ID CDD_SHEFN Reviewed; 298 AA. AC Q083S7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=Cytidine deaminase; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; DE Short=CDA; GN Name=cdd; OrderedLocusNames=Sfri_1637; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000447; ABI71488.1; -; Genomic_DNA. DR RefSeq; YP_750326.1; -. DR GeneID; 4277296; -. DR GenomeReviews; CP000447_GR; Sfri_1637. DR KEGG; sfr:Sfri_1637; -. DR NMPDR; fig|318167.10.peg.1579; -. DR HOGENOM; Q083S7; -. DR OMA; Q083S7; FSPCGHC. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR HAMAP; MF_01558; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn_bd. 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 PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Zinc. FT CHAIN 1 298 Cytidine deaminase. FT /FTId=PRO_1000068962. FT REGION 88 90 Substrate binding (By similarity). FT ACT_SITE 103 103 Proton donor (By similarity). FT METAL 101 101 Zinc; catalytic (By similarity). FT METAL 128 128 Zinc; catalytic (By similarity). FT METAL 131 131 Zinc; catalytic (By similarity). SQ SEQUENCE 298 AA; 32381 MW; 01CA4F986ED81484 CRC64; MQNRFLESIT QLDKPLANAL VPLLHDQFCG HIDASQFAGL VKASGKTEQQ VLMDLLPIAA ALANPPISEF YVGAIAKGSS GDLYMGANLE LPGEALFHSV HAEQSAISHA WLSGETEIVD IIVNFSPCGH CRQFMNELVN GSKINIHLPN QETQTLAHYL PYAFGPSDLD VTVPLLCKRE QEFNCDSDDP MIIEAIDQMG LSYAPYTNNN AAVVLETNDG ATFCGRYAES AAFNPSMQPM QMALSNLIRN NRQYSEIKRA VLVESSVGKI TLVGAAMDAL HAIAPIELQH MVVEPLLG //