ID CDD_YEAST Reviewed; 142 AA. AC Q06549; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 88. DE RecName: Full=Cytidine deaminase; DE Short=CDA; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; GN Name=CDD1; OrderedLocusNames=YLR245C; ORFNames=L9672.13; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=ATCC 28383 / FL100 / VTT C-80102; RX MEDLINE=99431800; PubMed=10501935; DOI=10.1007/s002940050482; RA Kurtz J.-E., Exinger F., Erbs P., Jund R.; RT "New insights into the pyrimidine salvage pathway of Saccharomyces RT cerevisiae: requirement of six genes for cytidine metabolism."; RL Curr. Genet. 36:130-136(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313267; PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND RP SUBUNIT. RX PubMed=15148397; DOI=10.1073/pnas.0400493101; RA Xie K., Sowden M.P., Dance G.S., Torelli A.T., Smith H.C., RA Wedekind J.E.; RT "The structure of a yeast RNA-editing deaminase provides insight into RT the fold and function of activation-induced deaminase and APOBEC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 101:8114-8119(2004). CC -!- FUNCTION: This enzyme scavenge exogenous and endogenous cytidine CC and 2'-deoxycytidine for UMP synthesis. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-4455, EBI-4455; CC P32502:GCD7; NbExp=1; IntAct=EBI-4455, EBI-6260; CC Q02866:MUK1; NbExp=1; IntAct=EBI-4455, EBI-32646; CC Q02821:SRP1; NbExp=1; IntAct=EBI-4455, EBI-1797; CC -!- MISCELLANEOUS: Present with 3120 molecules/cell in log phase SD CC medium. 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; AF080089; AAD04031.1; -; Genomic_DNA. DR EMBL; U20865; AAB67399.1; -; Genomic_DNA. DR EMBL; AY557930; AAS56256.1; -; Genomic_DNA. DR PIR; S59391; S59391. DR RefSeq; NP_013346.1; -. DR PDB; 1R5T; X-ray; 2.00 A; A/B/C/D=1-142. DR PDBsum; 1R5T; -. DR DIP; DIP:1252N; -. DR IntAct; Q06549; 6. DR PeptideAtlas; Q06549; -. DR PRIDE; Q06549; -. DR Ensembl; YLR245C; Saccharomyces cerevisiae. DR GeneID; 850946; -. DR GenomeReviews; Y13138_GR; YLR245C. DR KEGG; sce:YLR245C; -. DR NMPDR; fig|4932.3.peg.4359; -. DR CYGD; YLR245c; -. DR SGD; S000004235; CDD1. DR HOGENOM; Q06549; -. DR OMA; Q06549; YMTKLDG. DR BRENDA; 3.5.4.5; 250. DR NextBio; 967405; -. DR ArrayExpress; Q06549; -. DR GermOnline; YLR245C; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0004126; F:cytidine deaminase activity; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006216; P:cytidine catabolic process; IDA:SGD. DR GO; GO:0006217; P:deoxycytidine catabolic process; IDA:SGD. DR GO; GO:0008655; P:pyrimidine salvage; IDA:SGD. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn_bd. DR InterPro; IPR006262; Cyt_deam_tetra. DR PANTHER; PTHR11644:SF2; Cyt_deam_tetra; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR TIGRFAMs; TIGR01354; cyt_deam_tetra; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Metal-binding; Zinc. FT CHAIN 1 142 Cytidine deaminase. FT /FTId=PRO_0000171685. FT REGION 50 52 Substrate binding (By similarity). FT ACT_SITE 63 63 Proton donor (By similarity). FT METAL 61 61 Zinc; catalytic. FT METAL 96 96 Zinc; catalytic. FT METAL 99 99 Zinc; catalytic. FT HELIX 8 21 FT HELIX 22 24 FT TURN 28 30 FT STRAND 34 39 FT STRAND 45 49 FT HELIX 56 58 FT HELIX 62 72 FT STRAND 81 87 FT STRAND 89 91 FT HELIX 97 104 FT STRAND 112 116 FT STRAND 118 127 FT HELIX 128 131 FT HELIX 138 140 SQ SEQUENCE 142 AA; 15536 MW; 962BD69CCB30D51F CRC64; MKVGGIEDRQ LEALKRAALK ACELSYSPYS HFRVGCSILT NNDVIFTGAN VENASYSNCI CAERSAMIQV LMAGHRSGWK CMVICGDSED QCVSPCGVCR QFINEFVVKD FPIVMLNSTG SRSKVMTMGE LLPMAFGPSH LN //