CDD_SALG2
ID CDD_SALG2 Reviewed; 294 AA.
AC B5RC22;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=SG2219;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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}.
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; AM933173; CAR38054.1; -; Genomic_DNA.
DR RefSeq; WP_000553526.1; NC_011274.1.
DR AlphaFoldDB; B5RC22; -.
DR SMR; B5RC22; -.
DR EnsemblBacteria; CAR38054; CAR38054; SG2219.
DR KEGG; seg:SG2219; -.
DR HOGENOM; CLU_052424_0_0_6; -.
DR OMA; NYSPCGH; -.
DR Proteomes; UP000008321; 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..294
FT /note="Cytidine deaminase"
FT /id="PRO_1000147110"
FT DOMAIN 48..168
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 186..294
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 294 AA; 31619 MW; B9685CBDC800A8C8 CRC64;
MHPRFQTAFA QLADNLQSAL APILADHHFP AMLTAEQVST LKNTAGLDED ALAFALLPLA
AACARTDLSH FNVGAIARGV SGNWYFGANM EFLGATMQQT VHAEQSAISH AWLRGEKGLA
AVTVNYTPCG HCRQFMNELN SGLDLRIHLP GRAPHTLRDY LPDAFGPKDL EIKTLLMDEQ
DHGFTLTGDT LTQAAITAAN KSHMPYSHSP SGVALECKDG RIFTGSYAEN AAFNPTLPPL
QGALNLLSLN GYDYADIQRA ILAEKGDAAL IQWDATAATL KALGCHNIDR VLLG
