Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Manual assertion based on experiment ini

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei148acetyl-CoA; via amide nitrogen1 Publication1
    Binding sitei154acetyl-CoA1 Publication1
    Binding sitei166acetyl-CoA; via amide nitrogen1 Publication1
    Binding sitei190acetyl-CoA1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi121H → A: Reduces activity 50-fold. 1 Publication1
    Mutagenesisi145W → A: Reduces activity 56-fold. 1 Publication1
    Mutagenesisi171Y → A: Reduces activity 48-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307701 – 215Polysialic acid O-acetyltransferaseAdd BLAST215

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Structurei

    Secondary structure

    1215
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 12Combined sources6
    Beta strandi14 – 17Combined sources4
    Beta strandi27 – 34Combined sources8
    Beta strandi36 – 39Combined sources4
    Beta strandi44 – 47Combined sources4
    Beta strandi49 – 56Combined sources8
    Beta strandi58 – 61Combined sources4
    Beta strandi66 – 74Combined sources9
    Beta strandi79 – 82Combined sources4
    Beta strandi90 – 95Combined sources6
    Beta strandi100 – 103Combined sources4
    Beta strandi113 – 117Combined sources5
    Beta strandi123 – 125Combined sources3
    Turni126 – 128Combined sources3
    Beta strandi138 – 140Combined sources3
    Beta strandi160 – 164Combined sources5
    Beta strandi180 – 182Combined sources3
    Turni183 – 186Combined sources4
    Beta strandi187 – 190Combined sources4
    Beta strandi192 – 195Combined sources4
    Helixi204 – 206Combined sources3
    Helixi211 – 214Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ93S40.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93S40.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni119 – 121acetyl-CoA binding1 Publication3
    Regioni171 – 172acetyl-CoA binding1 Publication2

    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
    PDB 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.
    SMRiQ93S40.
    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: November 2, 2016
    This is version 51 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.