ID CDD_HAES1 Reviewed; 303 AA. AC Q0I4X6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-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=HS_1257; OS Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17172329; DOI=10.1128/JB.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) RT strain 129Pt and comparison to Haemophilus ducreyi 35000HP and RT Haemophilus influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). 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; CP000436; ABI25532.1; -; Genomic_DNA. DR RefSeq; YP_719469.1; -. DR GeneID; 4240768; -. DR GenomeReviews; CP000436_GR; HS_1257. DR KEGG; hso:HS_1257; -. DR NMPDR; fig|205914.1.peg.908; -. DR HOGENOM; Q0I4X6; -. DR OMA; Q0I4X6; FSPCGHC. DR BioCyc; HSOM205914:HS_1257-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 1 303 Cytidine deaminase. FT /FTId=PRO_0000318623. FT REGION 98 100 Substrate binding (By similarity). FT ACT_SITE 113 113 Proton donor (By similarity). FT METAL 111 111 Zinc; catalytic (By similarity). FT METAL 138 138 Zinc; catalytic (By similarity). FT METAL 141 141 Zinc; catalytic (By similarity). SQ SEQUENCE 303 AA; 34347 MW; 16CDCC47C9A6B43F CRC64; MTHHSLKHIS DRIKQALNQI ENRNLAQDLW YILGEQNFQG FLPAFTVNHF CEKYHMTDKE LALILLPVSA CYANPTISHF SVGAIAKGES GSFYFGANQE FCTTNIQQTV HAEQSAISHA WMRRESKITE ITVNYTPCGH CRQFMNELNS AETLRIHLPH SQDNLLHHYL PDAFGPHNLQ IDNRLFDKKA HNLFFVTEDP LIQAALDAAN QSHAPYSKTY SGIALQLQDQ QIFQGSYAEN AAFNPSLPPL QTALNYLLLN GNEVENIARA VLVEQPFRLS YRGMTEELLA YLGDIPLDYI QVS //