Rhamnulose-1-phosphate aldolase
Details
- Name
- Rhamnulose-1-phosphate aldolase
- Kind
- protein
- Synonyms
- 4.1.2.19
- rhuA
- Gene Name
- rhaD
- UniProtKB Entry
- P32169Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016592|Rhamnulose-1-phosphate aldolase MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK VYSMGGMKQTISREELIALGKRFGVTPLASALAL
- Number of residues
- 274
- Molecular Weight
- 30145.295
- Theoretical pI
- 5.79
- GO Classification
- Functionsidentical protein binding / metal ion binding / rhamnulose-1-phosphate aldolase activityProcessesrhamnose catabolic processComponentscytoplasm
- General Function
- Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde (PubMed:12962479). Also catalyzes the dephosphorylation of phospho-serine in vitro (PubMed:25848029).
- Specific Function
- aldehyde-lyase activity
- Pfam Domain Function
- Aldolase_II (PF00596)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016593|Rhamnulose-1-phosphate aldolase (rhaD) ATGCAAAACATTACTCAGTCCTGGTTTGTCCAGGGAATGATCAAAGCCACCACCGACGCC TGGCTGAAAGGCTGGGATGAGCGCAACGGCGGCAACCTGACGCTACGCCTGGATGACGCC GATATCGCACCATATCACGACAATTTCCACCAACAACCGCGCTATATCCCGCTCAGCCAG CCCATGCCTTTACTGGCAAATACACCGTTTATTGTCACCGGCTCGGGCAAATTCTTCCGT AACGTCCAGCTTGATCCTGCGGCTAACTTAGGCATCGTAAAAGTCGACAGCGACGGCGCG GGCTACCACATTCTTTGGGGGTTAACCAACGAAGCCGTCCCCACTTCCGAACTTCCGGCT CACTTCCTTTCCCACTGCGAGCGCATTAAAGCCACCAACGGCAAAGATCGGGTGATCATG CACTGCCACGCCACCAACCTGATCGCCCTCACCTATGTACTTGAAAACGACACCGCGGTC TTCACTCGCCAACTGTGGGAAGGCAGCACCGAGTGTCTGGTGGTATTCCCGGATGGCGTT GGCATTTTGCCGTGGATGGTGCCCGGCACGGACGAAATCGGCCAGGCGACCGCACAAGAG ATGCAAAAACATTCGCTGGTGTTGTGGCCCTTCCACGGCGTCTTCGGCAGCGGACCGACG CTGGATGAAACCTTCGGTTTAATCGACACCGCAGAAAAATCAGCACAAGTATTAGTGAAG GTTTATTCGATGGGCGGCATGAAACAGACCATCAGCCGTGAAGAGTTGATAGCGCTCGGC AAGCGTTTCGGCGTTACGCCACTCGCCAGTGCGCTGGCGCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P32169 UniProtKB Entry Name RHAD_ECOLI GenBank Protein ID 396681 GenBank Gene ID X60472 PDB ID(s) 1GT7, 1OJR, 2UYU, 2UYV, 2V29, 2V2A, 2V2B, 2V9E, 2V9F, 2V9G, 2V9I, 2V9L, 2V9M, 2V9N, 2V9O KEGG ID ecj:JW3873 NCBI Gene ID 948401 - General References
- Moralejo P, Egan SM, Hidalgo E, Aguilar J: Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli. J Bacteriol. 1993 Sep;175(17):5585-94. [Article]
- Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [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]
- Egan SM, Schleif RF: A regulatory cascade in the induction of rhaBAD. J Mol Biol. 1993 Nov 5;234(1):87-98. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Holcroft CC, Egan SM: Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon. J Bacteriol. 2000 Jun;182(12):3529-35. [Article]
- Kroemer M, Schulz GE: The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):824-32. Epub 2002 Apr 26. [Article]
- Kroemer M, Merkel I, Schulz GE: Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2003 Sep 16;42(36):10560-8. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Phosphoglycolohydroxamic Acid experimental unknown target Details