Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0TDY9 (KDUI_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:
4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase

EC=5.3.1.17
Alternative name(s):
5-keto-4-deoxyuronate isomerase
DKI isomerase
Gene names
Name:kduI
Ordered Locus Names:ECP_2856
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate By similarity. HAMAP-Rule MF_00687

Catalytic activity

5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate. HAMAP-Rule MF_00687

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00687

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 4/5. HAMAP-Rule MF_00687

Subunit structure

Homohexamer By similarity. HAMAP-Rule MF_00687

Sequence similarities

Belongs to the KduI family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpectin catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2782784-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase HAMAP-Rule MF_00687
PRO_1000045082

Sites

Metal binding1961Zinc By similarity
Metal binding1981Zinc By similarity
Metal binding2031Zinc By similarity
Metal binding2451Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TDY9 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 7AF3DD98DE74D597

FASTA27831,076
        10         20         30         40         50         60 
MDVRQSIHSA HAKTLDTQGL RNEFLVEKVF VADEYTMVYS HIDRIIVGGI MPVTKTVSVG 

        70         80         90        100        110        120 
GEVGKQLGVS YFLERRELGV INIGGAGTIT VDGQCYEIGH RDALYVGKGA KEVVFASIDT 

       130        140        150        160        170        180 
ATPAKFYYNC APAHTTYPTK KVTPDEVSPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG 

       190        200        210        220        230        240 
LTELAPGNLW NTMPCHTHER RMEVYFYFNM DDDACVFHMM GQPQETRHIV MHNEQAVISP 

       250        260        270 
SWSIHSGVGT KAYTFIWGMV GENQVFDDMD HVAVKDLR 

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000247 Genomic DNA. Translation: ABG70840.1.
RefSeqYP_670741.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TDY9.
SMRQ0TDY9. Positions 1-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362663.ECP_2856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG70840; ABG70840; ECP_2856.
GeneID4188108.
KEGGecp:ECP_2856.
PATRIC18196542. VBIEscCol77757_2894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3717.
HOGENOMHOG000124379.
KOK01815.
OMAIWAMAGE.
OrthoDBEOG664CJZ.
PhylomeDBQ0TDY9.
ProtClustDBPRK00924.

Enzyme and pathway databases

BioCycECOL362663:GIY5-2877-MONOMER.
UniPathwayUPA00545; UER00826.

Family and domain databases

Gene3D2.60.120.500. 1 hit.
2.60.120.520. 1 hit.
HAMAPMF_00687. KduI.
InterProIPR007045. KduI.
IPR021120. KduI/IolB_isomerase.
IPR027447. KduI_C.
IPR027449. KduI_N.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF04962. KduI. 1 hit.
[Graphical view]
PIRSFPIRSF006625. KduI. 1 hit.
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDUI_ECOL5
AccessionPrimary (citable) accession number: Q0TDY9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 54 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