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P0C0F4 (UDG_STRPY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-glucose 6-dehydrogenase
Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22
Gene names
Name:hasB
OrganismStreptococcus pyogenes
Taxonomic identifier1314 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=20 µM for UDP-glucose

KM=65 µM for NAD

Ontologies

Keywords
   Biological processCapsule biogenesis/degradation
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processUDP-glucuronate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

UDP-glucose 6-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402UDP-glucose 6-dehydrogenase
PRO_0000074054

Regions

Nucleotide binding2 – 1918NAD
Region142 – 1454Substrate binding
Region249 – 2535Substrate binding

Sites

Active site2601Nucleophile
Binding site291NAD
Binding site341NAD
Binding site831NAD
Binding site1181NAD; via amide nitrogen
Binding site1451NAD
Binding site2041Substrate
Binding site2571Substrate; via amide nitrogen
Binding site2631NAD
Binding site3191Substrate; via carbonyl oxygen
Binding site3201Substrate
Binding site3271NAD
Binding site4021Substrate

Experimental info

Mutagenesis1181T → A: Increases Km for substrate 3-fold. Increases Km for NAD 6-fold. Reduces catalytic activity 160-fold. Ref.2
Mutagenesis1411E → Q: Increases Km for substrate 3-fold. Increases Km for NAD 2-fold. Reduces catalytic activity about 10-fold. Ref.2
Mutagenesis1451E → Q: Increases Km for substrate 6-fold. Increases Km for NAD 3-fold. Reduces catalytic activity about 10-fold. Ref.2
Mutagenesis2601C → A or S: Loss of activity. Ref.2 Ref.3

Secondary structure

1 ............................................................... 402
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0F4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: DD1869D659F4CA58

FASTA40245,483
        10         20         30         40         50         60 
MKIAVAGSGY VGLSLGVLLS LQNEVTIVDI LPSKVDKINN GLSPIQDEYI EYYLKSKQLS 

        70         80         90        100        110        120 
IKATLDSKAA YKEAELVIIA TPTNYNSRIN YFDTQHVETV IKEVLSVNSH ATLIIKSTIP 

       130        140        150        160        170        180 
IGFITEMRQK FQTDRIIFSP EFLRESKALY DNLYPSRIIV SCEENDSPKV KADAEKFALL 

       190        200        210        220        230        240 
LKSAAKKNNV PVLIMGASEA EAVKLFANTY LALRVAYFNE LDTYAESRKL NSHMIIQGIS 

       250        260        270        280        290        300 
YDDRIGMHYN NPSFGYGGYC LPKDTKQLLA NYNNIPQTLI EAIVSSNNVR KSYIAKQIIN 

       310        320        330        340        350        360 
VLKEQESPVK VVGVYRLIMK SNSDNFRESA IKDVIDILKS KDIKIIIYEP MLNKLESEDQ 

       370        380        390        400 
SVLVNDLENF KKQANIIVTN RYDNELQDVK NKVYSRDIFG RD

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L08444 Genomic DNA. Translation: AAA26899.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLIX-ray2.31A1-402[»]
1DLJX-ray1.80A1-402[»]
1LTYmodel-A1-402[»]
ProteinModelPortalP0C0F4.
SMRP0C0F4. Positions 1-402.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1004.

Enzyme and pathway databases

SABIO-RKP0C0F4.
UniPathwayUPA00038; UER00491.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 2 hits.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
SSF52413. UDP-Glc/GDP-Man_DH_C. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C0F4.

Entry information

Entry nameUDG_STRPY
AccessionPrimary (citable) accession number: P0C0F4
Secondary accession number(s): Q07172
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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