Cytidine deaminase
Details
- Name
- Cytidine deaminase
- Synonyms
- 3.5.4.5
- CDA
- Cytidine aminohydrolase
- Gene Name
- cdd
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0004020|Cytidine deaminase MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLA AACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALA AITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDYLPDAFGPKDLEIKTLLMDEQ DHGYALTGDALSQAAIAAANRSHMPYSKSPSGVALECKDGRIFSGSYAENAAFNPTLPPL QGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA
- Number of residues
- 294
- Molecular Weight
- 31539.445
- Theoretical pI
- 5.53
- GO Classification
- Functionscytidine deaminase activity / deoxycytidine deaminase activity / identical protein binding / pyrimidine nucleoside binding / zinc ion bindingProcessescytidine deamination / deoxycytidine catabolic process / nucleobase-containing small molecule interconversionComponentscytosol
- General Function
- Zinc ion binding
- Specific Function
- This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0019226|Cytidine deaminase (cdd) ATGCATCCACGTTTTCAAACCGCTTTTGCCCAACTTGCGGATAACTTGCAATCTGCACTG GAACCTATTCTGGCAGACAAGTACTTCCCCGCTTTGTTGACCGGGGAGCAAGTCTCATCG CTGAAGAGCGCAACGGGGCTGGACGAAGACGCGCTGGCATTCGCACTACTTCCGCTGGCG GCGGCCTGTGCGCGTACGCCATTGTCGAATTTTAATGTTGGCGCAATTGCGCGCGGTGTG AGCGGAACCTGGTATTTCGGTGCCAATATGGAATTTATTGGTGCGACAATGCAGCAAACC GTTCATGCCGAACAAAGCGCGATCAGCCACGCCTGGTTGAGTGGTGAAAAAGCGCTTGCA GCCATCACCGTTAACTACACGCCTTGTGGTCACTGCCGTCAGTTTATGAATGAACTGAAC AGCGGTCTGGATCTGCGTATTCATCTGCCGGGCCGCGAGGCACACGCGCTGCGTGACTAT CTGCCAGATGCCTTTGGGCCGAAAGATCTGGAGATTAAAACGCTGCTGATGGACGAACAG GATCACGGCTATGCGCTGACGGGTGATGCGCTTTCTCAGGCAGCGATTGCGGCGGCAAAC CGTTCGCACATGCCTTACAGTAAGTCGCCAAGCGGTGTCGCGCTGGAATGTAAAGACGGT CGTATTTTCAGTGGCAGCTACGCTGAAAACGCCGCATTCAACCCGACTCTGCCACCGTTG CAGGGAGCGTTAATTCTGTTGAATCTCAAGGGTTATGATTACCCGGATATCCAGCGCGCG GTTCTGGCAGAAAAAGCCGATGCGCCGTTGATTCAGTGGGATGCCACCTCCGCAACGCTG AAAGCTCTCGGCTGTCACAGTATCGACCGAGTGCTTCTCGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0ABF6 UniProtKB Entry Name CDD_ECOLI GenBank Protein ID 145470 GenBank Gene ID M60916 - General References
- Yang C, Carlow D, Wolfenden R, Short SA: Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene. Biochemistry. 1992 May 5;31(17):4168-74. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Valentin-Hansen P, Holst B, Josephsen J, Hammer K, Albrechtsen B: CRP/cAMP- and CytR-regulated promoters in Escherichia coli K12: the cdd promoter. Mol Microbiol. 1989 Oct;3(10):1385-90. [Article]
- Frick L, Yang C, Marquez VE, Wolfenden R: 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. 1989 Nov 28;28(24):9423-30. [Article]
- Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C: Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5011-5. [Article]
- Gonzalez-Gil G, Bringmann P, Kahmann R: FIS is a regulator of metabolism in Escherichia coli. Mol Microbiol. 1996 Oct;22(1):21-9. [Article]
- Rida S, Caillet J, Alix JH: Amplification of a novel gene, sanA, abolishes a vancomycin-sensitive defect in Escherichia coli. J Bacteriol. 1996 Jan;178(1):94-102. [Article]
- Betts L, Xiang S, Short SA, Wolfenden R, Carter CW Jr: Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex. J Mol Biol. 1994 Jan 14;235(2):635-56. [Article]
- Xiang S, Short SA, Wolfenden R, Carter CW Jr: Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis. Biochemistry. 1996 Feb 6;35(5):1335-41. [Article]
- Xiang S, Short SA, Wolfenden R, Carter CW Jr: The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization. Biochemistry. 1997 Apr 22;36(16):4768-74. [Article]