ID   CDA1_ARATH              Reviewed;         301 AA.
AC   O65896; Q8LEF2; Q9XEX5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   04-NOV-2026, entry version 166.
DE   RecName: Full=Cytidine deaminase 1 {ECO:0000303|PubMed:10024464, ECO:0000303|PubMed:10469156};
DE            Short=At-CDA1 {ECO:0000303|PubMed:10024464, ECO:0000303|PubMed:10469156};
DE            EC=3.5.4.5 {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
GN   Name=CDA1; Synonyms=CDD, DESZ; OrderedLocusNames=At2g19570;
GN   ORFNames=F3P11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Columbia;
RX   PubMed=10024464; DOI=10.1006/prep.1998.0959;
RA   Vincenzetti S., Cambi A., Neuhard J., Schnorr K., Grelloni M., Vita A.;
RT   "Cloning, expression, and purification of cytidine deaminase from
RT   Arabidopsis thaliana.";
RL   Protein Expr. Purif. 15:8-15(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10469156; DOI=10.1046/j.1432-1327.1999.00591.x;
RA   Faivre-Nitschke E.S., Grienenberger J.M., Gualberto J.M.;
RT   "A prokaryotic-type cytidine deaminase from Arabidopsis thaliana.";
RL   Eur. J. Biochem. 263:896-903(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RA   Kafer C., Thornburg R.W.;
RT   "Arabidopsis thaliana cytidine deaminase 1 shows more similarity to
RT   prokaryotic enzymes than to eukaryotic enzymes.";
RL   J. Plant Biol. 43:162-170(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sanchez H., Schuster W.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [7]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC       2'-deoxycytidine for UMP synthesis. Functions as a conventional
CC       cytidine deaminase. Has no affinity for RNA and is not involved in RNA-
CC       editing by C-to-U deamination. {ECO:0000269|PubMed:10024464,
CC       ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + H2O + H(+) = uridine + NH4(+);
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:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156,
CC         ECO:0000269|Ref.3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16070;
CC         Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156,
CC         ECO:0000269|Ref.3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + H2O + H(+) = 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:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156,
CC         ECO:0000269|Ref.3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13434;
CC         Evidence={ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156,
CC         ECO:0000269|Ref.3};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:10024464};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:10024464};
CC   -!- ACTIVITY REGULATION: Inhibited by uridine, CMP and dCMP.
CC       {ECO:0000269|PubMed:10024464, ECO:0000269|PubMed:10469156}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=150 uM for cytidine (at pH 7.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:10024464};
CC         KM=250 uM for cytidine (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:10469156};
CC         KM=226.1 uM for cytidine (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|Ref.3};
CC         KM=75 uM for 2'-deoxycytidine (at pH 7.5 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:10024464};
CC         KM=120 uM for 2'-deoxycytidine (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:10469156};
CC         KM=49.3 uM for 2'-deoxycytidine (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|Ref.3};
CC         Vmax=59.5 umol/min/mg enzyme toward cytidine (at pH 7.5 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:10024464};
CC         Vmax=58 umol/min/mg enzyme toward cytidine (at pH 7.5 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:10469156};
CC         Vmax=39.7 umol/min/mg enzyme toward cytidine (at pH 8.0 and 25
CC         degrees Celsius) {ECO:0000269|Ref.3};
CC         Vmax=49 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 7.5 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:10024464};
CC         Vmax=38 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 7.5 and 25
CC         degrees Celsius) {ECO:0000269|PubMed:10469156};
CC         Vmax=24.4 umol/min/mg enzyme toward 2'-deoxycytidine (at pH 8.0 and
CC         25 degrees Celsius, Ref.3) {ECO:0000269|PubMed:10024464,
CC         ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
CC       pH dependence:
CC         Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:10024464,
CC         ECO:0000269|PubMed:10469156, ECO:0000269|Ref.3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:10469156}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems and
CC       flowers. {ECO:0000269|PubMed:10469156}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD30449.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AJ005261; CAA06460.1; -; mRNA.
