Rhamnulose-1-phosphate aldolase (P32169)

Identification
Name:Rhamnulose-1-phosphate aldolase
Synonyms:Not Available
Gene Name:rhaD
Enzyme Class:
Biological Properties
General Function:Involved in metal ion binding
Specific Function:Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Fructose and mannose metabolism ec00051
  • Microbial metabolism in diverse environments ec01120
  • Pentose and glucuronate interconversions ec00040
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Rhamnulose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde + 1.0(S)-Lactaldehyde
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Rhamnulose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde
ReactionCard
SMPDB Reactions:
1.0L-rhamnulose 1-phosphate+1.0Thumb → 1.0Thumb+1.0(S)-lactaldehyde+1.0Thumb
1.0L-rhamnulose 1-phosphate + 1.0L-Rhamnulose 1-phosphate → 1.0Dihydroxyacetone phosphate + 1.0(S)-lactaldehyde + 1.0Lactaldehyde
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Rhamnulose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde + 1.0(S)-Lactaldehyde
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Rhamnulose 1-phosphate → 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB23841(S)-LactaldehydeMetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB02165GlycolaldehydeMetaboCard
ECMDB20166L-Rhamnulose 1-phosphateMetaboCard
ECMDB03052LactaldehydeMetaboCard
GO Classification:
Function
aldehyde-lyase activity
binding
carbon-carbon lyase activity
catalytic activity
cation binding
ion binding
lyase activity
metal ion binding
rhamnulose-1-phosphate aldolase activity
Gene Properties
Blattner:b3902
Gene OrientationCounterclockwise
Centisome Percentage:88.18
Left Sequence End4091471
Right Sequence End4092295
Gene Sequence:
>825 bp
GTGCCGTTTCGCAGCAATAATCCCATCACGCGCGACGAATTGCTGTCGCGCTTTTTCCCG
CAGTATCATCCCGTCACGACGTTTAATAGTGGGCTTAGTGGCGGGAGTTTTCTCATTGAA
CATCAGGGCCAGCGTTTTGTTGTGCGTCAGCCGCACGATCCTGATGCGCCGCAGTCCGCG
TTCTTGCGCCAGTATCGGGCTTTATCACAACTACCCGCATGCATTGCACCGAAGCCGCAT
TTATATCTCCGTGACTGGATGGTAGTCGACTATCTGCCCGGCGCGGTAAAAACGTATTTG
CCGGATACCAACGAACTGGCAGGCTTGCTGTATTATCTACATCAACAACCACGTTTTGGC
TGGCGAATAACGCTGTTGCCGTTACTGGAACTGTACTGGCAGCAAAGCGATCCGGCGCGG
CGGACAGTGGGTTGGCTGCGAATGTTAAAACGTCTGCGCAAAGCGCGGGAACCACGGCCT
TTACGCTTAAGTCCATTGCATATGGATGTCCACGCCGGAAATTTAGTGCATAGCGCGTCA
GGGTTAAAACTCATCGACTGGGAGTATGCCGGAGATGGTGATATCGCGCTGGAACTGGCG
GCGGTGTGGGTGGAAAATACTGAACAGCACCGGCAATTGGTCAATGACTATGCCACTCGC
GCGAAGATTTATCCGGCGCAATTATGGCGTCAGGTCAGGCGATGGTTTCCCTGGCTGCTG
ATGCTCAAAGCAGGGTGGTTTGAGTACCGCTGGCGACAAACCGGCGATCAACAATTTATC
AGGCTGGCCGATGACACCTGGCGGCAGCTATTAATAAAACAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:274
Protein Molecular Weight:30145
Protein Theoretical pI:6
PDB File:1GT7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Rhamnulose-1-phosphate aldolase
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL
References
External Links:
ResourceLink
Uniprot ID:P32169
Uniprot Name:RHAD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062670
PDB ID:1GT7
Ecogene ID:EG11866
Ecocyc:EG11866
ColiBase:b3902
Kegg Gene:b3902
EchoBASE ID:EB1812
CCDB:RHAD_ECOLI
BacMap:16131742
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
  • Egan, S. M., Schleif, R. F. (1993). "A regulatory cascade in the induction of rhaBAD." J Mol Biol 234:87-98. Pubmed: 8230210
  • 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
  • Holcroft, C. C., Egan, S. M. (2000). "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 182:3529-3535. Pubmed: 10852886
  • Kroemer, M., Merkel, I., Schulz, G. E. (2003). "Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase." Biochemistry 42:10560-10568. Pubmed: 12962479
  • Kroemer, M., Schulz, G. E. (2002). "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 58:824-832. Pubmed: 11976494
  • Moralejo, P., Egan, S. M., Hidalgo, E., Aguilar, J. (1993). "Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli." J Bacteriol 175:5585-5594. Pubmed: 8396120
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018