Identification
Name:Deoxyribose-phosphate aldolase
Synonyms:
  • Phosphodeoxyriboaldolase
  • DERA
  • Deoxyriboaldolase
Gene Name:deoC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:2-deoxy-D-ribose 5-phosphate = D- glyceraldehyde 3-phosphate + acetaldehyde
Cellular Location:Cytoplasm
SMPDB Pathways:
  • purine deoxyribonucleosides degradation PW002077
KEGG Pathways:
KEGG Reactions:
1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Deoxyribose 5-phosphate1.0Thumb+1.0Thumb
1.0Deoxyribose 5-phosphate → 1.0Acetaldehyde + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00990AcetaldehydeMetaboCard
ECMDB01112D-Glyceraldehyde 3-phosphateMetaboCard
ECMDB01031Deoxyribose 5-phosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
aldehyde-lyase activity
carbon-carbon lyase activity
catalytic activity
deoxyribose-phosphate aldolase activity
lyase activity
Process
cellular nitrogen compound metabolic process
deoxyribonucleotide catabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide catabolic process
nucleotide metabolic process
Gene Properties
Blattner:b4381
Gene OrientationClockwise
Centisome Percentage:99.48
Left Sequence End4615346
Right Sequence End4616125
Gene Sequence:
>780 bp
ATGAACTCGCATAATATTACTAACGAATCATTAGCACTGGCATTAATGCTGGTGGTGGTG
GCAATCTTAATTAGCCATAAAGAAAAACTGGCGCTGGAGAAAGATATTCTCTGGAGCGTC
GGGCGAGCGATAATTCAGCTGATTATTGTCGGCTATGTGCTGAAGTATATTTTCAGCGTG
GATGATGCCAGCCTGACATTATTGATGGTGTTATTTATCTGCTTTAATGCGGCGTGGAAC
GCGCAAAAACGCAGTAAATATATTGCTAAAGCTTTTATCTCATCGTTTATTGCCATTACG
GTCGGGGCGGGAATTACCCTGGCGGTGCTGATTCTCTCAGGGTCGATTGAATTTATCCCG
ATGCAGGTGATCCCTATCGCCGGGATGATTGCCGGTAACGCCATGGTAGCGGTGGGGTTG
TGTTACAACAATTTAGGGCAACGGGTCATTAGCGAACAGCAACAGATTCAGGAGAAACTG
AGTCTTGGTGCGACGCCGAAGCAGGCTTCAGCGATATTGATTCGCGACAGTATTCGCGCG
GCTTTAATTCCGACGGTCGATTCAGCAAAAACGGTTGGCTTAGTGAGTTTACCAGGAATG
ATGTCCGGGCTGATATTTGCCGGGATTGATCCGGTGAAGGCGATTAAATATCAGATTATG
GTGACCTTTATGCTGCTCTCAACCGCCAGCTTGTCGACCATTATTGCCTGCTATTTAACC
TATCGTAAGTTTTATAATTCGCGCCACCAGTTGGTGGTGACGCAATTGAAGAAGAAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:259
Protein Molecular Weight:27733
Protein Theoretical pI:5
PDB File:1P1X
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Deoxyribose-phosphate aldolase
MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTL
KEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFD
LVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPE
SARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSL
LASLLKALGHGDGKSASSY
References
External Links:
ResourceLink
Uniprot ID:P0A6L0
Uniprot Name:DEOC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674630
PDB ID:1P1X
Ecogene ID:EG10221
Ecocyc:EG10221
ColiBase:b4381
Kegg Gene:b4381
EchoBASE ID:EB0217
CCDB:DEOC_ECOLI
BacMap:16132198
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Heine, A., DeSantis, G., Luz, J. G., Mitchell, M., Wong, C. H., Wilson, I. A. (2001). "Observation of covalent intermediates in an enzyme mechanism at atomic resolution." Science 294:369-374. Pubmed: 11598300
  • Valentin-Hansen, P., Boetius, F., Hammer-Jespersen, K., Svendsen, I. (1982). "The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme." Eur J Biochem 125:561-566. Pubmed: 6749498
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842