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Protein

L-fuculose phosphate aldolase

Gene

fucA

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 degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde (PubMed:13898172, Ref. 8, Ref. 9, PubMed:10821675, PubMed:11054289). Also able to catalyze the reversible cleavage of D-ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has a strong preference for L-configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref. 8, PubMed:10821675). FucA generates a vicinal diol unit having the absolute (3R,4R)-cis configuration (D-erythro) (Ref. 8, PubMed:10821675).6 Publications

Miscellaneous

During catalysis the binding of dihydroxyacetone phosphate (DHAP) frees Glu-73 residue from its interaction with zinc ion (PubMed:10821675, PubMed:11054289). Then Glu-73 residue abstracts a proton from the C3 atom of dihydroxyacetone phosphate (DHAP) (or from the O4 atom of L-fuculose 1-phosphate (Fuc1P) in the backward reaction), and moves to transfer its proton to the aldehyde oxygen atom (or to the C3 atom of dihydroxyacetone phosphate (DHAP)) (PubMed:10821675, PubMed:11054289).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

Zn2+UniRule annotation6 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation5 Publications

<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 phosphoglycolohydroxamate (PGH).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 19.3 sec(-1) for L-fuculose 1-phosphate (Fuc1P) as substrate.1 Publication
  1. KM=0.7 mM for L-fuculose 1-phosphate (Fuc1P)1 Publication
  2. KM=1.5 mM for L-fuculose 1-phosphate (Fuc1P)1 Publication
  3. KM=2.2 mM for L-fuculose 1-phosphate (Fuc1P)1 Publication

    pH dependencei

    Optimum pH is 7.2.1 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-fucose degradation

    This protein is involved in step 3 of the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose.UniRule annotation1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-fucose isomerase (fucI)
    2. L-fuculokinase (fucK)
    3. L-fuculose phosphate aldolase (fucA)
    This subpathway is part of the pathway L-fucose degradation, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose, the pathway L-fucose degradation and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 donor/acceptor2 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 bindingi73Zinc; catalyticUniRule annotationCombined sources4 Publications1
    Metal bindingi92Zinc; via tele nitrogenUniRule annotationCombined sources4 Publications1
    Metal bindingi94Zinc; via tele nitrogenUniRule annotationCombined sources4 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei113Plays a key role in the stabilization of the transition state and positioning the aldehyde component1 Publication1
    Sitei131Plays a key role in the stabilization of the transition state and positioning the aldehyde component1 Publication1
    Metal bindingi155Zinc; via tele nitrogenUniRule annotationCombined sources4 Publications1
    Sitei209Plays a key role in the stabilization of the transition state and positioning the aldehyde component1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    • D-arabinose catabolic process Source: EcoCyc
    • L-fucose catabolic process Source: EcoCyc
    • pentose catabolic process Source: GO_Central

    <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 functionLyase
    Biological processArabinose catabolism, Carbohydrate metabolism, Fucose metabolism
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:FUCPALDOL-MONOMER
    MetaCyc:FUCPALDOL-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.2.17 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0AB87

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

    More...
    UniPathwayi
    UPA00563;UER00626

    <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-fuculose phosphate aldolase1 PublicationUniRule annotation (EC:4.1.2.17UniRule annotation5 Publications)
    Alternative name(s):
    D-ribulose-phosphate aldolase1 PublicationUniRule annotation
    L-fuculose-1-phosphate aldolase1 PublicationUniRule 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:fucA1 PublicationUniRule annotation
    Synonyms:fucC, prd
    Ordered Locus Names:b2800, JW2771
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10348 fucA

    <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

    • cytosol Source: GO_Central

    <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>Mutagenesisi26T → A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). 1 Publication1
    Mutagenesisi27Missing : Strong decrease of the aldolase activity. 1 Publication1
    Mutagenesisi29N → L: Loss of aldolase activity; when associated with A-71. 1 Publication1
    Mutagenesisi29N → Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). 1 Publication1
    Mutagenesisi71S → A: Loss of aldolase activity; when associated with L-29. 1 Publication1
    Mutagenesisi71S → Q: Loss of aldolase activity. 1 Publication1
    Mutagenesisi73E → Q: Loss of aldolase activity; when associated with F-113 and F-209. 1 Publication1
    Mutagenesisi73E → S: Loss of aldolase activity. 2 Publications1
    Mutagenesisi113Y → F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209. 2 Publications1
    Mutagenesisi131F → A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206. 1 Publication1
    Mutagenesisi206F → W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131. 1 Publication1
    Mutagenesisi207 – 215Missing : Loss of aldolase activity. Has a slight preference for the D-aldehyde. 1 Publication9
    Mutagenesisi209Y → F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113. 2 Publications1
    Mutagenesisi211 – 215Missing : Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). 1 Publication5

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03026 Phosphoglycolohydroxamic Acid

    <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_00001629251 – 215L-fuculose phosphate aldolaseAdd BLAST215

    Proteomic databases

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

    More...
    PaxDbi
    P0AB87

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0AB87

    <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 L-fucose.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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

    Homotetramer.UniRule annotation5 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259224, 20 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9710N

    Protein interaction database and analysis system

    More...
    IntActi
    P0AB87, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_2969

    <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

    1215
    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
    P0AB87

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

    More...
    SMRi
    P0AB87

    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
    P0AB87

    <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>Regioni28 – 29Substrate bindingCombined sources2 Publications2
    Regioni43 – 44Substrate bindingCombined sources2 Publications2
    Regioni71 – 72Substrate bindingCombined sources2 Publications2

    <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 annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107W7X Bacteria
    COG0235 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000218184

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0AB87

    KEGG Orthology (KO)

    More...
    KOi
    K01628

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0AB87

    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_00987 FucA, 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
    IPR004782 FucA

    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

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01086 fucA, 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.