DR   EMBL; AJ005687; CAA06671.1; -; Genomic_DNA.
DR   EMBL; AF134487; AAF03358.1; -; mRNA.
DR   EMBL; AF121878; AAD30449.1; ALT_SEQ; mRNA.
DR   EMBL; AC005917; AAD10156.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06896.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7035561.1; -; Genomic_DNA.
DR   EMBL; AY128366; AAM91569.1; -; mRNA.
DR   EMBL; BT008708; AAP42721.1; -; mRNA.
DR   EMBL; AY085453; AAM62679.1; -; mRNA.
DR   PIR; T51733; T51733.
DR   RefSeq; NP_179547.1; NM_127515.4.
DR   PDB; 6L08; X-ray; 3.00 A; A/B=1-301.
DR   AlphaFoldDB; O65896; -.
DR   SMR; O65896; -.
DR   FunCoup; O65896; 225.
DR   IntAct; O65896; 1.
DR   STRING; 3702.O65896; -.
DR   PaxDb; 3702-O65896; -.
DR   ProteomicsDB; 223879; -.
DR   GeneID; 816476; -.
DR   KEGG; ath:AT2G19570; -.
DR   Araport; AT2G19570; -.
DR   TAIR; AT2G19570; CDA1.
DR   eggNOG; KOG0833; Eukaryota.
DR   HOGENOM; CLU_052424_1_0_1; -.
DR   InParanoid; O65896; -.
DR   OMA; AACNGFC; -.
DR   OrthoDB; 414540at2759; -.
DR   PhylomeDB; O65896; -.
DR   BioCyc; ARA:AT2G19570-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G19570-MONOMER; -.
DR   BRENDA; 3.5.4.5; 399.
DR   PRO; PR:O65896; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Proteomes; UP001984100; Chromosome 2.
DR   ExpressionAtlas; O65896; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0004126; F:cytidine deaminase activity; IDA:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006216; P:cytidine catabolic process; IMP:TAIR.
DR   GO; GO:0006217; P:deoxycytidine catabolic process; IBA:GO_Central.
DR   GO; GO:0046109; P:uridine biosynthetic process; IBA:GO_Central.
DR   CDD; cd01283; cytidine_deaminase; 2.
DR   FunFam; 3.40.140.10:FF:000006; Cytidine deaminase; 1.
DR   FunFam; 3.40.140.10:FF:000041; Cytidine deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR   InterPro; IPR050202; Cyt/Deoxycyt_deaminase.
DR   InterPro; IPR006263; Cyt_deam_dimer.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   NCBIfam; NF006537; cdd; 1.
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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..301
FT                   /note="Cytidine deaminase 1"
FT                   /id="PRO_0000429143"
FT   DOMAIN          23..156
FT                   /note="CMP/dCMP-type deaminase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   DOMAIN          188..301
FT                   /note="CMP/dCMP-type deaminase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        79
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        270
FT                   /note="E -> K (in Ref. 9; AAM62679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="F -> Y (in Ref. 9; AAM62679)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           10..20
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           78..88
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           194..202
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          233..237
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           243..250
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:6L08"
FT   HELIX           277..287
FT                   /evidence="ECO:0007829|PDB:6L08"
SQ   SEQUENCE   301 AA;  32582 MW;  91C17F09AA70CBB2 CRC64;
     MDKPSFVIQS KEAESAAKQL GVSVIQLLPS LVKPAQSYAR TPISKFNVAV VGLGSSGRIF
     LGVNVEFPNL PLHHSIHAEQ FLVTNLTLNG ERHLNFFAVS AAPCGHCRQF LQEIRDAPEI
     KILITDPNNS ADSDSAADSD GFLRLGSFLP HRFGPDDLLG KDHPLLLESH DNHLKISDLD
     SICNGNTDSS ADLKQTALAA ANRSYAPYSL CPSGVSLVDC DGKVYRGWYM ESAAYNPSMG
     PVQAALVDYV ANGGGGGYER IVGAVLVEKE DAVVRQEHTA RLLLETISPK CEFKVFHCYE
     A
//