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Protein

UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase

Gene

pseG

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleotide sugar hydrolase that catalyzes the fourth step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Mediates the removal of UDP from C-1 of UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose forming 2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.1 Publication

Catalytic activityi

UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + H2O = 2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose + UDP.1 Publication

Kineticsi

kcat is 27 sec(-1) (PubMed:16728396). Note=kcat is 25 sec(-1) (PubMed:19483088).2 Publications

  1. KM=174 µM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose2 Publications
  2. KM=250 µM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei17 – 171Proton acceptor1 Publication
    Binding sitei143 – 1431Substrate
    Binding sitei239 – 2391Substrate

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciCJEJ192222:GJTS-1285-MONOMER.
    BRENDAi3.6.1.57. 1087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase (EC:3.6.1.57)
    Alternative name(s):
    Pseudaminic acid biosynthesis protein G
    Gene namesi
    Name:pseG
    Ordered Locus Names:Cj1312
    OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
    Taxonomic identifieri192222 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    Proteomesi
    • UP000000799 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171H → F or L: Abolishes catalytic activity. 1 Publication
    Mutagenesisi17 – 171H → N: Strongly impaired catalytic activity. 1 Publication
    Mutagenesisi78 – 781Y → F: Impaired catalytic activity. 1 Publication
    Mutagenesisi255 – 2551N → A: Impaired catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 274274UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolasePRO_0000418931Add
    BLAST

    Proteomic databases

    PaxDbiQ0P8U5.
    PRIDEiQ0P8U5.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiQ0P8U5. 6 interactions.
    STRINGi192222.Cj1312.

    Structurei

    Secondary structure

    1
    274
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Turni11 – 133Combined sources
    Helixi16 – 2510Combined sources
    Beta strandi29 – 357Combined sources
    Helixi43 – 453Combined sources
    Beta strandi50 – 523Combined sources
    Beta strandi54 – 563Combined sources
    Helixi58 – 6811Combined sources
    Beta strandi71 – 755Combined sources
    Helixi82 – 9211Combined sources
    Beta strandi95 – 995Combined sources
    Beta strandi109 – 1135Combined sources
    Helixi120 – 1234Combined sources
    Turni124 – 1263Combined sources
    Beta strandi132 – 1365Combined sources
    Helixi137 – 1393Combined sources
    Helixi144 – 1496Combined sources
    Beta strandi158 – 1636Combined sources
    Beta strandi165 – 1673Combined sources
    Helixi172 – 1798Combined sources
    Beta strandi186 – 1905Combined sources
    Helixi197 – 2059Combined sources
    Beta strandi208 – 2158Combined sources
    Helixi219 – 2246Combined sources
    Beta strandi226 – 2349Combined sources
    Helixi235 – 2428Combined sources
    Beta strandi247 – 2504Combined sources
    Helixi254 – 2563Combined sources
    Helixi257 – 2659Combined sources
    Beta strandi269 – 2713Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HBMX-ray1.80A1-274[»]
    3HBNX-ray1.85A1-274[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0P8U5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 162Substrate binding
    Regioni234 – 2352Substrate binding

    Sequence similaritiesi

    Belongs to the PseG family.Curated

    Phylogenomic databases

    eggNOGiENOG4107DKY. Bacteria.
    COG3980. LUCA.
    HOGENOMiHOG000229436.
    KOiK15897.
    OMAiYEVEYRY.
    OrthoDBiEOG64R635.

    Family and domain databases

    InterProiIPR020023. PseG.
    [Graphical view]
    TIGRFAMsiTIGR03590. PseG. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q0P8U5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKVLFRSDSS SQIGFGHIKR DLVLAKQYSD VSFACLPLEG SLIDEIPYPV
    60 70 80 90 100
    YELSSESIYE LINLIKEEKF ELLIIDHYGI SVDDEKLIKL ETGVKILSFD
    110 120 130 140 150
    DEIKPHHCDI LLNVNAYAKA SDYEGLVPFK CEVRCGFSYA LIREEFYQEA
    160 170 180 190 200
    KENREKKYDF FICMGGTDIK NLSLQIASEL PKTKIISIAT SSSNPNLKKL
    210 220 230 240 250
    QKFAKLHNNI RLFIDHENIA KLMNESNKLI ISASSLVNEA LLLKANFKAI
    260 270
    CYVKNQESTA TWLAKKGYEV EYKY
    Length:274
    Mass (Da):31,319
    Last modified:September 19, 2006 - v1
    Checksum:iA65BF88D58502257
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35426.1.
    PIRiE81274.
    RefSeqiWP_002830499.1. NC_002163.1.
    YP_002344702.1. NC_002163.1.

    Genome annotation databases

    EnsemblBacteriaiCAL35426; CAL35426; Cj1312.
    GeneIDi905604.
    KEGGicje:Cj1312.
    PATRICi20059588. VBICamJej33762_1294.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35426.1.
    PIRiE81274.
    RefSeqiWP_002830499.1. NC_002163.1.
    YP_002344702.1. NC_002163.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HBMX-ray1.80A1-274[»]
    3HBNX-ray1.85A1-274[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ0P8U5. 6 interactions.
    STRINGi192222.Cj1312.

    Proteomic databases

    PaxDbiQ0P8U5.
    PRIDEiQ0P8U5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAL35426; CAL35426; Cj1312.
    GeneIDi905604.
    KEGGicje:Cj1312.
    PATRICi20059588. VBICamJej33762_1294.

    Phylogenomic databases

    eggNOGiENOG4107DKY. Bacteria.
    COG3980. LUCA.
    HOGENOMiHOG000229436.
    KOiK15897.
    OMAiYEVEYRY.
    OrthoDBiEOG64R635.

    Enzyme and pathway databases

    BioCyciCJEJ192222:GJTS-1285-MONOMER.
    BRENDAi3.6.1.57. 1087.

    Miscellaneous databases

    EvolutionaryTraceiQ0P8U5.

    Family and domain databases

    InterProiIPR020023. PseG.
    [Graphical view]
    TIGRFAMsiTIGR03590. PseG. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700819 / NCTC 11168.
    2. "PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked glycosyltransferase."
      Liu F., Tanner M.E.
      J. Biol. Chem. 281:20902-20909(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 700819 / NCTC 11168.
    3. "Structural and functional analysis of Campylobacter jejuni PseG: a udp-sugar hydrolase from the pseudaminic acid biosynthetic pathway."
      Rangarajan E.S., Proteau A., Cui Q., Logan S.M., Potetinova Z., Whitfield D., Purisima E.O., Cygler M., Matte A., Sulea T., Schoenhofen I.C.
      J. Biol. Chem. 284:20989-21000(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH URIDINE-5'-DIPHOSPHATE, ACTIVE SITE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-17; TYR-78 AND ASN-255.
      Strain: ATCC 700819 / NCTC 11168.

    Entry informationi

    Entry nameiPSEG_CAMJE
    AccessioniPrimary (citable) accession number: Q0P8U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: September 19, 2006
    Last modified: January 20, 2016
    This is version 52 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. 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.