    P0AB87-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL
    60 70 80 90 100
    TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA
    110 120 130 140 150
    VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT
    160 170 180 190 200
    LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA
    210
    VVLEKFKTYG LRIEE
    Length:215
    Mass (Da):23,775
    Last modified:November 8, 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:iBA9897E13ABE4A22
    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
    M31059 Genomic DNA Translation: AAA23823.1
    X15025 Genomic DNA Translation: CAA33125.1
    U29581 Genomic DNA Translation: AAB40450.1
    U00096 Genomic DNA Translation: AAC75842.1
    AP009048 Genomic DNA Translation: BAE76872.1
    M27177 Genomic DNA No translation available.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B33495 ADECFP

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417280.1, NC_000913.3
    WP_000440781.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75842; AAC75842; b2800
    BAE76872; BAE76872; BAE76872

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947282

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2771
    eco:b2800

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3933

    <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
    M31059 Genomic DNA Translation: AAA23823.1
    X15025 Genomic DNA Translation: CAA33125.1
    U29581 Genomic DNA Translation: AAB40450.1
    U00096 Genomic DNA Translation: AAC75842.1
    AP009048 Genomic DNA Translation: BAE76872.1
    M27177 Genomic DNA No translation available.
    PIRiB33495 ADECFP
    RefSeqiNP_417280.1, NC_000913.3
    WP_000440781.1, 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
    1DZUX-ray2.09P1-215[»]
    1DZVX-ray1.86P1-215[»]
    1DZWX-ray2.17P1-215[»]
    1DZXX-ray2.18P1-215[»]
    1DZYX-ray2.44P1-213[»]
    1DZZX-ray1.92P1-215[»]
    1E46X-ray2.55P1-215[»]
    1E47X-ray2.15P1-215[»]
    1E48X-ray1.97P1-215[»]
    1E49X-ray2.53P1-215[»]
    1E4AX-ray2.15P1-215[»]
    1E4BX-ray1.84P1-215[»]
    1E4CX-ray1.66P1-215[»]
    1FUAX-ray1.92A1-215[»]
    2FUAX-ray2.00A1-215[»]
    3FUAX-ray2.67A1-215[»]
    4FUAX-ray2.43A1-215[»]
    ProteinModelPortaliP0AB87
    SMRiP0AB87
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259224, 20 interactors
    DIPiDIP-9710N
    IntActiP0AB87, 1 interactor
    STRINGi316385.ECDH10B_2969

    Chemistry databases

    DrugBankiDB03026 Phosphoglycolohydroxamic Acid

    Proteomic databases

    PaxDbiP0AB87
    PRIDEiP0AB87

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75842; AAC75842; b2800
    BAE76872; BAE76872; BAE76872
    GeneIDi947282
    KEGGiecj:JW2771
    eco:b2800
    PATRICifig|1411691.4.peg.3933

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0344
    EcoGeneiEG10348 fucA

    Phylogenomic databases

    eggNOGiENOG4107W7X Bacteria
    COG0235 LUCA
    HOGENOMiHOG000218184
    InParanoidiP0AB87
    KOiK01628
    PhylomeDBiP0AB87

    Enzyme and pathway databases

    UniPathwayi
    UPA00563;UER00626

    BioCyciEcoCyc:FUCPALDOL-MONOMER
    MetaCyc:FUCPALDOL-MONOMER
    BRENDAi4.1.2.17 2026
    SABIO-RKiP0AB87

    Miscellaneous databases

    EvolutionaryTraceiP0AB87

    Protein Ontology

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    PROi
    PR:P0AB87

    Family and domain databases

    Gene3Di3.40.225.10, 1 hit
    HAMAPiMF_00987 FucA, 1 hit
    InterProiView protein in InterPro
    IPR001303 Aldolase_II/adducin_N
    IPR036409 Aldolase_II/adducin_N_sf
    IPR004782 FucA
    PfamiView protein in Pfam
    PF00596 Aldolase_II, 1 hit
    SMARTiView protein in SMART
    SM01007 Aldolase_II, 1 hit
    SUPFAMiSSF53639 SSF53639, 1 hit
    TIGRFAMsiTIGR01086 fucA, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    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 nameiFUCA_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: P0AB87
    Secondary accession number(s): P11550, Q2MA34
    <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: November 8, 2005
    Last sequence update: November 8, 2005
    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, 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
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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