiQ9X5C9

    Family and domain databases

    HAMAPiMF_00222 Shikimate_DH_AroE, 1 hit
    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR013708 Shikimate_DH-bd_N
    IPR022893 Shikimate_DH_fam
    PfamiView protein in Pfam
    PF08501 Shikimate_dh_N, 1 hit
    SUPFAMiSSF51735 SSF51735, 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 nameiAROE_CORGL
    <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: Q9X5C9
    <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 1, 2000
    Last sequence update: July 26, 2002
    Last modified: December 5, 2018
    This is version 132 of the entry and version 2 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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