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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

Manual assertion based on experiment ini

  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: N-acetylneuraminate degradation

    This protein is involved in step 1 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. N-acetylneuraminate lyase (nanA)
    2. no protein annotated in this organism
    3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
    4. no protein annotated in this organism
    5. Glucosamine-6-phosphate deaminase (nagB)
    This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei137Involved in proton transfer during cleavageUniRule annotation1
    Active sitei165Schiff-base intermediate with substrateUniRule annotation1 Publication1

    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

    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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
    Proteomesi
    • UP000008816 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi165K → C: 3125-fold decrease in catalytic activity, and 3-fold increase in substrate affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_10000669381 – 293N-acetylneuraminate lyaseAdd BLAST293

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00295.

    Structurei

    Secondary structure

    1293
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 11Combined sources5
    Helixi24 – 36Combined sources13
    Beta strandi41 – 47Combined sources7
    Helixi48 – 50Combined sources3
    Helixi52 – 54Combined sources3
    Helixi57 – 69Combined sources13
    Beta strandi75 – 80Combined sources6
    Helixi86 – 99Combined sources14
    Beta strandi102 – 107Combined sources6
    Helixi116 – 130Combined sources15
    Beta strandi134 – 137Combined sources4
    Helixi140 – 143Combined sources4
    Helixi149 – 156Combined sources8
    Beta strandi161 – 164Combined sources4
    Helixi171 – 180Combined sources10
    Beta strandi184 – 188Combined sources5
    Helixi191 – 193Combined sources3
    Helixi194 – 199Combined sources6
    Beta strandi203 – 208Combined sources6
    Helixi210 – 226Combined sources17
    Helixi229 – 249Combined sources21
    Helixi251 – 261Combined sources11
    Helixi278 – 280Combined sources3
    Helixi281 – 291Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5A8GX-ray1.72A/B2-293[»]
    ProteinModelPortaliQ2G160.
    SMRiQ2G160.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni48 – 49Substrate bindingUniRule annotation1 Publication2

    Sequence similaritiesi

    Belongs to the DapA family. NanA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4107SCR. Bacteria.
    COG0329. LUCA.
    HOGENOMiHOG000173608.
    KOiK01639.
    OMAiTGEFNML.

    Family and domain databases

    CDDicd00954. NAL. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01237. N_acetylneuram_lyase. 1 hit.
    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.
    SMARTiSM01130. DHDPS. 1 hit.
    [Graphical view]
    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.
    GeneIDi28379356.
    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
    PDB 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[»]
    5A8GX-ray1.72A/B2-293[»]
    ProteinModelPortaliQ2G160.
    SMRiQ2G160.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00295.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABD29464; ABD29464; SAOUHSC_00295.
    GeneIDi28379356.
    3918976.
    KEGGisao:SAOUHSC_00295.
    PATRICi19578184. VBIStaAur99865_0268.

    Phylogenomic databases

    eggNOGiENOG4107SCR. Bacteria.
    COG0329. LUCA.
    HOGENOMiHOG000173608.
    KOiK01639.
    OMAiTGEFNML.

    Enzyme and pathway databases

    UniPathwayiUPA00629; UER00680.
    BRENDAi4.1.3.3. 3352.

    Family and domain databases

    CDDicd00954. NAL. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01237. N_acetylneuram_lyase. 1 hit.
    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.
    SMARTiSM01130. DHDPS. 1 hit.
    [Graphical view]
    PROSITEiPS00666. DHDPS_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 73 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

    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 one 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.