Cytidine deaminase (P0ABF6)

Identification
Name:Cytidine deaminase
Synonyms:
  • Cytidine aminohydrolase
  • CDA
Gene Name:cdd
Enzyme Class:
Biological Properties
General Function:Involved in zinc ion binding
Specific Function:This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis
Cellular Location:Cytoplasmic
SMPDB Pathways:
  • Pyrimidine metabolism PW000942
  • Pyrimidine ribonucleosides degradtion PW002024
  • pyrimidine deoxyribonucleosides degradation PW002063
  • pyrimidine ribonucleosides degradation PW002104
  • salvage pathways of pyrimidine deoxyribonucleotides PW002061
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Cytidine + 1.0Water ↔ 1.0Uridine + 1.0Ammonia
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Deoxycytidine + 1.0Water ↔ 1.0Deoxyuridine + 1.0Ammonia
ReactionCard
1.05'-Deoxy-5-fluorocytidine+1.0Thumb ↔ 1.05'-Deoxy-5-fluorouridine+1.0Thumb
1.05'-Deoxy-5-fluorocytidine + 1.0Water ↔ 1.05'-Deoxy-5-fluorouridine + 1.0Ammonia
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Deoxycytidine → 1.0Ammonia + 1.0Deoxyuridine
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Cytidine → 1.0Ammonia + 1.0Uridine
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1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Cytidine + 1.0Water + 1.0Deoxycytidine ↔ 1.0Uridine + 1.0Ammonia + 1.0Deoxyuridine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Deoxycytidine → 1.0Ammonia + 1.0Deoxyuridine
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Cytidine → 1.0Ammonia + 1.0Uridine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Deoxycytidine + 1.0Hydrogen ion + 1.0Water → 1.0Deoxyuridine + 1.0Ammonium
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cytidine + 1.0Hydrogen ion + 1.0Water → 1.0Ammonium + 1.0Uridine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB00089CytidineMetaboCard
ECMDB00014DeoxycytidineMetaboCard
ECMDB00012DeoxyuridineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00296UridineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
cytidine deaminase activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
ion binding
metal ion binding
transition metal ion binding
zinc ion binding
Process
cellular nitrogen compound metabolic process
cytidine metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside metabolic process
pyrimidine nucleoside metabolic process
pyrimidine ribonucleoside metabolic process
Gene Properties
Blattner:b2143
Gene OrientationClockwise
Centisome Percentage:48.06
Left Sequence End2229866
Right Sequence End2230750
Gene Sequence:
>885 bp
ATGGCTATGGAAACGCAGGACATTATCAAAAGGTCCGCAACTAACTCCATCACGCCGCCT
TCTCAGGTGCGTGATTACAAAGCAGAAGTCGCAAAACTTATCGACGTTTCCACCTGTATC
GGCTGTAAAGCCTGTCAGGTGGCGTGTTCGGAGTGGAACGACATCCGTGATGAAGTGGGG
CACTGCGTCGGGGTTTACGATAACCCCGCCGATCTGAGCGCCAAGTCCTGGACGGTGATG
CGCTTTAGCGAAACCGAACAGAACGGCAAGCTGGAGTGGCTGATCCGTAAAGACGGCTGT
ATGCACTGTGAAGATCCCGGCTGCCTGAAGGCGTGCCCGTCTGCTGGTGCAATCATTCAG
TACGCTAACGGGATTGTCGATTTCCAGTCGGAAAACTGCATCGGCTGTGGTTACTGCATT
GCCGGGTGTCCGTTTAATATTCCGCGCCTCAACAAAGAGGATAACCGGGTATATAAATGC
ACGCTCTGCGTCGATCGCGTCAGCGTCGGCCAGGAACCGGCTTGTGTGAAAACCTGTCCG
ACCGGGGCTATCCACTTCGGCACCAAGAAGGAGATGCTGGAGCTGGCGGAACAGCGCGTG
GCGAAACTGAAAGCGCGTGGTTACGAACATGCTGGCGTCTACAACCCGGAAGGGGTCGGT
GGTACGCACGTTATGTACGTGCTGCATCACGCCGATCAGCCGGAGCTGTATCACGGTCTG
CCGAAAGATCCGAAGATCGACACCTCGGTAAGCCTGTGGAAAGGCGCGTTGAAACCGCTG
GCAGCGGCTGGCTTTATTGCCACTTTTGCCGGGTTGATTTTCCACTACATCGGTATTGGC
CCGAATAAGGAAGTGGACGATGACGAGGAGGATCATCATGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:294
Protein Molecular Weight:31539
Protein Theoretical pI:6
PDB File:1ALN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cytidine deaminase
MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLA
AACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALA
AITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDYLPDAFGPKDLEIKTLLMDEQ
DHGYALTGDALSQAAIAAANRSHMPYSKSPSGVALECKDGRIFSGSYAENAAFNPTLPPL
QGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA
References
External Links:
ResourceLink
Uniprot ID:P0ABF6
Uniprot Name:CDD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742408
PDB ID:1ALN
Ecogene ID:EG10137
Ecocyc:EG10137
ColiBase:b2143
Kegg Gene:b2143
EchoBASE ID:EB0135
CCDB:CDD_ECOLI
BacMap:16130081
General Reference:
  • Betts, L., Xiang, S., Short, S. A., Wolfenden, R., Carter, C. W. Jr (1994). "Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex." J Mol Biol 235:635-656. Pubmed: 8289286
  • 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
  • Frick, L., Yang, C., Marquez, V. E., Wolfenden, R. (1989). "Binding of pyrimidin-2-one ribonucleoside by cytidine deaminase as the transition-state analogue 3,4-dihydrouridine and the contribution of the 4-hydroxyl group to its binding affinity." Biochemistry 28:9423-9430. Pubmed: 2692708
  • Gonzalez-Gil, G., Bringmann, P., Kahmann, R. (1996). "FIS is a regulator of metabolism in Escherichia coli." Mol Microbiol 22:21-29. Pubmed: 8899705
  • 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
  • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Watanabe, C. (1993). "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Proc Natl Acad Sci U S A 90:5011-5015. Pubmed: 8506346
  • Rida, S., Caillet, J., Alix, J. H. (1996). "Amplification of a novel gene, sanA, abolishes a vancomycin-sensitive defect in Escherichia coli." J Bacteriol 178:94-102. Pubmed: 8550448
  • Valentin-Hansen, P., Holst, B., Josephsen, J., Hammer, K., Albrechtsen, B. (1989). "CRP/cAMP- and CytR-regulated promoters in Escherichia coli K12: the cdd promoter." Mol Microbiol 3:1385-1390. Pubmed: 2575702
  • Xiang, S., Short, S. A., Wolfenden, R., Carter, C. W. Jr (1996). "Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis." Biochemistry 35:1335-1341. Pubmed: 8634261
  • Xiang, S., Short, S. A., Wolfenden, R., Carter, C. W. Jr (1997). "The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization." Biochemistry 36:4768-4774. Pubmed: 9125497
  • Yang, C., Carlow, D., Wolfenden, R., Short, S. A. (1992). "Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene." Biochemistry 31:4168-4174. Pubmed: 1567863