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P67653 (KDSC_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-deoxy-D-manno-octulosonate 8-phosphate phosphatas KdsC
EC=3.1.3.45
Alternative name(s):
KDO 8-P phosphatase
Gene names
Name:kdsC
Ordered Locus Names:c3958
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of lipopolysaccharides (LPSs) By similarity. Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. Ref.2

Catalytic activity

3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate.

Cofactor

Magnesium. Ref.2

Pathway

Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 3/3.

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

Belongs to the kdsC family.

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-deoxy-manno-octulosonate-8-phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1881883-deoxy-D-manno-octulosonate 8-phosphate phosphatas KdsC
PRO_0000201698

Regions

Region32 – 343Substrate binding
Region55 – 595Substrate binding
Region76 – 772Substrate binding

Sites

Metal binding321Magnesium
Metal binding341Magnesium; via carbonyl oxygen
Metal binding1251Magnesium
Binding site341Substrate
Binding site631Substrate
Binding site781Substrate
Binding site861Substrate
Binding site1021Substrate
Binding site1871Substrate; via carbonyl oxygen

Secondary structure

1 .................................. 188
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67653 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6A40ED8C20B1E3A7

FASTA18820,015
        10         20         30         40         50         60 
MSKAGASLAT CYGPVSADVM AKAENIRLLI LDVDGVLSDG LIYMGNNGEE LKAFNVRDGY 

        70         80         90        100        110        120 
GIRCALTSDI EVAIITGRKA KLVEDRCATL GITHLYQGQS NKLIAFSDLL EKLAIAPENV 

       130        140        150        160        170        180 
AYVGDDLIDW PVMEKVGLSV AVADAHPLLI PRADYVTRIA GGRGAVREVC DLLLLAQGKL 


DEAKGQSI

« Hide

References

« Hide 'large scale' references
[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.
[2]"The tail of KdsC: conformational changes control the activity of a haloacid dehalogenase superfamily phosphatase."
Biswas T., Yi L., Aggarwal P., Wu J., Rubin J.R., Stuckey J.A., Woodard R.W., Tsodikov O.V.
J. Biol. Chem. 284:30594-30603(2009) [PubMed: 19726684] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND DIVALENT METALS, FUNCTION AS A KDO 8-P PHOSPHATASE, REACTION MECHANISM, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014075 Genomic DNA. Translation: AAN82398.1.
RefSeqNP_755824.1. NC_004431.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R8EX-ray1.40A/B/C/D/E/F/G/H1-188[»]
2R8XX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8YX-ray1.85A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
2R8ZX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-188[»]
3HYCX-ray3.06A/B/C/D/E/F/G/H1-188[»]
3I6BX-ray2.49A/B/C/D1-180[»]
ProteinModelPortalP67653.
SMRP67653. Positions 8-188.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000043950; EBESCP00000042299; EBESCG00000043000.
GeneID1040319.
GenomeReviewsGene locus c3958 in contig AE014075_GR.
KEGGecc:c3958.
PATRIC18285690. VBIEscCol75197_3725.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009685.
HOGENOMHBG471796.
OMAKTFNTLD.
ProtClustDBPRK09484.

Family and domain databases

InterProIPR023214. HAD-like_dom.
IPR013200. HAD-SF_hydro-like_3.
IPR010023. KDO_8-P_phosphatase.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KOK03270.
PANTHERPTHR26053. PTHR26053. 1 hit.
PfamPF08282. Hydrolase_3. 1 hit.
[Graphical view]
PIRSFPIRSF006118. KDO8-P_Ptase. 1 hit.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01670. YrbI-phosphatas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKDSC_ECOL6
AccessionPrimary (citable) accession number: P67653
Secondary accession number(s): Q83JF3, Q8FD72
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 49 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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