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Protein

N-acetylneuraminate lyase

Gene

nanA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.UniRule annotation1 Publication

Catalytic activityi

N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate.UniRule annotation1 Publication

Kineticsi

kcat is 250 min(-1) for the cleavage of Neu5Ac at pH 7.4, and is 260 min(-1) at pH 6.8.1 Publication

  1. KM=2.2 mM for N-acetylneuraminate (at pH 7.4)1 Publication
  2. KM=2.4 mM for N-acetylneuraminate (at pH 6.8)1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei137 – 1371Involved in proton transfer during cleavageUniRule annotation
    Active sitei165 – 1651Schiff-base intermediate with substrateUniRule annotation1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciSAUR93061:GIWJ-279-MONOMER.
    BRENDAi4.1.3.3. 3352.
    UniPathwayiUPA00629; UER00680.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylneuraminate lyase1 PublicationUniRule annotation (EC:4.1.3.3UniRule annotation1 Publication)
    Short name:
    NAL1 PublicationUniRule annotation
    Short name:
    Neu5Ac lyase1 PublicationUniRule annotation
    Alternative name(s):
    N-acetylneuraminate pyruvate-lyaseUniRule annotation
    N-acetylneuraminic acid aldolaseUniRule annotation
    Sialate lyaseUniRule annotation
    Sialic acid aldolaseUniRule annotation
    Sialic acid lyaseUniRule annotation
    Gene namesi
    Name:nanA1 PublicationUniRule annotation
    Ordered Locus Names:SAOUHSC_00295
    OrganismiStaphylococcus aureus (strain NCTC 8325)
    Taxonomic identifieri93061 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000008816 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651K → C: 3125-fold decrease in catalytic activity, and 3-fold increase in substrate affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 293293N-acetylneuraminate lyasePRO_1000066938Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00295.

    Structurei

    Secondary structure

    1
    293
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115Combined sources
    Helixi24 – 3613Combined sources
    Beta strandi41 – 477Combined sources
    Helixi48 – 503Combined sources
    Helixi52 – 543Combined sources
    Helixi57 – 6913Combined sources
    Beta strandi75 – 806Combined sources
    Helixi86 – 9914Combined sources
    Beta strandi102 – 1076Combined sources
    Helixi116 – 13015Combined sources
    Beta strandi134 – 1385Combined sources
    Helixi140 – 1434Combined sources
    Helixi149 – 1568Combined sources
    Beta strandi161 – 1666Combined sources
    Helixi171 – 18010Combined sources
    Beta strandi184 – 1885Combined sources
    Helixi191 – 1933Combined sources
    Helixi194 – 1996Combined sources
    Beta strandi203 – 2086Combined sources
    Helixi210 – 22516Combined sources
    Helixi229 – 24921Combined sources
    Helixi251 – 26010Combined sources
    Turni261 – 2633Combined sources
    Helixi278 – 2803Combined sources
    Helixi281 – 29111Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AH7X-ray2.30A/B/C/D2-293[»]
    4AHOX-ray2.00A/B/C/D1-293[»]
    4AHPX-ray2.10A/B/C/D2-293[»]
    4AHQX-ray1.95A/B/C/D2-293[»]
    4AMAX-ray2.35A/B/C/D2-293[»]
    ProteinModelPortaliQ2G160.
    SMRiQ2G160. Positions 2-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 492Substrate bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the DapA family. NanA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0329.
    HOGENOMiHOG000173608.
    KOiK01639.
    OMAiTGEFNML.
    OrthoDBiEOG6W7235.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01237. N_acetylneuram_lyase.
    InterProiIPR013785. Aldolase_TIM.
    IPR002220. DapA-like.
    IPR005264. NanA.
    IPR020625. Schiff_base-form_aldolases_AS.
    [Graphical view]
    PANTHERiPTHR12128. PTHR12128. 1 hit.
    PfamiPF00701. DHDPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001365. DHDPS. 1 hit.
    PRINTSiPR00146. DHPICSNTHASE.
    PROSITEiPS00666. DHDPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2G160-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNKDLKGLYA ALLVPFDENG QVNEQGLKQI AQNAIETEEL DGLYVNGSSG
    60 70 80 90 100
    ENFLLNTEQK KQVFKVAKEA VGDKVKLIAQ VGSLDLNEAI ELGKYATELG
    110 120 130 140 150
    YDALSAVTPF YYPFTFEEIR DYYFDIIEAT QNNMIIYAIP DLTGVNISIE
    160 170 180 190 200
    QFSELFNHEK IVGVKYTAPN FFLLERIRKA FPDKLILSGF DEMLVQATIS
    210 220 230 240 250
    GVDGAIGSTY NVNGRRARKI FDLARQGQIQ EAYQLQHDSN DIIETVLSMG
    260 270 280 290
    IYPTLKEILR HRGIDAGLPK RPFKPFNEAH RQTLDQLIAK YDL
    Length:293
    Mass (Da):33,043
    Last modified:March 21, 2006 - v1
    Checksum:i62D7DEFFDC1AF431
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000253 Genomic DNA. Translation: ABD29464.1.
    RefSeqiWP_001030738.1. NC_007795.1.
    YP_498885.1. NC_007795.1.

