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UniProtKB - P39306 (ULAF_ECOLI)

Entry version 146 (11 Dec 2019)
Sequence version 1 (01 Feb 1995)
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Protein

L-ribulose-5-phosphate 4-epimerase UlaF

Gene

ulaF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization.UniRule annotation1 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

Zn2+UniRule annotationBy similarityNote: Binds 1 zinc ion per subunit.UniRule annotationBy similarity

<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 25 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.1 Publication
  1. KM=657 µM for L-ribulose 5-phosphate (LRu5P)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: L-ascorbate degradation

    This protein is involved in step 4 of the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate.UniRule annotation1 Publication
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG), Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG), Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG)
    2. 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD), 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD), 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD)
    3. L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE)
    4. L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF)
    This subpathway is part of the pathway L-ascorbate degradation, which is itself part of Cofactor degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate, the pathway L-ascorbate degradation and in Cofactor degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi74ZincUniRule annotationBy similarity1
    Metal bindingi93Zinc; via tele nitrogenUniRule annotationBy similarity1
    Metal bindingi95Zinc; via tele nitrogenUniRule annotationBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei118Proton donor/acceptorUniRule annotationBy similarity1
    Metal bindingi167Zinc; via tele nitrogenUniRule annotationBy similarity1
    Active sitei225Proton donor/acceptorUniRule annotationBy similarity1

    <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

    • aldehyde-lyase activity Source: GO_Central
    • L-ribulose-phosphate 4-epimerase activity Source: EcoCyc
    • zinc ion binding Source: UniProtKB
    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 functionIsomerase
    Biological processCarbohydrate metabolism
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:G7860-MONOMER
    ECOL316407:JW4156-MONOMER
    MetaCyc:G7860-MONOMER

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

    More...    UniPathwayi    		UPA00263;UER00380

    <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:
    L-ribulose-5-phosphate 4-epimerase UlaF1 PublicationUniRule annotation (EC:5.1.3.4UniRule annotation1 Publication)
    Alternative name(s):
    L-ascorbate utilization protein F1 PublicationUniRule annotation
    Phosphoribulose isomeraseUniRule annotation
    <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:ulaF1 PublicationUniRule annotation
    Synonyms:sgaE, yjfX
    Ordered Locus Names:b4198, JW4156
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    <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_00001629211 – 228L-ribulose-5-phosphate 4-epimerase UlaFAdd BLAST228

    Proteomic databases

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

    More...    PaxDbi    		P39306

    PRoteomics IDEntifications database

    More...    PRIDEi    		P39306

    <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

    Induced by L-ascorbate. Repressed by UlaR.UniRule annotation2 Publications

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4262716, 6 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10868N

    Protein interaction database and analysis system

    More...    IntActi    		P39306, 12 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b4198

    <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

    3D structure databases

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

    More...    SMRi    		P39306

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <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>Regioni26 – 27Substrate bindingUniRule annotationBy similarity2
    Regioni43 – 44Substrate bindingUniRule annotationBy similarity2
    Regioni72 – 73Substrate bindingUniRule annotationBy similarity2

    <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 aldolase class II family. AraD/FucA subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4107R0P Bacteria
    COG0235 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000218183

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P39306

    KEGG Orthology (KO)

    More...    KOi    		K03077

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P39306

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.225.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01952 UlaF, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001303 Aldolase_II/adducin_N
    IPR036409 Aldolase_II/adducin_N_sf
    IPR023499 UlaF

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00596 Aldolase_II, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM01007 Aldolase_II, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53639 SSF53639, 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.

    P39306-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQKLKQQVFE ANMELPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM 
            60         70         80         90        100
    KAADMVVVDM SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT 
           110        120        130        140        150
    AWAQAGLAIP ALGTTHADYF FGDIPCTRGL SEEEVQGEYE LNTGKVIIET 
           160        170        180        190        200
    LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV HNAVVMEEVA KMAWIARGIN 
           210        220 
    PQLNHIDSFL MNKHFMRKHG PNAYYGQK
    Length:228
    Mass (Da):25,278
    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:i3E96E7E0261E36B6
    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
    		U14003 Genomic DNA Translation: AAA97094.1
    U00096 Genomic DNA Translation: AAC77155.1
    AP009048 Genomic DNA Translation: BAE78199.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S56423

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418619.1, NC_000913.3
    WP_001170847.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC77155; AAC77155; b4198
    BAE78199; BAE78199; BAE78199

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948711

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW4156
    eco:b4198

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2503

    <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
    		U14003 Genomic DNA Translation: AAA97094.1
    U00096 Genomic DNA Translation: AAC77155.1
    AP009048 Genomic DNA Translation: BAE78199.1
    PIRiS56423
    RefSeqiNP_418619.1, NC_000913.3
    WP_001170847.1, NZ_LN832404.1

    3D structure databases

    SMRiP39306
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4262716, 6 interactors
    DIPiDIP-10868N
    IntActiP39306, 12 interactors
    STRINGi511145.b4198

    Proteomic databases

    PaxDbiP39306
    PRIDEiP39306

    Genome annotation databases

    EnsemblBacteriaiAAC77155; AAC77155; b4198
    BAE78199; BAE78199; BAE78199
    GeneIDi948711
    KEGGiecj:JW4156
    eco:b4198
    PATRICifig|1411691.4.peg.2503

    Organism-specific databases

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

    More...    EchoBASEi    		EB2391

    Phylogenomic databases

    eggNOGiENOG4107R0P Bacteria
    COG0235 LUCA
    HOGENOMiHOG000218183
    InParanoidiP39306
    KOiK03077
    PhylomeDBiP39306

    Enzyme and pathway databases

    UniPathwayiUPA00263;UER00380
    BioCyciEcoCyc:G7860-MONOMER
    ECOL316407:JW4156-MONOMER
    MetaCyc:G7860-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P39306

    Family and domain databases

    Gene3Di3.40.225.10, 1 hit
    HAMAPiMF_01952 UlaF, 1 hit
    InterProiView protein in InterPro
    IPR001303 Aldolase_II/adducin_N
    IPR036409 Aldolase_II/adducin_N_sf
    IPR023499 UlaF
    PfamiView protein in Pfam
    PF00596 Aldolase_II, 1 hit
    SMARTiView protein in SMART
    SM01007 Aldolase_II, 1 hit
    SUPFAMiSSF53639 SSF53639, 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 nameiULAF_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: P39306
    Secondary accession number(s): Q2M6A7
    <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 11, 2019
    This is version 146 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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