Canmetcon
Identification
Name:Cyanate hydratase
Synonyms:
  • Cyanase
  • Cyanate hydrolase
  • Cyanate lyase
Gene Name:cynS
Enzyme Class:
Biological Properties
General Function:Involved in cyanate hydratase activity
Specific Function:Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb
Thumb+Thumb+2 Thumb+ThumbThumb+2 Thumb
SMPDB Reactions:
Thumb+Cyanate+Thumb+ThumbThumb
Thumb+Thumb+ThumbThumb+Thumb
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb
Complex Reactions:
Thumb+3 Thumb+Thumb2 Thumb+Thumb
Thumb+Thumb+2 ThumbThumb+2 Thumb
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB03551Carbamic acidMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB02078CyanateMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
binding
carbon-nitrogen lyase activity
carbon-oxygen lyase activity
catalytic activity
cyanate hydratase activity
DNA binding
hydro-lyase activity
lyase activity
nucleic acid binding
Process
cellular metabolic process
cyanate metabolic process
metabolic process
organic acid metabolic process
Gene Properties
Blattner:b0340
Gene OrientationClockwise
Centisome Percentage:7.73
Left Sequence End358713
Right Sequence End359183
Gene Sequence:
>471 bp
ATGATTCAGTCACAAATTAACCGCAATATTCGTCTTGATCTTGCCGATGCCATTTTGCTC
AGCAAAGCTAAAAAAGATCTCTCATTTGCCGAGATTGCCGACGGCACCGGTCTGGCAGAA
GCCTTTGTAACCGCGGCTTTGCTGGGTCAGCAGGCGCTTCCTGCCGACGCCGCCCGCCTG
GTCGGGGCGAAGCTGGATCTCGACGAAGACTCCATTCTACTGTTGCAGATGATTCCACTG
CGTGGCTGCATTGATGACCGTATTCCAACTGACCCAACGATGTATCGTTTCTATGAAATG
TTGCAGGTGTACGGTACAACCCTGAAAGCGTTGGTTCATGAGAAATTTGGCGATGGCATT
ATTAGCGCGATTAACTTCAAACTCGACGTTAAGAAAGTGGCGGACCCGGAAGGTGGCGAA
CGTGCGGTCATCACCTTAGATGGTAAATATCTGCCGACCAAACCGTTCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:156
Protein Molecular Weight:17049
Protein Theoretical pI:5
PDB File:1DWK
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cyanate hydratase
MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARL
VGAKLDLDEDSILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGI
ISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF
References
External Links:
ResourceLink
Uniprot ID:P00816
Uniprot Name:CYNS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674482
PDB ID:1DWK
Ecogene ID:EG10175
Ecocyc:EG10175
ColiBase:b0340
Kegg Gene:b0340
EchoBASE ID:EB0172
CCDB:CYNS_ECOLI
BacMap:16128325
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
  • Chin, C. C., Anderson, P. M., Wold, F. (1983). "The amino acid sequence of Escherichia coli cyanase." J Biol Chem 258:276-282. Pubmed: 6336748
  • 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
  • Little, R. M., Anderson, P. M. (1987). "Structural properties of cyanase. Denaturation, renaturation, and role of sulfhydryls and oligomeric structure in catalytic activity." J Biol Chem 262:10120-10126. Pubmed: 3301828
  • Sung, Y. C., Anderson, P. M., Fuchs, J. A. (1987). "Characterization of high-level expression and sequencing of the Escherichia coli K-12 cynS gene encoding cyanase." J Bacteriol 169:5224-5230. Pubmed: 2822670
  • Sung, Y. C., Fuchs, J. A. (1988). "Characterization of the cyn operon in Escherichia coli K12." J Biol Chem 263:14769-14775. Pubmed: 3049588
  • Walsh, M. A., Otwinowski, Z., Perrakis, A., Anderson, P. M., Joachimiak, A. (2000). "Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site." Structure 8:505-514. Pubmed: 10801492