CDD_PECCP
ID CDD_PECCP Reviewed; 296 AA.
AC C6DDS7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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}; OrderedLocusNames=PC1_1495;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP001657; ACT12539.1; -; Genomic_DNA.
DR RefSeq; WP_015839765.1; NC_012917.1.
DR AlphaFoldDB; C6DDS7; -.
DR SMR; C6DDS7; -.
DR STRING; 561230.PC1_1495; -.
DR EnsemblBacteria; ACT12539; ACT12539; PC1_1495.
DR KEGG; pct:PC1_1495; -.
DR eggNOG; COG0295; Bacteria.
DR HOGENOM; CLU_052424_0_0_6; -.
DR OMA; NYSPCGH; -.
DR OrthoDB; 959039at2; -.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF08211; dCMP_cyt_deam_2; 1.
DR SUPFAM; SSF53927; SSF53927; 2.
DR TIGRFAMs; TIGR01355; cyt_deam_dimer; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..296
FT /note="Cytidine deaminase"
FT /id="PRO_1000215505"
FT DOMAIN 48..168
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 187..296
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"
SQ SEQUENCE 296 AA; 32120 MW; 44DDC91C25AA3485 CRC64;
MHPRFENAFR QLPASLQAAL RPLIDKPDFA AMLTADDVNA VCEASQLDAD ALAFALLPLA
AACAQAPISN FQVGAIAQGL SGNFYFGANM EFSAVQLQQT VHAEQSAVSH AWMRNERGLR
AVTVNYTPCG HCRQFMNELR DAASLRIQLP GRQPATLSHY LPDSFGPVDL QIDTLLMDDI
NHGATLQNMN ALARQALDAA NRSHAPYSKA ISGIVLETSS GNTYTGRYAE NAAFNPSLPP
LQTALNLMNL AGEDLSTVKH AVVVERRNAV VSHWAISQIM LAELGCTDVE HHFIEE
