ID A0A0L7TAE0_9GAMM Unreviewed; 296 AA.
AC A0A0L7TAE0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=NG42_03025 {ECO:0000313|EMBL:KOC92191.1}, NG43_19575
GN {ECO:0000313|EMBL:KOC88852.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC92191.1, ECO:0000313|Proteomes:UP000037088};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC92191.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC88852.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC92191.1}.
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; JRXF01000041; KOC88852.1; -; Genomic_DNA.
DR EMBL; JRXE01000003; KOC92191.1; -; Genomic_DNA.
DR RefSeq; WP_052897703.1; NZ_JRXF01000041.1.
DR AlphaFoldDB; A0A0L7TAE0; -.
DR STRING; 1560201.NG42_03025; -.
DR PATRIC; fig|1560201.3.peg.650; -.
DR OrthoDB; 9795347at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
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; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR020797; Cytidine_deaminase_bacteria.
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:UP000037088};
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..296
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 296 AA; 31668 MW; 66C86941F56D82FE CRC64;
MHPRFQSAFA DLSPELQSAL KPILDAEDFS ARFSPEQIAA IKQQTALDED ALAFALLPLA
AACALAPLSD FNVGAVARGK SGSWYFGANM EFAGATMQQT VHAEQSAVTH AWLSGELALE
AITVNYSPCG HCRQFMNELN SGTALRIYLP GRQPATLGDY LPYAFGPRDL AIETLLLDPV
DHGYHLSGDA LEQQAINAAS HSHAPYSNAH SGVALESASG QIYAGRYAEN AAFNPSLPPL
QAALILLNMH GESCTQITRA VLAESPDGKL IQRQATEATL QALGCQHIRC VELQKP
//
