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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Binding sitei120NAD2 PublicationsImported1
    Binding sitei169NAD2 PublicationsImported1
    Binding sitei173NAD2 PublicationsImported1
    Binding sitei199NAD; via amide nitrogen and carbonyl oxygen2 PublicationsImported1
    Binding sitei237Substrate2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi26 – 31NAD2 PublicationsImported6
    Nucleotide bindingi50 – 55NAD2 PublicationsImported6
    Nucleotide bindingi81 – 82NAD2 PublicationsImported2
    Nucleotide bindingi101 – 103NAD2 PublicationsImported3

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesunclassified EnterobacteralesPlesiomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi147S → T: No effect on epimerase activity. 1 Publication1
    Mutagenesisi236S → G: No effect on epimerase activity. 1 Publication1
    Mutagenesisi271R → G: No effect on epimerase activity. 1 Publication1
    Mutagenesisi307R → A: No effect on epimerase activity. 1 Publication1
    Mutagenesisi308H → A: No effect on epimerase activity. 1 Publication1
    Mutagenesisi309S → Y: Abolishes epimerase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004308511 – 345UDP-N-acetylglucosamine 4-epimeraseAdd BLAST345

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1345
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 17Combined sources12
    Beta strandi21 – 25Combined sources5
    Turni26 – 28Combined sources3
    Helixi30 – 41Combined sources12
    Beta strandi45 – 50Combined sources6
    Beta strandi52 – 54Combined sources3
    Helixi57 – 65Combined sources9
    Helixi69 – 72Combined sources4
    Beta strandi75 – 79Combined sources5
    Helixi85 – 91Combined sources7
    Turni92 – 94Combined sources3
    Beta strandi96 – 100Combined sources5
    Helixi107 – 112Combined sources6
    Helixi114 – 121Combined sources8
    Helixi123 – 134Combined sources12
    Beta strandi138 – 145Combined sources8
    Helixi146 – 149Combined sources4
    Beta strandi155 – 157Combined sources3
    Helixi168 – 187Combined sources20
    Beta strandi192 – 196Combined sources5
    Beta strandi198 – 201Combined sources4
    Helixi213 – 223Combined sources11
    Beta strandi228 – 233Combined sources6
    Helixi242 – 253Combined sources12
    Helixi257 – 259Combined sources3
    Beta strandi261 – 267Combined sources7
    Helixi274 – 286Combined sources13
    Beta strandi297 – 299Combined sources3
    Helixi314 – 320Combined sources7
    Helixi328 – 343Combined sources16

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ7BJX9.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni145 – 146Substrate binding2 Publications2
    Regioni196 – 198Substrate binding2 Publications3
    Regioni213 – 216Substrate binding2 Publications4
    Regioni228 – 230Substrate binding2 Publications3
    Regioni302 – 305Substrate binding2 Publications4

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase.
    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
    PDB 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.
    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.
    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: November 30, 2016
    This is version 62 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.