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P0AB87

- FUCA_ECOLI

UniProt

P0AB87 - FUCA_ECOLI

Protein

L-fuculose phosphate aldolase

Gene

fucA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde.1 PublicationUniRule annotation

    Catalytic activityi

    L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.1 PublicationUniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.3 PublicationsUniRule annotation

    pH dependencei

    Optimum pH is 7.2.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731Proton acceptor1 Publication
    Metal bindingi73 – 731Zinc3 PublicationsUniRule annotation
    Metal bindingi92 – 921Zinc3 PublicationsUniRule annotation
    Metal bindingi94 – 941Zinc3 PublicationsUniRule annotation
    Active sitei113 – 1131Proton donor1 Publication
    Metal bindingi155 – 1551Zinc3 PublicationsUniRule annotation

    GO - Molecular functioni

    1. aldehyde-lyase activity Source: EcoCyc
    2. L-fuculose-phosphate aldolase activity Source: EcoCyc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. D-arabinose catabolic process Source: EcoCyc
    2. L-fucose catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:FUCPALDOL-MONOMER.
    ECOL316407:JW2771-MONOMER.
    MetaCyc:FUCPALDOL-MONOMER.
    SABIO-RKP0AB87.
    UniPathwayiUPA00563; UER00626.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-fuculose phosphate aldolaseUniRule annotation (EC:4.1.2.17UniRule annotation)
    Alternative name(s):
    L-fuculose-1-phosphate aldolaseUniRule annotation
    Gene namesi
    Name:fucAUniRule annotation
    Synonyms:fucC, prd
    Ordered Locus Names:b2800, JW2771
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10348. fucA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215L-fuculose phosphate aldolasePRO_0000162925Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP0AB87.

    Interactioni

    Subunit structurei

    Homotetramer.4 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    yneKP761501EBI-1130362,EBI-1128384

    Protein-protein interaction databases

    DIPiDIP-9710N.
    IntActiP0AB87. 1 interaction.
    STRINGi511145.b2800.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1917
    Helixi24 – 263
    Beta strandi29 – 346
    Beta strandi37 – 404
    Beta strandi42 – 443
    Helixi47 – 493
    Helixi52 – 543
    Beta strandi56 – 583
    Helixi74 – 8310
    Beta strandi89 – 935
    Helixi96 – 1049
    Beta strandi110 – 1123
    Helixi113 – 1186
    Beta strandi120 – 1234
    Beta strandi131 – 1333
    Helixi134 – 14310
    Beta strandi144 – 1463
    Beta strandi148 – 1525
    Turni153 – 1553
    Beta strandi156 – 1638
    Helixi164 – 18522
    Helixi196 – 20510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 1-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB87.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldolase class II family. AraD/FucA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0235.
    HOGENOMiHOG000218184.
    KOiK01628.
    OMAiYATFGTH.
    OrthoDBiEOG6HQSSQ.
    PhylomeDBiP0AB87.

