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O66496 (KDSA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:aq_085
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Oligomer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the KdsA family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-deoxy-8-phosphooctulonate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2672672-dehydro-3-deoxyphosphooctonate aldolase HAMAP-Rule MF_00056
PRO_0000187099

Secondary structure

................................................... 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66496 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0A3CFEA3337F1964

FASTA26729,734
        10         20         30         40         50         60 
MEKFLVIAGP CAIESEELLL KVGEEIKRLS EKFKEVEFVF KSSFDKANRS SIHSFRGHGL 

        70         80         90        100        110        120 
EYGVKALRKV KEEFGLKITT DIHESWQAEP VAEVADIIQI PAFLCRQTDL LLAAAKTGRA 

       130        140        150        160        170        180 
VNVKKGQFLA PWDTKNVVEK LKFGGAKEIY LTERGTTFGY NNLVVDFRSL PIMKQWAKVI 

       190        200        210        220        230        240 
YDATHSVQLP GGLGDKSGGM REFIFPLIRA AVAVGCDGVF METHPEPEKA LSDASTQLPL 

       250        260 
SQLEGIIEAI LEIREVASKY YETIPVK 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Functional and biochemical characterization of a recombinant 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic bacterium Aquifex aeolicus."
Duewel H.S., Sheflyan G.Y., Woodard R.W.
Biochem. Biophys. Res. Commun. 263:346-351(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Function of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate 8-phosphate synthase."
Wang J., Duewel H.S., Stuckey J.A., Woodard R.W., Gatti D.L.
J. Mol. Biol. 324:205-214(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06457.1.
PIRE70308.
RefSeqNP_213056.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FWNX-ray1.94A/B1-267[»]
1FWSX-ray1.90A/B1-267[»]
1FWTX-ray1.90A/B1-267[»]
1FWWX-ray1.85A/B1-267[»]
1FX6X-ray2.06A/B1-267[»]
1FXPX-ray1.80A/B1-267[»]
1FXQX-ray1.80A/B1-267[»]
1FY6X-ray1.89A/B1-267[»]
1JCXX-ray1.80A/B1-267[»]
1JCYX-ray1.90A/B1-267[»]
1LRNX-ray2.10A/B1-267[»]
1LROX-ray1.80A/B1-267[»]
1LRQX-ray1.80A/B1-267[»]
1PCKX-ray1.80A/B1-267[»]
1PCWX-ray1.85A/B1-267[»]
1PE1X-ray1.74A/B1-267[»]
1T8XX-ray1.80A/B1-267[»]
1T96X-ray1.85A/B1-267[»]
1T99X-ray1.85A/B1-267[»]
1ZHAX-ray1.74A/B1-267[»]
1ZJIX-ray2.25A/B1-267[»]
2A21X-ray1.80A/B1-267[»]
2A2IX-ray1.95A/B1-267[»]
2EF9X-ray2.00A/B1-267[»]
2NWRX-ray1.50A/B1-267[»]
2NWSX-ray1.80A/B1-267[»]
2NX1X-ray1.80A/B1-267[»]
2NX3X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-267[»]
2NXGX-ray1.95A/B2-264[»]
2NXHX-ray2.11A/B/C/D/E/F/G/H/I/J/K/L2-264[»]
2NXIX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L2-264[»]
3E0IX-ray1.70A/B1-267[»]
3E12X-ray1.70A/B1-267[»]
ProteinModelPortalO66496.
SMRO66496. Positions 2-264.
ModBaseSearch...

Protein-protein interaction databases

STRING224324.aq_085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06457; AAC06457; aq_085.
GeneID1192509.
KEGGaae:aq_085.
PATRIC20957869. VBIAquAeo85532_0075.

Phylogenomic databases

eggNOGCOG2877.
HOGENOMHOG000023021.
KOK01627.
OMAYHEDESI.
ProtClustDBPRK05198.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-71-MONOMER.
BRENDA2.5.1.55. 396.
UniPathwayUPA00030.
UPA00357; UER00474.

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

EvolutionaryTraceO66496.

Entry information

Entry nameKDSA_AQUAE
AccessionPrimary (citable) accession number: O66496
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 96 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