ID A0A085GJB2_9GAMM Unreviewed; 294 AA.
AC A0A085GJB2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:KFC83807.1};
GN ORFNames=GEAM_0990 {ECO:0000313|EMBL:KFC83807.1};
OS Ewingella americana ATCC 33852.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Ewingella.
OX NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC83807.1, ECO:0000313|Proteomes:UP000028640};
RN [1] {ECO:0000313|EMBL:KFC83807.1, ECO:0000313|Proteomes:UP000028640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC83807.1,
RC ECO:0000313|Proteomes:UP000028640};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFC83807.1}.
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DR EMBL; JMPJ01000033; KFC83807.1; -; Genomic_DNA.
DR RefSeq; WP_034789069.1; NZ_JMPJ01000033.1.
DR AlphaFoldDB; A0A085GJB2; -.
DR STRING; 910964.GEAM_0990; -.
DR GeneID; 78379332; -.
DR eggNOG; COG0295; Bacteria.
DR OrthoDB; 9795347at2; -.
DR Proteomes; UP000028640; Unassembled WGS sequence.
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 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 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:UP000028640};
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 187..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; 31626 MW; F6B586BDD481853C CRC64;
MHSRFLDAFA TLPATLQTAL EPLLSRDDFP AMLTAEQVAN VKAQTGLDDD ALAFSLLPLA
AACSLTPISH FHVGAVARGV SGNLYFGANM EFSGASMQQT VHAEQSAVTH AWLRGEAKLA
SITVNYTPCG HCRQFMNELN SGTELNIHLP DRDVATLGDY LPYSFGPKDL DITTLLMDKV
NHGYQIAEQD ALSQQALDAC NQSHAPYSQS HSGVALETEN GKIFAGRYAE NAAFNPSLPP
LQGALILLNL SGEDCLKIRR AVIVERHQPL VSQHDATRAT LAALGCQELS AITL
//