ID CDD_ECOUT Reviewed; 294 AA. AC Q1R9T0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Cytidine deaminase; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; DE Short=CDA; GN Name=cdd; OrderedLocusNames=UTI89_C2416; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: This enzyme scavenge exogenous and endogenous cytidine CC and 2'-deoxycytidine for UMP synthesis (By similarity). CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Binds 1 zinc ion (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE07884.1; -; Genomic_DNA. DR RefSeq; YP_541415.1; -. DR SMR; Q1R9T0; 1-294. DR GeneID; 3990463; -. DR GenomeReviews; CP000243_GR; UTI89_C2416. DR KEGG; eci:UTI89_C2416; -. DR HOGENOM; Q1R9T0; -. DR OMA; Q1R9T0; FSPCGHC. DR BioCyc; ECOL364106:UTI89_C2416-MON; -. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0046087; P:cytidine metabolic process; IEA:InterPro. DR HAMAP; MF_01558; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn_bd. DR InterPro; IPR006263; Cyt_deam_dimer. DR InterPro; IPR013171; dC_C_deam_Zn_bd. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF08211; dCMP_cyt_deam_2; 1. DR TIGRFAMs; TIGR01355; cyt_deam_dimer; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Zinc. FT CHAIN 1 294 Cytidine deaminase. FT /FTId=PRO_1000068952. FT REGION 89 91 Substrate binding (By similarity). FT ACT_SITE 104 104 Proton donor (By similarity). FT METAL 102 102 Zinc; catalytic (By similarity). FT METAL 129 129 Zinc; catalytic (By similarity). FT METAL 132 132 Zinc; catalytic (By similarity). SQ SEQUENCE 294 AA; 31567 MW; 69B5CD68AB145D6C CRC64; MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA //