2-dehydro-3-deoxyphosphooctonate aldolase (P0A715)

Identification
Name:2-dehydro-3-deoxyphosphooctonate aldolase
Synonyms:
  • 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase
  • KDO-8-phosphate synthase
  • KDO 8-P synthase
  • KDOPS
  • Phospho-2-dehydro-3-deoxyoctonate aldolase
Gene Name:kdsA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Arabinose 5-phosphate + 1.0Water + 1.0Phosphoenolpyruvic acid ↔ 1.03-Deoxy-D-manno-octulosonate 8-phosphate + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.03-Deoxy-D-manno-octulosonate 8-phosphate + 1.0Phosphate ↔ 1.0Phosphoenolpyruvic acid + 1.0D-Arabinose 5-phosphate + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.03-deoxy-D-manno-octulosonate 8-phosphate +1.0Thumb
1.0D-Arabinose 5-phosphate + 1.0Phosphoenolpyruvic acid + 1.0Water → 1.0Phosphate + 1.03-deoxy-D-manno-octulosonate 8-phosphate + 1.03-Deoxy-D-manno-octulosonate 8-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Arabinose 5-phosphate + 1.0Water + 1.0Phosphoenolpyruvic acid ↔ 1.03-Deoxy-D-manno-octulosonate 8-phosphate + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0D-Arabinose 5-phosphate + 1.0Water → 1.03-Deoxy-D-manno-octulosonate 8-phosphate + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200683-Deoxy-D-manno-octulosonate 8-phosphateMetaboCard
ECMDB11734D-Arabinose 5-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
3-deoxy-8-phosphooctulonate synthase activity
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
biosynthetic process
metabolic process
Gene Properties
Blattner:b1215
Gene OrientationClockwise
Centisome Percentage:27.32
Left Sequence End1267388
Right Sequence End1268242
Gene Sequence:
>855 bp
ATGACGCTATTTACAACCTTACTGGTGTTAATTTTCGAGCGCCTGTTTAAGTTGGGCGAG
CACTGGCAGCTTGATCATCGTCTTGAAGCGTTCTTTCGGCGGGTGAAACATTTTTCTCTC
GGGCGCACGTTAGGCATGACCATTATTGCGATGGGCGTGACTTTTTTACTGTTACGCGCA
TTGCAGGGAGTATTGTTCAACGTTCCCACGCTACTGGTGTGGCTGCTGATTGGTTTGCTG
TGTATTGGCGCAGGTAAAGTTCGTCTTCATTATCATGCTTATCTGACAGCTGCTTCACGT
AATGATAGCCATGCCCGTGCCACGATGGCTGGCGAACTCACCATGATTCACGGCGTCCCG
GCAGGCTGCGACGAACGTGAGTATTTGCGTGAGCTGCAAAATGCATTGCTGTGGATTAAC
TTTCGTTTTTATCTTGCACCGCTGTTCTGGCTGATTGTGGGGGGAACCTGGGGACCCGTT
ACGCTGATGGGGTATGCGTTTTTGCGTGCATGGCAATACTGGCTGGCGCGATATCAGACG
CCGCATCATCGTTTACAGTCCGGCATTGATGCCGTGCTTCATGTACTGGATTGGGTGCCG
GTTCGTCTTGCGGGTGTGGTATATGCCTTGATCGGTCATGGTGAGAAAGCGTTACCGGCC
TGGTTTGCTTCGCTGGGTGATTTCCATACTTCGCAGTATCAGGTGTTAACGCGTCTGGCG
CAGTTCTCTCTGGCGCGTGAACCGCATGTCGATAAGGTGGAGACGCCGAAGGCAGCGGTT
TCAATGGCGAAGAAAACCTCGTTCGTGGTCGTGGTGGTGATTGCACTACTGACGATTTAC
GGGGCGTTGGTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:284
Protein Molecular Weight:30833
Protein Theoretical pI:7
PDB File:1PL9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-dehydro-3-deoxyphosphooctonate aldolase
MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDK
ANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLAR
QTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVD
MLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEA
HPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK
References
External Links:
ResourceLink
Uniprot ID:P0A715
Uniprot Name:KDSA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238959
PDB ID:1PL9
Ecogene ID:EG10518
Ecocyc:EG10518
ColiBase:b1215
Kegg Gene:b1215
EchoBASE ID:EB0513
CCDB:KDSA_ECOLI
BacMap:16129178
General Reference:
  • Asojo, O., Friedman, J., Adir, N., Belakhov, V., Shoham, Y., Baasov, T. (2001). "Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor." Biochemistry 40:6326-6334. Pubmed: 11371194
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Dotson, G. D., Dua, R. K., Clemens, J. C., Wooten, E. W., Woodard, R. W. (1995). "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." J Biol Chem 270:13698-13705. Pubmed: 7775423
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • 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., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "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." DNA Res 3:137-155. Pubmed: 8905232
  • Strohmaier, H., Remler, P., Renner, W., Hogenauer, G. (1995). "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." J Bacteriol 177:4488-4500. Pubmed: 7543480
  • Wagner, T., Kretsinger, R. H., Bauerle, R., Tolbert, W. D. (2000). "3-Deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli. Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate." J Mol Biol 301:233-238. Pubmed: 10926505
  • Woisetschlager, M., Hogenauer, G. (1987). "The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichia coli." Mol Gen Genet 207:369-373. Pubmed: 3039295