Skip Header

Contribute Send feedback
Read comments (?) or add your own

C5A0C6 (KDUI_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 31. 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
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:BWG_2579
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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.

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.

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: HAMAP

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

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: 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_1000212560

Sites

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

Sequences

Sequence LengthMass (Da)Tools
C5A0C6 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: F7CD5C259503CD1A

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

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

       130        140        150        160        170        180 
GTPAKFYYNC 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]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001396 Genomic DNA. Translation: ACR64105.1.
RefSeqYP_002927775.1. NC_012759.1.

3D structure databases

ProteinModelPortalC5A0C6.
SMRC5A0C6. Positions 1-277.
ModBaseSearch...

Protein-protein interaction databases

STRING595496.BWG_2579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR64105; ACR64105; BWG_2579.
GeneID7952257.
KEGGebw:BWG_2579.
PATRIC18274642. VBIEscCol60876_2824.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3717.
HOGENOMHOG000124379.
KOK01815.
OMAAGENYTF.
ProtClustDBPRK00924.

Enzyme and pathway databases

BioCycECOL595496:GI18-2564-MONOMER.
UniPathwayUPA00545; UER00826.

Family and domain databases

HAMAPMF_00687. KduI.
InterProIPR007045. KduI.
IPR021120. KduI/IolB_isomerase.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF04962. KduI. 1 hit.
[Graphical view]
PIRSFPIRSF006625. KduI. 1 hit.
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDUI_ECOBW
AccessionPrimary (citable) accession number: C5A0C6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 1, 2013
This is version 31 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents