2-keto-3-deoxy-L-rhamnonate aldolase (P76469)

Identification
Name:2-keto-3-deoxy-L-rhamnonate aldolase
Synonyms:
  • KDR aldolase
  • 2-dehydro-3-deoxyrhamnonate aldolase
  • 2-keto-3-deoxy acid sugar aldolase
Gene Name:rhmA
Enzyme Class:
Biological Properties
General Function:Involved in carbon-carbon lyase activity
Specific Function:Catalyzes the reversible retro-aldol cleavage of 2-keto- 3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde. 2-keto-3- deoxy-L-mannonate, 2-keto-3-deoxy-L-lyxonate and 4-hydroxy-2- ketoheptane-1,7-dioate (HKHD) are also reasonably good substrates, although 2-keto-3-deoxy-L-rhamnonate is likely to be the physiological substrate
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
  • Fructose and mannose metabolism ec00051
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-L-rhamnonate ↔ 1.0Lactaldehyde + 1.0Pyruvic acid + 1.0(S)-Lactaldehyde
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Dehydro-3-deoxy-L-rhamnonate → 1.0Pyruvic acid + 1.0D-Lactaldehyde
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB23841(S)-LactaldehydeMetaboCard
ECMDB216442-Dehydro-3-deoxy-L-rhamnonateMetaboCard
ECMDB06458D-LactaldehydeMetaboCard
ECMDB03052LactaldehydeMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
catalytic activity
lyase activity
Process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b2245
Gene OrientationCounterclockwise
Centisome Percentage:50.78
Left Sequence End2356064
Right Sequence End2356867
Gene Sequence:
>804 bp
ATGGCTATCCCTGCATTTGGTTTAGGTACTTTCCGTCTGAAAGACGACGTTGTTATTTCA
TCTGTGATAACGGCGCTTGAACTTGGTTATCGCGCAATTGATACCGCACAAATCTATGAT
AACGAAGCCGCAGTAGGTCAGGCGATTGCAGAAAGTGGCGTGCCACGTCATGAACTCTAC
ATCACCACTAAAATCTGGATTGAAAATCTCAGCAAAGACAAATTGATCCCAAGTCTGAAA
GAGAGCCTGCAAAAATTGCGTACCGATTATGTTGATCTGACGCTAATCCACTGGCCGTCA
CCAAACGATGAAGTCTCTGTTGAAGAGTTTATGCAGGCGCTGCTGGAAGCCAAAAAACAA
GGGCTGACGCGTGAGATCGGTATTTCCAACTTCACGATCCCGTTGATGGAAAAAGCGATT
GCTGCTGTTGGTGCTGAAAACATCGCTACTAACCAGATTGAACTCTCTCCTTATCTGCAA
AACCGTAAAGTGGTTGCCTGGGCTAAACAGCACGGCATCCATATTACTTCCTATATGACG
CTGGCGTATGGTAAGGCCCTGAAAGATGAGGTTATTGCTCGTATCGCAGCTAAACACAAT
GCGACTCCGGCACAAGTGATTCTGGCGTGGGCTATGGGGGAAGGTTACTCAGTAATTCCT
TCTTCTACTAAACGTAAAAACCTGGAAAGTAATCTTAAGGCACAAAATTTACAGCTTGAT
GCCGAAGATAAAAAAGCGATCGCCGCACTGGATTGCAACGACCGCCTGGTTAGCCCGGAA
GGTCTGGCTCCTGAATGGGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:267
Protein Molecular Weight:28916
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-keto-3-deoxy-L-rhamnonate aldolase
MNALLSNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQ
LQAVAPYASQPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTAEQARQVVSATRYPPYGER
GVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADL
SASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDT
MLYSDALDQRLAMFKSGKNGPRIKGSY
References
External Links:
ResourceLink
Uniprot ID:P76469
Uniprot Name:RHMA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674382
Ecogene ID:EG14083
Ecocyc:EG14083
ColiBase:b2245
Kegg Gene:b2245
EchoBASE ID:EB3836
CCDB:RHMA_ECOLI
BacMap:16130180
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
  • 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
  • Rakus, J. F., Fedorov, A. A., Fedorov, E. V., Glasner, M. E., Hubbard, B. K., Delli, J. D., Babbitt, P. C., Almo, S. C., Gerlt, J. A. (2008). "Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase." Biochemistry 47:9944-9954. Pubmed: 18754693
  • Rea, D., Hovington, R., Rakus, J. F., Gerlt, J. A., Fulop, V., Bugg, T. D., Roper, D. I. (2008). "Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12." Biochemistry 47:9955-9965. Pubmed: 18754683
  • Wright, A., Blewett, A., Fulop, V., Cooper, R., Burrows, S., Jones, C., Roper, D. (2002). "Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12." Acta Crystallogr D Biol Crystallogr 58:2191-2193. Pubmed: 12454498
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837