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Reviewed, UniProtKB/Swiss-Prot Q47329 (UDG5_ECOLX)

Last modified November 25, 2008. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: kfiD
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the formation of UDP-glucuronic acid which is required for K5 capsule synthesis.

Catalytic activity

UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.

Pathway

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

Capsule biogenesis; capsule polysaccharide biosynthesis.

Post-translational modification

Phosphorylated on a tyrosine residue. It results in a significant increase of the dehydrogenase activity By similarity.

Sequence similarities

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

Ontologies

Keywords

   Biological processCapsule biogenesis/degradation
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 392392UDP-glucose 6-dehydrogenase
PRO_0000074045

Regions

Nucleotide binding6 – 2318NAD Potential

Sites

Active site2571 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47329-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 69E15A27FCD25C79

FASTA39244,108
        10         20         30         40         50         60 
MFGTLKITVS GAGYVGLSNG ILMAQNHEVV AFDTHQKKVD LLNDKLSPIE DKEIENYLST 

        70         80         90        100        110        120 
KILNFRATTN KYEAYKNANY VIIATPTNYD PGSNYFDTSS VEAVIRDVTE INPNAIMVVK 

       130        140        150        160        170        180 
STVPVGFTKT IKEHLGINNI IFSPEFLREG RALYDNLHPS RIIIGECSER AERLAVLFQE 

       190        200        210        220        230        240 
GAIKQNIPVL FTDSTEAEAI KLFSNTYLAM RVAFFNELDS YAESFGLNTR QIIDGVCLDP 

       250        260        270        280        290        300 
RIGNYYNNPS FGYGGYCLPK DTKQLLANYQ SVPNKLISAI VDANRTRKDF ITNVILKHRP 

       310        320        330        340        350        360 
QVVGVYRLIM KSGSDNFRDS SILGIIKRIK KKGVKVIIYE PLISGDTFFN SPLERELAIF 

       370        380        390 
KGKADIIITN RMSEELNDVV DKVYSRDLFK CD 

« Hide

References

[1]"Region 2 of the Escherichia coli K5 capsule gene cluster encoding proteins for the biosynthesis of the K5 polysaccharide."
Petit C., Rigg G., Pazzani C., Smith A., Sieberth V., Stevens M., Boulnois G., Jann K., Roberts I.S.
Mol. Microbiol. 17:611-620(1995) [PubMed: 8801416] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

X77617 Genomic DNA. Translation: CAA54708.1.
PIRS70197.

3D structure databases

HSSPHSSP built from PDB template 1DLI based on UniProtKB Q07172.
ModBaseSearch...

Family and domain databases

InterProIPR016040. NAD(P)-bd.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DHase_C.
IPR014026. UDP-Glc/GDP-Man_DHase_dimer.
IPR014028. UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732. UDP-Glc/GDP-Man_DHase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.
PANTHERPTHR11374. UDPG_MGDP_DH_Creg. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUDG5_ECOLX
AccessionPrimary (citable) accession number: Q47329
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents