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P0A715 (KDSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
2-dehydro-3-deoxyphosphooctonate aldolase

EC=2.5.1.55
Alternative name(s):
3-deoxy-D-manno-octulosonic acid 8-phosphate synthase
KDO-8-phosphate synthase
Short name=KDO 8-P synthase
Short name=KDOPS
Phospho-2-dehydro-3-deoxyoctonate aldolase
Gene names
Name:kdsA
Ordered Locus Names:b1215, JW1206
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. HAMAP-Rule MF_00056

Catalytic activity

Phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate. HAMAP-Rule MF_00056

Pathway

Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate: step 2/3. HAMAP-Rule MF_00056

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP-Rule MF_00056

Subunit structure

Homotrimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00056.

Sequence similarities

Belongs to the KdsA family.

Mass spectrometry

Molecular mass is 30842±17 Da from positions 1 - 284. Determined by ESI. Ref.9

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processketo-3-deoxy-D-manno-octulosonic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_function3-deoxy-8-phosphooctulonate synthase activity

Inferred from direct assay PubMed 8223657. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2842842-dehydro-3-deoxyphosphooctonate aldolase HAMAP-Rule MF_00056
PRO_0000187124

Experimental info

Sequence conflict221F → L in CAA29067. Ref.1

Secondary structure

............................................................... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A715 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 35E79D692D134535

FASTA28430,833
        10         20         30         40         50         60 
MKQKVVSIGD INVANDLPFV LFGGMNVLES RDLAMRICEH YVTVTQKLGI PYVFKASFDK 

        70         80         90        100        110        120 
ANRSSIHSYR GPGLEEGMKI FQELKQTFGV KIITDVHEPS QAQPVADVVD VIQLPAFLAR 

       130        140        150        160        170        180 
QTDLVEAMAK TGAVINVKKP QFVSPGQMGN IVDKFKEGGN EKVILCDRGA NFGYDNLVVD 

       190        200        210        220        230        240 
MLGFSIMKKV SGNSPVIFDV THALQCRDPF GAASGGRRAQ VAELARAGMA VGLAGLFIEA 

       250        260        270        280 
HPDPEHAKCD GPSALPLAKL EPFLKQMKAI DDLVKGFEEL DTSK 

« Hide

References

« Hide 'large scale' references
[1]"The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichia coli."
Woisetschlaeger M., Hoegenauer G.
Mol. Gen. Genet. 207:369-373(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
Strohmaier H., Remler P., Renner W., Hoegenauer G.
J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[7]"Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR."
Dotson G.D., Dua R.K., Clemens J.C., Wooten E.W., Woodard R.W.
J. Biol. Chem. 270:13698-13705(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-10.
[8]"3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli. Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate."
Wagner T., Kretsinger R.H., Bauerle R., Tolbert W.D.
J. Mol. Biol. 301:233-238(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]"Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor."
Asojo O., Friedman J., Adir N., Belakhov V., Shoham Y., Baasov T.
Biochemistry 40:6326-6334(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05552 Genomic DNA. Translation: CAA29067.1.
U18555 Genomic DNA. Translation: AAC43441.1.
U00096 Genomic DNA. Translation: AAC74299.1.
AP009048 Genomic DNA. Translation: BAA36073.1.
PIRSYECOL. I83573.
RefSeqNP_415733.1. NC_000913.3.
YP_489482.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9EX-ray2.40A/B/C/D1-284[»]
1G7UX-ray2.80A1-284[»]
1G7VX-ray2.40A1-284[»]
1GG0X-ray3.00A1-284[»]
1PHQX-ray2.70A1-284[»]
1PHWX-ray2.36A1-284[»]
1PL9X-ray2.90A1-284[»]
1Q3NX-ray2.70A1-284[»]
1X6UX-ray2.70A1-284[»]
1X8FX-ray2.40A1-284[»]
ProteinModelPortalP0A715.
SMRP0A715. Positions 1-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35940N.
IntActP0A715. 46 interactions.
MINTMINT-1220797.
STRING511145.b1215.

2D gel databases

SWISS-2DPAGEP0A715.

Proteomic databases

PaxDbP0A715.
PRIDEP0A715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74299; AAC74299; b1215.
BAA36073; BAA36073; BAA36073.
GeneID12931123.
945785.
KEGGecj:Y75_p1187.
eco:b1215.
PATRIC32117682. VBIEscCol129921_1263.

Organism-specific databases

EchoBASEEB0513.
EcoGeneEG10518. kdsA.

Phylogenomic databases

eggNOGCOG2877.
HOGENOMHOG000023021.
KOK01627.
OMAANDKPMV.
OrthoDBEOG680X4R.
PhylomeDBP0A715.

Enzyme and pathway databases

BioCycEcoCyc:KDO-8PSYNTH-MONOMER.
ECOL316407:JW1206-MONOMER.
MetaCyc:KDO-8PSYNTH-MONOMER.
SABIO-RKP0A715.
UniPathwayUPA00030.
UPA00357; UER00474.

Gene expression databases

GenevestigatorP0A715.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00056. KDO8P_synth.
InterProIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006269. KDO8P_synthase.
[Graphical view]
PANTHERPTHR21057:SF2. PTHR21057:SF2. 1 hit.
PfamPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01362. KDO8P_synth. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A715.
PROP0A715.

Entry information

Entry nameKDSA_ECOLI
AccessionPrimary (citable) accession number: P0A715
Secondary accession number(s): P17579
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 88 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene