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
- Functionsdeoxyribose-phosphate aldolase activity / lyase activityProcessescarbohydrate catabolic process / cellular response to DNA damage stimulus / deoxyribonucleotide catabolic process / deoxyribose phosphate catabolic process / nucleobase-containing small molecule interconversionComponentscytosol / 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
- DeoC (PF01791)
- 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
Resource Link UniProtKB ID P0A6L0 UniProtKB Entry Name DEOC_ECOLI GenBank Protein ID 41252 GenBank Gene ID X03224 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]