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Protein

UDP-glucose 6-dehydrogenase

Gene

hasB

Organism
Streptococcus pyogenes
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis.

Catalytic activityi

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

Kineticsi

  1. KM=20 µM for UDP-glucose
  2. KM=65 µM for NAD

    Pathway:iUDP-alpha-D-glucuronate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose.
    Proteins known to be involved in this subpathway in this organism are:
    1. UDP-glucose 6-dehydrogenase (hasB)
    This subpathway is part of the pathway UDP-alpha-D-glucuronate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose, the pathway UDP-alpha-D-glucuronate biosynthesis and in Nucleotide-sugar biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei29 – 291NAD1 Publication
    Binding sitei34 – 341NAD1 Publication
    Binding sitei83 – 831NAD1 Publication
    Binding sitei118 – 1181NAD; via amide nitrogen1 Publication
    Binding sitei145 – 1451NAD1 Publication
    Binding sitei204 – 2041Substrate1 Publication
    Binding sitei257 – 2571Substrate; via amide nitrogen1 Publication
    Active sitei260 – 2601Nucleophile
    Binding sitei263 – 2631NAD1 Publication
    Binding sitei319 – 3191Substrate; via carbonyl oxygen1 Publication
    Binding sitei320 – 3201Substrate1 Publication
    Binding sitei327 – 3271NAD1 Publication
    Binding sitei402 – 4021Substrate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi2 – 1918NAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    • NAD binding Source: InterPro
    • UDP-glucose 6-dehydrogenase activity Source: CACAO

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Capsule biogenesis/degradation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP0C0F4.
    UniPathwayiUPA00038; UER00491.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 6-dehydrogenase (EC:1.1.1.22)
    Short name:
    UDP-Glc dehydrogenase
    Short name:
    UDP-GlcDH
    Short name:
    UDPGDH
    Gene namesi
    Name:hasB
    OrganismiStreptococcus pyogenes
    Taxonomic identifieri1314 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181T → A: Increases Km for substrate 3-fold. Increases Km for NAD 6-fold. Reduces catalytic activity 160-fold. 1 Publication
    Mutagenesisi141 – 1411E → Q: Increases Km for substrate 3-fold. Increases Km for NAD 2-fold. Reduces catalytic activity about 10-fold. 1 Publication
    Mutagenesisi145 – 1451E → Q: Increases Km for substrate 6-fold. Increases Km for NAD 3-fold. Reduces catalytic activity about 10-fold. 1 Publication
    Mutagenesisi260 – 2601C → A or S: Loss of activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 402402UDP-glucose 6-dehydrogenasePRO_0000074054Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi160490.SPy_2201.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi10 – 1910Combined sources
    Turni20 – 223Combined sources
    Beta strandi23 – 286Combined sources
    Helixi32 – 398Combined sources
    Helixi48 – 569Combined sources
    Beta strandi61 – 655Combined sources
    Helixi67 – 737Combined sources
    Beta strandi75 – 795Combined sources
    Turni87 – 904Combined sources
    Helixi95 – 10713Combined sources
    Beta strandi112 – 1154Combined sources
    Helixi123 – 1308Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi150 – 1534Combined sources
    Beta strandi158 – 1614Combined sources
    Helixi168 – 18417Combined sources
    Beta strandi186 – 1883Combined sources
    Beta strandi192 – 1954Combined sources
    Helixi197 – 22731Combined sources
    Helixi232 – 2409Combined sources
    Turni243 – 2453Combined sources
    Beta strandi247 – 2493Combined sources
    Helixi260 – 27213Combined sources
    Helixi279 – 30224Combined sources
    Beta strandi311 – 3155Combined sources
    Helixi330 – 33910Combined sources
    Beta strandi344 – 3485Combined sources
    Beta strandi361 – 3633Combined sources
    Helixi367 – 3737Combined sources
    Beta strandi375 – 3784Combined sources
    Helixi384 – 3929Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DLIX-ray2.31A1-402[»]
    1DLJX-ray1.80A1-402[»]
    1LTYmodel-A1-402[»]
    ProteinModelPortaliP0C0F4.
    SMRiP0C0F4. Positions 1-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C0F4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 1454Substrate binding
    Regioni249 – 2535Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1004.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028357. UDPglc_DH_bac.
    [Graphical view]
    PANTHERiPTHR11374. PTHR11374. 1 hit.
    PfamiPF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0C0F4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI
    60 70 80 90 100
    EYYLKSKQLS IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV
    110 120 130 140 150
    IKEVLSVNSH ATLIIKSTIP IGFITEMRQK FQTDRIIFSP EFLRESKALY
    160 170 180 190 200
    DNLYPSRIIV SCEENDSPKV KADAEKFALL LKSAAKKNNV PVLIMGASEA
    210 220 230 240 250
    EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMIIQGIS YDDRIGMHYN
    260 270 280 290 300
    NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN
    310 320 330 340 350
    VLKEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP
    360 370 380 390 400
    MLNKLESEDQ SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG

    RD
    Length:402
    Mass (Da):45,483
    Last modified:September 13, 2005 - v1
    Checksum:iDD1869D659F4CA58
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L08444 Genomic DNA. Translation: AAA26899.1.
    RefSeqiWP_011018341.1. NZ_JHTN01000039.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L08444 Genomic DNA. Translation: AAA26899.1.
    RefSeqiWP_011018341.1. NZ_JHTN01000039.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DLIX-ray2.31A1-402[»]
    1DLJX-ray1.80A1-402[»]
    1LTYmodel-A1-402[»]
    ProteinModelPortaliP0C0F4.
    SMRiP0C0F4. Positions 1-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi160490.SPy_2201.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiCOG1004.

    Enzyme and pathway databases

    UniPathwayiUPA00038; UER00491.
    SABIO-RKP0C0F4.

    Miscellaneous databases

    EvolutionaryTraceiP0C0F4.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    IPR017476. UDP-Glc/GDP-Man.
    IPR014027. UDP-Glc/GDP-Man_DH_C.
    IPR014026. UDP-Glc/GDP-Man_DH_dimer.
    IPR001732. UDP-Glc/GDP-Man_DH_N.
    IPR028357. UDPglc_DH_bac.
    [Graphical view]
    PANTHERiPTHR11374. PTHR11374. 1 hit.
    PfamiPF00984. UDPG_MGDP_dh. 1 hit.
    PF03720. UDPG_MGDP_dh_C. 1 hit.
    PF03721. UDPG_MGDP_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500134. UDPglc_DH_bac. 1 hit.
    PIRSF000124. UDPglc_GDPman_dh. 1 hit.
    SMARTiSM00984. UDPG_MGDP_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF52413. SSF52413. 1 hit.
    TIGRFAMsiTIGR03026. NDP-sugDHase. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity."
      Dougherty B.A., van de Rijn I.
      J. Biol. Chem. 268:7118-7124(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: WF50.
    2. "Active site residues and mechanism of UDP-glucose dehydrogenase."
      Ge X., Penney L.C., van de Rijn I., Tanner M.E.
      Eur. J. Biochem. 271:14-22(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-118; GLU-141; GLU-145 AND CYS-260.
    3. "The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation."
      Campbell R.E., Mosimann S.C., van De Rijn I., Tanner M.E., Strynadka N.C.
      Biochemistry 39:7012-7023(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, MUTAGENESIS OF CYS-260.

    Entry informationi

    Entry nameiUDG_STRPY
    AccessioniPrimary (citable) accession number: P0C0F4
    Secondary accession number(s): Q07172
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: September 13, 2005
    Last modified: June 24, 2015
    This is version 65 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

    External Data

    Dasty 3

    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 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.