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Protein

Polysialic acid O-acetyltransferase

Gene

oatWY

Organism
Neisseria meningitidis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the O-acetylation of capsular polymeric sialic acid. Shows high substrate specificity toward polymers of sialic acid that contains a large number of residues.1 Publication

Catalytic activityi

Acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + polysialic acid acetylated at O-7 or O-9.1 Publication

Kineticsi

kcat is 1.3 sec(-1) with acetyl-CoA as substrate. kcat is 2.1 sec(-1) with polymer of sialic acid as substrate.1 Publication

  1. KM=210 µM for acetyl-CoA1 Publication
  2. KM=18.5 µM for polymer of sialic acid1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei148 – 1481acetyl-CoA; via amide nitrogen1 Publication
    Binding sitei154 – 1541acetyl-CoA1 Publication
    Binding sitei166 – 1661acetyl-CoA; via amide nitrogen1 Publication
    Binding sitei190 – 1901acetyl-CoA1 Publication

    GO - Molecular functioni

    • polysialic-acid O-acetyltransferase activity Source: UniProtKB

    GO - Biological processi

    • protein homotrimerization Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polysialic acid O-acetyltransferase1 Publication (EC:2.3.1.1361 Publication)
    Alternative name(s):
    Polysialyltransferase1 Publication
    Short name:
    PST1 Publication
    Gene namesi
    Name:oatWY1 Publication
    Synonyms:siaD1 Publication
    OrganismiNeisseria meningitidisImported
    Taxonomic identifieri487 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi121 – 1211H → A: Reduces activity 50-fold. 1 Publication
    Mutagenesisi145 – 1451W → A: Reduces activity 56-fold. 1 Publication
    Mutagenesisi171 – 1711Y → A: Reduces activity 48-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Polysialic acid O-acetyltransferasePRO_0000430770Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126Combined sources
    Beta strandi14 – 174Combined sources
    Beta strandi27 – 348Combined sources
    Beta strandi36 – 394Combined sources
    Beta strandi44 – 474Combined sources
    Beta strandi49 – 568Combined sources
    Beta strandi58 – 614Combined sources
    Beta strandi66 – 749Combined sources
    Beta strandi79 – 824Combined sources
    Beta strandi90 – 956Combined sources
    Beta strandi100 – 1034Combined sources
    Beta strandi113 – 1175Combined sources
    Beta strandi123 – 1253Combined sources
    Turni126 – 1283Combined sources
    Beta strandi138 – 1403Combined sources
    Beta strandi160 – 1645Combined sources
    Beta strandi180 – 1823Combined sources
    Turni183 – 1864Combined sources
    Beta strandi187 – 1904Combined sources
    Beta strandi192 – 1954Combined sources
    Helixi204 – 2063Combined sources
    Helixi211 – 2144Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WLCX-ray1.95A1-215[»]
    2WLDX-ray2.20A/B/C1-215[»]
    2WLEX-ray2.19A/B/C1-215[»]
    2WLFX-ray2.35A/B/C1-215[»]
    2WLGX-ray1.90A/B/C1-215[»]
    ProteinModelPortaliQ93S40.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93S40.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1213acetyl-CoA binding1 Publication
    Regioni171 – 1722acetyl-CoA binding1 Publication

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR001451. Hexapep.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q93S40-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGTHMYSEQG INNTINISTT SLTNATQLTV IGNNNSVYIG NNCKIVSSNI
    60 70 80 90 100
    RLKGNNITLF IADDVENMGL VCSLHSDCSL QIQAKTTMGN GEITIAEKGK
    110 120 130 140 150
    ISIGKDCMLA HGYEIRNTDM HPIYSLENGE RINHGKDVII GNHVWLGRNV
    160 170 180 190 200
    TILKGVCIPN NVVVGSHTVL YKSFKEPNCV IAGSPAKIVK ENIVWGRKMY
    210
    HSTMYDDPTL NEFYK
    Length:215
    Mass (Da):23,705
    Last modified:December 1, 2001 - v1
    Checksum:i27DEDA09223F1FBB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13969 Genomic DNA. Translation: CAC38867.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13969 Genomic DNA. Translation: CAC38867.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WLCX-ray1.95A1-215[»]
    2WLDX-ray2.20A/B/C1-215[»]
    2WLEX-ray2.19A/B/C1-215[»]
    2WLFX-ray2.35A/B/C1-215[»]
    2WLGX-ray1.90A/B/C1-215[»]
    ProteinModelPortaliQ93S40.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93S40.

    Family and domain databases

    InterProiIPR001451. Hexapep.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiOATWY_NEIME
    AccessioniPrimary (citable) accession number: Q93S40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: December 1, 2001
    Last modified: September 16, 2015
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Polymeric sialic acid-containing capsule provides a means for the bacteria to evade the immune response during infection by mimicking host sialic acid-containing cell surface structures. O-acetylation of the sialic acid residues of capsular polysaccharides alters their immunogenicity and susceptibility to glycosidases.1 Publication

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.