N-acetylneuraminate lyase (P0A6L4)

Identification
Name:N-acetylneuraminate lyase
Synonyms:
  • N-acetylneuraminate pyruvate-lyase
  • N-acetylneuraminic acid aldolase
  • NALase
  • Sialate lyase
  • Sialic acid aldolase
  • Sialic acid lyase
Gene Name:nanA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate
Cellular Location:Cytoplasm
SMPDB Pathways:
  • N-acetylneuraminate and N-acetylmannosamine and N-acetylglucosamine degradation PW002030
KEGG Pathways:
  • Amino sugar and nucleotide sugar metabolism ec00520
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylneuraminic acid + 1.0N-acetylneuraminate ↔ 1.0N-Acetylmannosamine + 1.0Pyruvic acid
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylneuraminic acid ↔ 1.0N-Acetylmannosamine + 1.0Pyruvic acid
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0N-Acetylmannosamine
1.0N-Acetylneuraminic acid → 1.0Pyruvic acid + 1.0N-Acetylmannosamine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylneuraminic acid + 1.0N-acetylneuraminate ↔ 1.0N-Acetylmannosamine + 1.0Pyruvic acid
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-acetylneuraminate → 1.0N-Acetylmannosamine + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01129N-AcetylmannosamineMetaboCard
ECMDB23218N-acetylneuraminateMetaboCard
ECMDB00830N-Acetylneuraminic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
carbon-carbon lyase activity
catalytic activity
lyase activity
N-acetylneuraminate lyase activity
oxo-acid-lyase activity
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3225
Gene OrientationCounterclockwise
Centisome Percentage:72.65
Left Sequence End3370705
Right Sequence End3371598
Gene Sequence:
>894 bp
ATGAAAACACTGGTTGTGGCTCTTGGGGGCAACGCCTTACTCCAGCGCGGTGAGGCGCTG
ACGGCAGAAAATCAATATCGCAATATCGCCAGTGCTGTACCCGCGCTGGCACGCCTGGCC
CGTTCTTATCGGTTGGCGATTGTTCACGGCAACGGGCCGCAGGTGGGGCTGCTGGCATTG
CAGAATCTGGCGTGGAAAGAGGTAGAACCGTATCCGCTGGATGTGCTGGTTGCGGAAAGC
CAGGGGATGATTGGCTATATGCTGGCGCAGAGTTTGAGCGCACAGCCGCAGATGCCGCCC
GTGACGACGGTGCTGACGCGCATTGAGGTTTCGCCTGATGATCCGGCGTTTTTGCAGCCA
GAGAAATTTATTGGTCCGGTTTATCAGCCAGAAGAACAAGAGGCACTGGAAGCGGCTTAC
GGCTGGCAGATGAAACGTGATGGTAAATATTTGCGCCGGGTGGTGGCGTCTCCGCAACCG
CGTAAAATTCTCGACAGCGAAGCCATCGAGTTGTTGCTCAAAGAGGGGCATGTGGTGATT
TGCAGTGGCGGCGGCGGTGTGCCTGTGACGGATGACGGAGCAGGGAGTGAAGCAGTGATT
GATAAAGATCTCGCCGCTGCGTTGCTCGCCGAGCAGATTAATGCAGATGGACTGGTGATC
CTCACCGATGCTGATGCGGTATATGAAAACTGGGGAACGCCGCAGCAACGTGCCATTCGC
CATGCCACACCGGATGAGTTAGCGCCATTTGCCAAAGCCGATGGTTCGATGGGGCCGAAT
GTAACGGCGGTGAGTGGTTATGTCAGAAGCCGTGGTAAACCCGCGTGGATTGGGGCGTTA
TCGCGAATTGAAGAGACGCTGGCGGGCGAAGCGGGGACCTGTATTTCGCTGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:297
Protein Molecular Weight:32593
Protein Theoretical pI:6
PDB File:1HL2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>N-acetylneuraminate lyase
MATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSERE
QVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCD
HYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRRE
HPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECN
KVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG
References
External Links:
ResourceLink
Uniprot ID:P0A6L4
Uniprot Name:NANA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674658
PDB ID:1HL2
Ecogene ID:EG10637
Ecocyc:EG10637
ColiBase:b3225
Kegg Gene:b3225
EchoBASE ID:EB0631
CCDB:NANA_ECOLI
BacMap:16131115
General Reference:
  • Aisaka, K., Igarashi, A., Yamaguchi, K., Uwajima, T. (1991). "Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli." Biochem J 276 ( Pt 2):541-546. Pubmed: 1646603
  • 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
  • Izard, T., Lawrence, M. C., Malby, R. L., Lilley, G. G., Colman, P. M. (1994). "The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli." Structure 2:361-369. Pubmed: 8081752
  • Lawrence, M. C., Barbosa, J. A., Smith, B. J., Hall, N. E., Pilling, P. A., Ooi, H. C., Marcuccio, S. M. (1997). "Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase." J Mol Biol 266:381-399. Pubmed: 9047371
  • Ohta, Y., Watanabe, K., Kimura, A. (1985). "Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase." Nucleic Acids Res 13:8843-8852. Pubmed: 3909108