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Q04872 (UDG_ECO11) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ugd
OrganismEscherichia coli O111:H-
Taxonomic identifier168927 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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.

Bacterial outer membrane biogenesis; lipopolysaccharide 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
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological_processUDP-glucuronate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipopolysaccharide 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388UDP-glucose 6-dehydrogenase
PRO_0000074044

Regions

Nucleotide binding2 – 1918NAD Potential

Sites

Active site2531 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04872 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: E85B4550BB1FA02F

FASTA38843,289
        10         20         30         40         50         60 
MKITISGTGY VGLSNGILIA QHHEVVALDI VPTKVEMLNQ KKSPIVDKEI EEYLATKQLN 

        70         80         90        100        110        120 
FRATTDKYDA YRDGTYVIIA TPTDYDPKTN YFNTSSVESV IRDVVDINPN AVMVIKSTIP 

       130        140        150        160        170        180 
VGFTNLLKER LGIDNIFFSP EFLREGRALY DNLHPSRIVI GERSERAGRF AALLQEGAVK 

       190        200        210        220        230        240 
KDIPTLFTDS TEAEAIKLFA NTYLALRVAY FNELDSYAES LGLNSRQIIE GVCLDPRIGN 

       250        260        270        280        290        300 
HYNNPSFGYG GYCLPKDTKQ LLANYASVPN NIIGAIVDAN RTRKDFIADS ILARKPKVVG 

       310        320        330        340        350        360 
VYRLIMKSGS DNFRASSIQG IMKRIKAKGV PVIIYEPVMV EDEFFHSRVV RDLTAFKNEA 

       370        380 
DIIISNRMTS ELADVADKVY TRGLFGSD 

« Hide

References

[1]"Repeat unit polysaccharides of bacteria: a model for polymerization resembling that of ribosomes and fatty acid synthetase, with a novel mechanism for determining chain length."
Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R.
Mol. Microbiol. 7:725-734(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O111:H- / M92 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z17241 Genomic DNA. Translation: CAA78939.1.
PIRS33668.

3D structure databases

ProteinModelPortalQ04872.
SMRQ04872. Positions 1-388.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00030.
UPA00038; 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. 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]
PANTHERPTHR11374. PTHR11374. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500134. UDPglc_DH_bac. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUDG_ECO11
AccessionPrimary (citable) accession number: Q04872
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways