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Protein

UDP-N-acetylglucosamine 4,6-dehydratase (inverting)

Gene

pseB

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Has both C6 dehydratase and C5 epimerase activities that result in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose.1 Publication

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O.1 Publication

Cofactori

NADP+1 Publication

Kineticsi

  1. KM=159 µM for UDP-GlcNAc1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei87 – 871NADP; via carbonyl oxygen1 Publication
    Binding sitei91 – 911NADP1 Publication
    Binding sitei91 – 911Substrate
    Active sitei133 – 1331Curated
    Binding sitei141 – 1411NADP1 Publication
    Binding sitei145 – 1451NADP1 Publication
    Binding sitei173 – 1731Substrate
    Binding sitei181 – 1811Substrate; via amide nitrogen
    Binding sitei199 – 1991Substrate
    Binding sitei258 – 2581Substrate
    Binding sitei261 – 2611Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 224NADP1 Publication
    Nucleotide bindingi43 – 486NADP1 Publication
    Nucleotide bindingi67 – 682NADP1 Publication
    Nucleotide bindingi129 – 1302NADP1 Publication
    Nucleotide bindingi174 – 1785NADP1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciHPY:HP0840-MONOMER.
    MetaCyc:MONOMER-14516.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine 4,6-dehydratase (inverting) (EC:4.2.1.115)
    Alternative name(s):
    Pseudaminic acid biosynthesis protein B
    UDP-GlcNAc-inverting 4,6-dehydratase
    Gene namesi
    Name:pseB
    Synonyms:flaA1
    Ordered Locus Names:HP_0840
    OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
    Taxonomic identifieri85962 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    Proteomesi
    • UP000000429 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331K → A or E: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 333333UDP-N-acetylglucosamine 4,6-dehydratase (inverting)PRO_0000418954Add
    BLAST

    Proteomic databases

    PaxDbiO25511.
    PRIDEiO25511.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    IntActiO25511. 1 interaction.
    STRINGi85962.HP0840.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104Combined sources
    Beta strandi12 – 165Combined sources
    Turni17 – 193Combined sources
    Helixi21 – 3313Combined sources
    Beta strandi37 – 448Combined sources
    Helixi46 – 5611Combined sources
    Beta strandi61 – 655Combined sources
    Helixi71 – 777Combined sources
    Turni78 – 803Combined sources
    Beta strandi82 – 865Combined sources
    Helixi93 – 986Combined sources
    Helixi100 – 12021Combined sources
    Beta strandi124 – 1296Combined sources
    Helixi132 – 1343Combined sources
    Helixi140 – 15415Combined sources
    Helixi155 – 1573Combined sources
    Beta strandi160 – 1623Combined sources
    Beta strandi165 – 1695Combined sources
    Helixi181 – 19111Combined sources
    Beta strandi196 – 1994Combined sources
    Beta strandi204 – 2085Combined sources
    Helixi210 – 22314Combined sources
    Beta strandi229 – 2324Combined sources
    Beta strandi236 – 2383Combined sources
    Helixi239 – 2468Combined sources
    Beta strandi252 – 2543Combined sources
    Beta strandi266 – 2683Combined sources
    Helixi270 – 2756Combined sources
    Beta strandi276 – 2783Combined sources
    Beta strandi280 – 2856Combined sources
    Beta strandi315 – 3195Combined sources
    Helixi326 – 3305Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GN4X-ray1.90A/B1-333[»]
    2GN6X-ray2.70A/B1-333[»]
    2GN8X-ray2.10A/B1-333[»]
    2GN9X-ray2.80A/B1-333[»]
    2GNAX-ray2.60A/B1-333[»]
    ProteinModelPortaliO25511.
    SMRiO25511. Positions 5-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO25511.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polysaccharide synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C5E. Bacteria.
    COG1086. LUCA.
    KOiK15894.
    OMAiICIHAAA.
    OrthoDBiEOG6WQD59.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR003869. Polysac_CapD-like.
    IPR020025. PseB.
    [Graphical view]
    PfamiPF02719. Polysacc_synt_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR03589. PseB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O25511-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPNHQNMLDN QTILITGGTG SFGKCFVRKV LDTTNAKKII VYSRDELKQS
    60 70 80 90 100
    EMAMEFNDPR MRFFIGDVRD LERLNYALEG VDICIHAAAL KHVPIAEYNP
    110 120 130 140 150
    LECIKTNIMG ASNVINACLK NAISQVIALS TDKAANPINL YGATKLCSDK
    160 170 180 190 200
    LFVSANNFKG SSQTQFSVVR YGNVVGSRGS VVPFFKKLVQ NKASEIPITD
    210 220 230 240 250
    IRMTRFWITL DEGVSFVLKS LKRMHGGEIF VPKIPSMKMT DLAKALAPNT
    260 270 280 290 300
    PTKIIGIRPG EKLHEVMIPK DESHLALEFE DFFIIQPTIS FQTPKDYTLT
    310 320 330
    KLHEKGQKVA PDFEYSSHNN NQWLEPDDLL KLL
    Length:333
    Mass (Da):37,354
    Last modified:January 1, 1998 - v1
    Checksum:i8EF0A39F0FBF0516
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000511 Genomic DNA. Translation: AAD07887.1.
    PIRiH64624.
    RefSeqiNP_207633.1. NC_000915.1.
    WP_001132631.1. NC_000915.1.

