ID CDD_SHIF8 Reviewed; 294 AA. AC Q0T2Y0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Cytidine deaminase; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; DE Short=CDA; GN Name=cdd; OrderedLocusNames=SFV_2218; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(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; CP000266; ABF04335.1; -; Genomic_DNA. DR RefSeq; YP_689640.1; -. DR SMR; Q0T2Y0; 1-294. DR GeneID; 4209516; -. DR GenomeReviews; CP000266_GR; SFV_2218. DR KEGG; sfv:SFV_2218; -. DR HOGENOM; Q0T2Y0; -. DR OMA; Q0T2Y0; FSPCGHC. DR BioCyc; SFLE373384:SFV_2218-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_1000068969. 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; 31540 MW; F0B5CD68AB145D7D 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 KALGCHSIDR VLLA //