Deoxyribose-phosphate aldolase
Details
- Name
- Deoxyribose-phosphate aldolase
- Synonyms
- 2-deoxy-D-ribose 5-phosphate aldolase
- 4.1.2.4
- Deoxyriboaldolase
- DERA
- Phosphodeoxyriboaldolase
- Gene Name
- deoC
- Organism
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- Amino acid sequence
>lcl|BSEQ0017487|Deoxyribose-phosphate aldolase MDLAAHIDHTLLKPTATLEEVAKAAEEALEYGFYGLCIPPSYVAWVRARYPHAPFRLVTV VGFPLGYQEKEVKALEAALACARGADEVDMVLHLGRAKAGDLDYLEAEVRAVREAVPQAV LKVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRGASLEDVALLVRVAQGRAQVK AAGGIRDRETALRMLKAGASRLGTSSGVALVAGEGGTLGY
- Number of residues
- 220
- Molecular Weight
- 23306.525
- Theoretical pI
- Not Available
- GO Classification
- Functionsdeoxyribose-phosphate aldolase activityProcessescarbohydrate catabolic process / deoxyribonucleotide catabolic process / deoxyribose phosphate catabolic processComponentscytoplasm
- General Function
- Deoxyribose-phosphate aldolase 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|BSEQ0017488|Deoxyribose-phosphate aldolase (deoC) ATGGACCTGGCCGCCCACATTGACCACACCCTCCTCAAGCCCACCGCCACCCTCGAGGAG GTGGCGAAGGCAGCGGAGGAGGCGCTGGAGTACGGCTTCTATGGCCTCTGCATCCCCCCT TCCTACGTGGCCTGGGTCAGGGCCCGCTACCCCCACGCGCCCTTCCGTCTGGTCACGGTG GTGGGCTTTCCCCTGGGCTACCAGGAGAAGGAGGTGAAGGCCCTGGAGGCGGCCCTCGCC TGCGCCCGGGGGGCGGACGAGGTGGACATGGTCCTCCACCTGGGCCGGGCCAAGGCGGGG GACCTGGACTACCTGGAGGCCGAGGTGCGGGCCGTGCGGGAGGCCGTTCCCCAAGCGGTG CTCAAGGTGATCCTGGAAACGGGGTACTTCTCCCCGGAGGAGATCGCCCGCCTGGCCGAG GCGGCCATCCGGGGCGGGGCGGACTTCCTCAAGACCTCCACGGGCTTCGGCCCCCGGGGG GCGAGCCTCGAGGACGTGGCGCTTTTGGTCCGGGTGGCCCAGGGGCGGGCCCAGGTGAAG GCCGCAGGGGGCATCCGGGACCGGGAGACCGCCCTGAGGATGCTGAAGGCCGGGGCGAGC CGCCTCGGGACCTCCAGCGGCGTGGCCCTGGTGGCGGGGGAAGGGGGGACCCTTGGCTAC TAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q5SJ28 UniProtKB Entry Name DEOC_THET8 - General References
- Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N: Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1816-23. Epub 2004 Sep 23. [Article]