    Genome annotation databases

    EnsemblBacteriaiAAD07887; AAD07887; HP_0840.
    GeneIDi899369.
    KEGGihpy:HP0840.
    PATRICi20592973. VBIHelPyl33062_0874.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000511 Genomic DNA. Translation: AAD07887.1.
    PIRiH64624.
    RefSeqiNP_207633.1. NC_000915.1.
    WP_001132631.1. NC_000915.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GN4X-ray1.90A/B1-333[»]
    2GN6X-ray2.70A/B1-333[»]
    2GN8X-ray2.10A/B1-333[»]
    2GN9X-ray2.80A/B1-333[»]
    2GNAX-ray2.60A/B1-333[»]
    ProteinModelPortaliO25511.
    SMRiO25511. Positions 5-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiO25511. 1 interaction.
    STRINGi85962.HP0840.

    Proteomic databases

    PaxDbiO25511.
    PRIDEiO25511.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD07887; AAD07887; HP_0840.
    GeneIDi899369.
    KEGGihpy:HP0840.
    PATRICi20592973. VBIHelPyl33062_0874.

    Phylogenomic databases

    eggNOGiENOG4105C5E. Bacteria.
    COG1086. LUCA.
    KOiK15894.
    OMAiICIHAAA.
    OrthoDBiEOG6WQD59.

    Enzyme and pathway databases

    BioCyciHPY:HP0840-MONOMER.
    MetaCyc:MONOMER-14516.

    Miscellaneous databases

    EvolutionaryTraceiO25511.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR003869. Polysac_CapD-like.
    IPR020025. PseB.
    [Graphical view]
    PfamiPF02719. Polysacc_synt_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR03589. PseB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700392 / 26695.
    2. "FlaA1, a new bifunctional UDP-GlcNAc C6 Dehydratase/ C4 reductase from Helicobacter pylori."
      Creuzenet C., Schur M.J., Li J., Wakarchuk W.W., Lam J.S.
      J. Biol. Chem. 275:34873-34880(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori."
      Schirm M., Soo E.C., Aubry A.J., Austin J., Thibault P., Logan S.M.
      Mol. Microbiol. 48:1579-1592(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. "Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction."
      Schoenhofen I.C., McNally D.J., Brisson J.R., Logan S.M.
      Glycobiology 16:8C-14C(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PATHWAY.
      Strain: ATCC 700392 / 26695.
    5. "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways."
      Schoenhofen I.C., McNally D.J., Vinogradov E., Whitfield D., Young N.M., Dick S., Wakarchuk W.W., Brisson J.R., Logan S.M.
      J. Biol. Chem. 281:723-732(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
      Strain: ATCC 700392 / 26695.
    6. "Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity."
      Ishiyama N., Creuzenet C., Miller W.L., Demendi M., Anderson E.M., Harauz G., Lam J.S., Berghuis A.M.
      J. Biol. Chem. 281:24489-24495(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP AND UDP-D-GALACTOPYRANOSE, COFACTOR, SUBUNIT, MUTAGENESIS OF LYS-133.
      Strain: ATCC 700392 / 26695.

    Entry informationi

    Entry nameiPSEB_HELPY
    AccessioniPrimary (citable) accession number: O25511
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: January 1, 1998
    Last modified: December 9, 2015
    This is version 85 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. Helicobacter pylori
      Helicobacter pylori (strain 26695): entries and gene names
    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.