ID CDD_SODGM Reviewed; 309 AA. AC Q2NUD2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Cytidine deaminase; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; DE Short=CDA; GN Name=cdd; OrderedLocusNames=SG0968; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Sodalis. OX NCBI_TaxID=343509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., RA Hattori M., Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse RT host."; RL Genome Res. 16:149-156(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; AP008232; BAE74243.1; -; Genomic_DNA. DR RefSeq; YP_454648.1; -. DR GeneID; 3867095; -. DR GenomeReviews; AP008232_GR; SG0968. DR KEGG; sgl:SG0968; -. DR NMPDR; fig|343509.6.peg.2011; -. DR HOGENOM; Q2NUD2; -. DR OMA; Q2NUD2; FSPCGHC. DR BioCyc; SGLO343509:SG0968-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 1 309 Cytidine deaminase. FT /FTId=PRO_1000068970. 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 309 AA; 32837 MW; 9A267DF61C0391EF CRC64; MIARFAPALA AVSPALHTAL APLLDHHAFA GWLSAPQVKE LMQAGGLDED ALCFTLLPLA AAYAVTPLSH FNVGAIACGI SGNLYFGANM EFLAAPLQQT VHAEQSAIAH AWLRGEKRLR ALTVNYTPCG HCRQFMNELN SGTDLIICLP ERSAATLASY LPDAFGPRDL AIQSLLLDEI DHAFAAAAWL DHDLSAPSPD DNDPLVSTAL DAASRSHAPY SQSHSGVALQ TQDGCVYAGR YAENAAFNPS LPPLQTALIL MNAAGADDRQ IRRAVLAERQ NAPITQWPAT NATLAALGCH EVHHLSLSL //