ID D8MUK1_ERWBE Unreviewed; 294 AA.
AC D8MUK1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Cytidine deaminase {ECO:0000256|HAMAP-Rule:MF_01558};
DE EC=3.5.4.5 {ECO:0000256|HAMAP-Rule:MF_01558};
DE AltName: Full=Cytidine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_01558};
DE Short=CDA {ECO:0000256|HAMAP-Rule:MF_01558};
GN Name=cdd {ECO:0000256|HAMAP-Rule:MF_01558,
GN ECO:0000313|EMBL:CAX60508.1};
GN OrderedLocusNames=EbC_29770 {ECO:0000313|EMBL:CAX60508.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX60508.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60508.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60508.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC 2'-deoxycytidine for UMP synthesis. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01558};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01558,
CC ECO:0000256|PIRSR:PIRSR006334-3};
CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_01558,
CC ECO:0000256|PIRSR:PIRSR006334-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01558}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576, ECO:0000256|HAMAP-
CC Rule:MF_01558}.
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DR EMBL; FP236843; CAX60508.1; -; Genomic_DNA.
DR RefSeq; WP_013202993.1; NC_014306.1.
DR AlphaFoldDB; D8MUK1; -.
DR STRING; 634500.EbC_29770; -.
DR KEGG; ebi:EbC_29770; -.
DR eggNOG; COG0295; Bacteria.
DR HOGENOM; CLU_052424_0_0_6; -.
DR Proteomes; UP000008793; 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; 1.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01558};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01558}; Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01558}.
FT DOMAIN 48..168
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 186..294
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01558,
FT ECO:0000256|PIRSR:PIRSR006334-1"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01558,
FT ECO:0000256|PIRSR:PIRSR006334-2"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01558,
FT ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01558,
FT ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01558,
FT ECO:0000256|PIRSR:PIRSR006334-3"
SQ SEQUENCE 294 AA; 30950 MW; 77794D407DAFF21C CRC64;
MHPRFQAAFA TQPTALQTAL LPILSAADFQ AFLTPAQVAD VKSASGLDDR ELAFALLPLA
AACAVAPLSH FNVGALARGK SGHLYFGANM EFVGATMQQT VHAEQSAVTH AWMRGEASLE
AITVNYTPCG HCRQFMNELN SGTALNIHLP GRAPATLGDY LPDAFGPRDL EIKTLLLDDV
DHQLSIKGDA LTQAALQAAN RSHAPYTQAW SGVALQSADG AIFAGSYAEN AAFNPSLPPL
QAALNLLSLA GHDVLTIQRA VLAEAPDARV IQRQATQATL HALGCANLTT VPLD
//
