Deoxyribose-phosphate aldolase

Details

Name
Deoxyribose-phosphate aldolase
Synonyms
  • 2-deoxy-D-ribose 5-phosphate aldolase
  • 4.1.2.4
  • Deoxyriboaldolase
  • DERA
  • dra
  • Phosphodeoxyriboaldolase
  • thyR
Gene Name
deoC
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019179|Deoxyribose-phosphate aldolase
MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTL
KEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFD
LVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPE
SARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSL
LASLLKALGHGDGKSASSY
Number of residues
259
Molecular Weight
27733.44
Theoretical pI
5.43
GO Classification
Functions
deoxyribose-phosphate aldolase activity / lyase activity
Processes
carbohydrate catabolic process / cellular response to DNA damage stimulus / deoxyribonucleotide catabolic process / deoxyribose phosphate catabolic process / nucleobase-containing small molecule interconversion
Components
cytosol / membrane
General Function
Lyase activity
Specific Function
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019180|Deoxyribose-phosphate aldolase (deoC)
ATGACTGATCTGAAAGCAAGCAGCCTGCGTGCACTGAAATTGATGGACCTGACCACCCTG
AATGACGACGACACCGACGAGAAAGTGATCGCCCTGTGTCATCAGGCCAAAACTCCGGTC
GGCAATACCGCCGCTATCTGTATCTATCCTCGCTTTATCCCGATTGCTCGCAAAACTCTG
AAAGAGCAGGGCACCCCGGAAATCCGTATCGCTACGGTAACCAACTTCCCACACGGTAAC
GACGACATCGACATCGCGCTGGCAGAAACCCGTGCGGCAATCGCCTACGGTGCTGATGAA
GTTGACGTTGTGTTCCCGTACCGCGCGCTGATGGCGGGTAACGAGCAGGTTGGTTTTGAC
CTGGTGAAAGCCTGTAAAGAGGCTTGCGCGGCAGCGAATGTACTGCTGAAAGTGATCATC
GAAACCGGCGAACTGAAAGACGAAGCGCTGATCCGTAAAGCGTCTGAAATCTCCATCAAA
GCGGGTGCGGACTTCATCAAAACCTCTACCGGTAAAGTGGCTGTGAACGCGACGCCGGAA
AGCGCGCGCATCATGATGGAAGTGATCCGTGATATGGGCGTAGAAAAAACCGTTGGTTTC
AAACCGGCGGGCGGCGTGCGTACTGCGGAAGATGCGCAGAAATATCTCGCCATTGCAGAT
GAACTGTTCGGTGCTGACTGGGCAGATGCGCGTCACTACCGCTTTGGCGCTTCCAGCCTG
CTGGCAAGCCTGCTGAAAGCGCTGGGTCACGGCGACGGTAAGAGCGCCAGCAGCTACTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6L0
UniProtKB Entry NameDEOC_ECOLI
GenBank Protein ID41252
GenBank Gene IDX03224
General References
  1. Valentin-Hansen P, Boetius F, Hammer-Jespersen K, Svendsen I: 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. 1982 Jul;125(3):561-6. [Article]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  6. Heine A, DeSantis G, Luz JG, Mitchell M, Wong CH, Wilson IA: Observation of covalent intermediates in an enzyme mechanism at atomic resolution. Science. 2001 Oct 12;294(5541):369-74. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04087Open Form of 2'-Deoxy-Ribofuranose-5'-PhosphateexperimentalunknownDetails