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Protein

UDP-N-acetylglucosamine 4-epimerase

Gene

wbgU

Organism
Plesiomonas shigelloides (Aeromonas shigelloides)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc). Has very low epimerase activity with UDP-Glc and UDP-Gal. Plays a role in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid, a building block of the O-antigen in bacterial lipopolysaccharide (LPS).Curated2 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine.2 Publications

Cofactori

NAD+3 PublicationsNote: Binds 1 NAD+ per subunit.3 Publications

Kineticsi

kcat is 461 (s-1) with UDP-GlcNAc. kcat is 1038 (s-1) with UDP-GalNAc.1 Publication

  1. KM=131 µM for UDP-GalNAc1 Publication
  2. KM=137 µM for UDP-GalNAc1 Publication

    pH dependencei

    Optimum pH is 7.0-9.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Pathwayi: LPS O-antigen biosynthesis

    This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.2 PublicationsCurated
    View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201NAD2 PublicationsImported
    Binding sitei169 – 1691NAD2 PublicationsImported
    Binding sitei173 – 1731NAD2 PublicationsImported
    Binding sitei199 – 1991NAD; via amide nitrogen and carbonyl oxygen2 PublicationsImported
    Binding sitei237 – 2371Substrate2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 316NAD2 PublicationsImported
    Nucleotide bindingi50 – 556NAD2 PublicationsImported
    Nucleotide bindingi81 – 822NAD2 PublicationsImported
    Nucleotide bindingi101 – 1033NAD2 PublicationsImported

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13183.
    BRENDAi5.1.3.7. 4904.
    UniPathwayiUPA00281.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine 4-epimerase (EC:5.1.3.72 Publications)
    Alternative name(s):
    UDP-GalNAc 4-epimerase2 Publications
    Gene namesi
    Name:wbgUImported
    OrganismiPlesiomonas shigelloides (Aeromonas shigelloides)Imported
    Taxonomic identifieri703 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePlesiomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi147 – 1471S → T: No effect on epimerase activity. 1 Publication
    Mutagenesisi236 – 2361S → G: No effect on epimerase activity. 1 Publication
    Mutagenesisi271 – 2711R → G: No effect on epimerase activity. 1 Publication
    Mutagenesisi307 – 3071R → A: No effect on epimerase activity. 1 Publication
    Mutagenesisi308 – 3081H → A: No effect on epimerase activity. 1 Publication
    Mutagenesisi309 – 3091S → Y: Abolishes epimerase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345UDP-N-acetylglucosamine 4-epimerasePRO_0000430851Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1712Combined sources
    Beta strandi21 – 255Combined sources
    Turni26 – 283Combined sources
    Helixi30 – 4112Combined sources
    Beta strandi45 – 506Combined sources
    Beta strandi52 – 543Combined sources
    Helixi57 – 659Combined sources
    Helixi69 – 724Combined sources
    Beta strandi75 – 795Combined sources
    Helixi85 – 917Combined sources
    Turni92 – 943Combined sources
    Beta strandi96 – 1005Combined sources
    Helixi107 – 1126Combined sources
    Helixi114 – 1218Combined sources
    Helixi123 – 13412Combined sources
    Beta strandi138 – 1458Combined sources
    Helixi146 – 1494Combined sources
    Beta strandi155 – 1573Combined sources
    Helixi168 – 18720Combined sources
    Beta strandi192 – 1965Combined sources
    Beta strandi198 – 2014Combined sources
    Helixi213 – 22311Combined sources
    Beta strandi228 – 2336Combined sources
    Helixi242 – 25312Combined sources
    Helixi257 – 2593Combined sources
    Beta strandi261 – 2677Combined sources
    Helixi274 – 28613Combined sources
    Beta strandi297 – 2993Combined sources
    Helixi314 – 3207Combined sources
    Helixi328 – 34316Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LU1X-ray2.50A/B/C/D1-345[»]
    3RU7X-ray2.60A/B/C/D1-345[»]
    3RU9X-ray2.21A/B/C/D1-345[»]
    3RUAX-ray2.10A/B/C/D1-345[»]
    3RUCX-ray2.10A/B/C/D1-345[»]
    3RUDX-ray2.30A/B/C/D1-345[»]
    3RUEX-ray2.80A/B/S/b1-345[»]
    3RUFX-ray2.00A/B/S/b1-345[»]
    3RUHX-ray2.88A/B/C/D1-345[»]
    ProteinModelPortaliQ7BJX9.
    SMRiQ7BJX9. Positions 5-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7BJX9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni145 – 1462Substrate binding2 Publications
    Regioni196 – 1983Substrate binding2 Publications
    Regioni213 – 2164Substrate binding2 Publications
    Regioni228 – 2303Substrate binding2 Publications
    Regioni302 – 3054Substrate binding2 Publications

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR008089. Nuc_sugar_epim.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    PRINTSiPR01713. NUCEPIMERASE.
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7BJX9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDIYMSRYEE ITQQLIFSPK TWLITGVAGF IGSNLLEKLL KLNQVVIGLD
    60 70 80 90 100
    NFSTGHQYNL DEVKTLVSTE QWSRFCFIEG DIRDLTTCEQ VMKGVDHVLH
    110 120 130 140 150
    QAALGSVPRS IVDPITTNAT NITGFLNILH AAKNAQVQSF TYAASSSTYG
    160 170 180 190 200
    DHPALPKVEE NIGNPLSPYA VTKYVNEIYA QVYARTYGFK TIGLRYFNVF
    210 220 230 240 250
    GRRQDPNGAY AAVIPKWTAA MLKGDDVYIN GDGETSRDFC YIDNVIQMNI
    260 270 280 290 300
    LSALAKDSAK DNIYNVAVGD RTTLNELSGY IYDELNLIHH IDKLSIKYRE
    310 320 330 340
    FRSGDVRHSQ ADVTKAIDLL KYRPNIKIRE GLRLSMPWYV RFLKG
    Length:345
    Mass (Da):38,949
    Last modified:July 5, 2004 - v1
    Checksum:i90A364D247CCA810
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF285970 Genomic DNA. Translation: AAG17409.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF285970 Genomic DNA. Translation: AAG17409.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LU1X-ray2.50A/B/C/D1-345[»]
    3RU7X-ray2.60A/B/C/D1-345[»]
    3RU9X-ray2.21A/B/C/D1-345[»]
    3RUAX-ray2.10A/B/C/D1-345[»]
    3RUCX-ray2.10A/B/C/D1-345[»]
    3RUDX-ray2.30A/B/C/D1-345[»]
    3RUEX-ray2.80A/B/S/b1-345[»]
    3RUFX-ray2.00A/B/S/b1-345[»]
    3RUHX-ray2.88A/B/C/D1-345[»]
    ProteinModelPortaliQ7BJX9.
    SMRiQ7BJX9. Positions 5-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00281.
    BioCyciMetaCyc:MONOMER-13183.
    BRENDAi5.1.3.7. 4904.

    Miscellaneous databases

    EvolutionaryTraceiQ7BJX9.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR008089. Nuc_sugar_epim.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    PRINTSiPR01713. NUCEPIMERASE.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGNE_PLESH
    AccessioniPrimary (citable) accession number: Q7BJX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: July 5, 2004
    Last modified: December 9, 2015
    This is version 59 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

    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.