    Genome annotation databases

    EnsemblBacteriaiABD29464; ABD29464; SAOUHSC_00295.
    GeneIDi23196138.
    3918976.
    KEGGisao:SAOUHSC_00295.
    PATRICi19578184. VBIStaAur99865_0268.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000253 Genomic DNA. Translation: ABD29464.1.
    RefSeqiWP_001030738.1. NC_007795.1.
    YP_498885.1. NC_007795.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AH7X-ray2.30A/B/C/D2-293[»]
    4AHOX-ray2.00A/B/C/D1-293[»]
    4AHPX-ray2.10A/B/C/D2-293[»]
    4AHQX-ray1.95A/B/C/D2-293[»]
    4AMAX-ray2.35A/B/C/D2-293[»]
    ProteinModelPortaliQ2G160.
    SMRiQ2G160. Positions 2-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00295.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABD29464; ABD29464; SAOUHSC_00295.
    GeneIDi23196138.
    3918976.
    KEGGisao:SAOUHSC_00295.
    PATRICi19578184. VBIStaAur99865_0268.

    Phylogenomic databases

    eggNOGiCOG0329.
    HOGENOMiHOG000173608.
    KOiK01639.
    OMAiTGEFNML.
    OrthoDBiEOG6W7235.

    Enzyme and pathway databases

    UniPathwayiUPA00629; UER00680.
    BioCyciSAUR93061:GIWJ-279-MONOMER.
    BRENDAi4.1.3.3. 3352.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01237. N_acetylneuram_lyase.
    InterProiIPR013785. Aldolase_TIM.
    IPR002220. DapA-like.
    IPR005264. NanA.
    IPR020625. Schiff_base-form_aldolases_AS.
    [Graphical view]
    PANTHERiPTHR12128. PTHR12128. 1 hit.
    PfamiPF00701. DHDPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001365. DHDPS. 1 hit.
    PRINTSiPR00146. DHPICSNTHASE.
    PROSITEiPS00666. DHDPS_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The Staphylococcus aureus NCTC 8325 genome."
      Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
      (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 8325.
    2. "Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with gamma-thialysine by using a chemical mutagenesis strategy."
      Timms N., Windle C.L., Polyakova A., Ault J.R., Trinh C.H., Pearson A.R., Nelson A., Berry A.
      ChemBioChem 14:474-481(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME, WILD-TYPE AND MUTANTS CYS-165 AND GAMMA-THIALYSINE-165 IN COMPLEX WITH PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-165, ACTIVE SITE.
      Strain: NCTC 8325.

    Entry informationi

    Entry nameiNANA_STAA8
    AccessioniPrimary (citable) accession number: Q2G160
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: March 21, 2006
    Last modified: May 27, 2015
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    When the catalytic Lys-165 residue is replaced by the unnatural amino acid gamma-thialysine, the enzyme regains significant activity compared with the Cys-165 mutant; regains of approximately 17% of the wild-type catalytic efficiency.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.