4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase

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Reviewed, UniProtKB/Swiss-Prot Q46938 (KDUI_ECOLI)

Last modified June 16, 2009. Version 65. History...

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

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Names and origin

Protein names

Recommended 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
Synonyms:	yqeE
Ordered Locus Names:	b2843, JW2811

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	4-deoxy-L-threo-5-hexosulose uronate = 3-deoxy-D-glycero-2,5-hexodiulosonate. HAMAP MF_00687
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconic acid from pectin: step 4/5. HAMAP MF_00687
Subunit structure	Homohexamer. HAMAP MF_00687
Sequence similarities	Belongs to the kduI family.

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Ontologies

Keywords
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	pectin catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 278

278

4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase HAMAP MF_00687

PRO_0000215485

Secondary structure

278

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q46938-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F7CD5C259503CD1A
Show »

FASTA

278

31,076

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli." Dunten P., Jaffe H., Aksamit R.R. Acta Crystallogr. D 54:678-680(1998) [PubMed: 9761873] [Abstract] Cited for: CRYSTALLIZATION, PROTEIN SEQUENCE OF 1-20 AND 227-247.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U29581 Genomic DNA. Translation: AAB40490.1.
U00096 Genomic DNA. Translation: AAC75882.1.
AP009048 Genomic DNA. Translation: BAE76912.1.

PIR

D65067.

RefSeq

AP_003406.1.
NP_417320.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X8M	X-ray	2.60	A/B/C/D/E/F	2-278	[»]
1XRU	X-ray	1.94	A/B	1-275	[»]

ModBase

Search...

Genome annotation databases

GeneID

947319.

GenomeReviews

Gene locus JW2811 in contig AP009048_GR.
Gene locus b2843 in contig U00096_GR.

KEGG

ecj:JW2811.
eco:b2843.

Organism-specific databases

EchoBASE

EB2899.

EcoGene

EG13096. kduI.

CMR

Search...

Phylogenomic databases

HOGENOM

Q46938.

OMA

Q46938. QAVISPP.

Enzyme and pathway databases

BioCyc

EcoCyc:G7463-MON.

BRENDA

5.3.1.17. 246.

Family and domain databases

HAMAP

MF_00687.
[Tree]

InterPro

IPR007045. KduI.
[Graphical view]

Pfam

PF04962. KduI. 1 hit.
[Graphical view]

PIRSF

PIRSF006625. KduI. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

KDUI_ECOLI

Accession

Primary (citable) accession number: Q46938
Secondary accession number(s): Q2M9Z4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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