ID CDD_KLEP7 Reviewed; 294 AA. AC A6TBN1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Cytidine deaminase {ECO:0000255|HAMAP-Rule:MF_01558}; DE EC=3.5.4.5 {ECO:0000255|HAMAP-Rule:MF_01558}; DE AltName: Full=Cytidine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01558}; DE Short=CDA {ECO:0000255|HAMAP-Rule:MF_01558}; GN Name=cdd {ECO:0000255|HAMAP-Rule:MF_01558}; GN OrderedLocusNames=KPN78578_25410; ORFNames=KPN_02584; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and CC 2'-deoxycytidine for UMP synthesis. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; CC Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+); CC Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01558}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000255|HAMAP-Rule:MF_01558}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000647; ABR78002.1; -; Genomic_DNA. DR RefSeq; WP_002912869.1; NC_009648.1. DR PDB; 6K63; X-ray; 2.07 A; A/B/C/D=1-294. DR PDBsum; 6K63; -. DR AlphaFoldDB; A6TBN1; -. DR SMR; A6TBN1; -. DR STRING; 272620.KPN_02584; -. DR jPOST; A6TBN1; -. DR PaxDb; 272620-KPN_02584; -. DR EnsemblBacteria; ABR78002; ABR78002; KPN_02584. DR KEGG; kpn:KPN_02584; -. DR HOGENOM; CLU_052424_0_0_6; -. DR BRENDA; 3.5.4.5; 2817. DR Proteomes; UP000000265; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA. DR GO; GO:0042802; F:identical protein binding; IEA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR CDD; cd01283; cytidine_deaminase; 2. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2. DR HAMAP; MF_01558; Cyt_deam; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_dom. DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd. DR InterPro; IPR006263; Cyt_deam_dimer. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR020797; Cytidine_deaminase_bacteria. DR NCBIfam; TIGR01355; cyt_deam_dimer; 1. DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1. DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF08211; dCMP_cyt_deam_2; 1. DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Metal-binding; Zinc. FT CHAIN 1..294 FT /note="Cytidine deaminase" FT /id="PRO_1000068957" FT DOMAIN 48..168 FT /note="CMP/dCMP-type deaminase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT DOMAIN 186..294 FT /note="CMP/dCMP-type deaminase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083" FT ACT_SITE 104 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 89..91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01558" FT HELIX 6..10 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:6K63" FT TURN 21..24 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 49..61 FT /evidence="ECO:0007829|PDB:6K63" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 119..126 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 190..200 FT /evidence="ECO:0007829|PDB:6K63" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 239..249 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 257..264 FT /evidence="ECO:0007829|PDB:6K63" FT HELIX 273..282 FT /evidence="ECO:0007829|PDB:6K63" FT STRAND 289..292 FT /evidence="ECO:0007829|PDB:6K63" SQ SEQUENCE 294 AA; 31477 MW; F19BB2A84665249A CRC64; MHSRFQAALT TLAADLQAAI APMLADPHFP ALLEADQVAT LQHATGLDED ALAFALLPLA AACARPDLSH FNVGAIARGV SGRWYFGGNM EFLGATMQQT VHAEQSAISH AWLRGETSLR AITVNYTPCG HCRQFMNELN SGLALRIHLP GREAHALEHY LPDAFGPKDL EIKTLLMDEQ DHGFPVSGDA LTQAAIQAAN RCHAPYSHSP SGVALELKDG TIFSGSYAEN AAFNPTLPPL QGALNLLSLN GYDYPAIQRA ILAEKADAAL IQWDATVATL KALGCHNIER VLLG //