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Database: UniProt
Entry: A0A085GJB2_9GAMM
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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
//
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