    Family and domain databases

    Gene3Di3.40.225.10. 1 hit.
    HAMAPiMF_00987. FucA.
    InterProiIPR001303. Aldolase_II/adducin_N.
    IPR004782. FucA.
    [Graphical view]
    PfamiPF00596. Aldolase_II. 1 hit.
    [Graphical view]
    SMARTiSM01007. Aldolase_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF53639. SSF53639. 1 hit.
    TIGRFAMsiTIGR01086. fucA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AB87-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL    50
    TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA 100
    VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT 150
    LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA 200
    VVLEKFKTYG LRIEE 215
    Length:215
    Mass (Da):23,775
    Last modified:November 8, 2005 - v1
    Checksum:iBA9897E13ABE4A22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491008.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75842; AAC75842; b2800.
    BAE76872; BAE76872; BAE76872.
    GeneIDi12930230.
    947282.
    KEGGiecj:Y75_p2737.
    eco:b2800.
    PATRICi32121016. VBIEscCol129921_2900.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi B33495. ADECFP.
    RefSeqi NP_417280.1. NC_000913.3.
    YP_491008.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DZU X-ray 2.09 P 1-215 [» ]
    1DZV X-ray 1.86 P 1-215 [» ]
    1DZW X-ray 2.17 P 1-215 [» ]
    1DZX X-ray 2.18 P 1-215 [» ]
    1DZY X-ray 2.44 P 1-213 [» ]
    1DZZ X-ray 1.92 P 1-215 [» ]
    1E46 X-ray 2.55 P 1-215 [» ]
    1E47 X-ray 2.15 P 1-215 [» ]
    1E48 X-ray 1.97 P 1-215 [» ]
    1E49 X-ray 2.53 P 1-215 [» ]
    1E4A X-ray 2.15 P 1-215 [» ]
    1E4B X-ray 1.84 P 1-215 [» ]
    1E4C X-ray 1.66 P 1-215 [» ]
    1FUA X-ray 1.92 A 1-215 [» ]
    2FUA X-ray 2.00 A 1-215 [» ]
    3FUA X-ray 2.67 A 1-215 [» ]
    4FUA X-ray 2.43 A 1-215 [» ]
    ProteinModelPortali P0AB87.
    SMRi P0AB87. Positions 1-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9710N.
    IntActi P0AB87. 1 interaction.
    STRINGi 511145.b2800.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75842 ; AAC75842 ; b2800 .
    BAE76872 ; BAE76872 ; BAE76872 .
    GeneIDi 12930230.
    947282.
    KEGGi ecj:Y75_p2737.
    eco:b2800.
    PATRICi 32121016. VBIEscCol129921_2900.

    Organism-specific databases

    EchoBASEi EB0344.
    EcoGenei EG10348. fucA.

    Phylogenomic databases

    eggNOGi COG0235.
    HOGENOMi HOG000218184.
    KOi K01628.
    OMAi YATFGTH.
    OrthoDBi EOG6HQSSQ.
    PhylomeDBi P0AB87.

    Enzyme and pathway databases

    UniPathwayi UPA00563 ; UER00626 .
    BioCyci EcoCyc:FUCPALDOL-MONOMER.
    ECOL316407:JW2771-MONOMER.
    MetaCyc:FUCPALDOL-MONOMER.
    SABIO-RK P0AB87.

    Miscellaneous databases

    EvolutionaryTracei P0AB87.
    PROi P0AB87.

    Gene expression databases

    Genevestigatori P0AB87.

    Family and domain databases

    Gene3Di 3.40.225.10. 1 hit.
    HAMAPi MF_00987. FucA.
    InterProi IPR001303. Aldolase_II/adducin_N.
    IPR004782. FucA.
    [Graphical view ]
    Pfami PF00596. Aldolase_II. 1 hit.
    [Graphical view ]
    SMARTi SM01007. Aldolase_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53639. SSF53639. 1 hit.
    TIGRFAMsi TIGR01086. fucA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
      Lu Z., Lin E.C.C.
      Nucleic Acids Res. 17:4883-4884(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol."
      Chen Y.M., Lu Z., Lin E.C.C.
      J. Bacteriol. 171:6097-6105(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae."
      Conway T., Ingram L.O.
      J. Bacteriol. 171:3754-3759(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-215.
      Strain: K12.
    6. "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate."
      Ghalambor M.A., Heath E.C.
      J. Biol. Chem. 237:2427-2433(1962) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
      Strain: O111:B4.
    7. "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli."
      Dreyer M.K., Schulz G.E.
      J. Mol. Biol. 231:549-553(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS), COFACTOR, SUBUNIT.
    8. "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure."
      Dreyer M.K., Schulz G.E.
      J. Mol. Biol. 259:458-466(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC MECHANISM, COFACTOR, SUBUNIT, ACTIVE SITES.
    9. "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli."
      Dreyer M.K., Schulz G.E.
      Acta Crystallogr. D 52:1082-1091(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.
    10. "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis."
      Joerger A.C., Gosse C., Fessner W.-D., Schulz G.E.
      Biochemistry 39:6033-6041(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ZINC, MUTAGENESIS.
    11. "Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis."
      Joerger A.C., Mueller-Dieckmann C., Schulz G.E.
      J. Mol. Biol. 303:531-543(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF MUTANTS.

    Entry informationi

    Entry nameiFUCA_ECOLI
    AccessioniPrimary (citable) accession number: P0AB87
    Secondary accession number(s): P11550, Q2MA34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3