CDA8_ARATH
ID CDA8_ARATH Reviewed; 293 AA.
AC Q9XEX4; Q9XHQ8;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cytidine deaminase 8;
DE EC=3.5.4.5;
GN Name=CDA8; Synonyms=DESA; OrderedLocusNames=At4g29570; ORFNames=T16L4.80;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Sanchez H., Schuster W.;
RT "Cytidine deaminases in Arabidopsis thaliana: a gene family of eight
RT members are located within a 24 kb region.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Faivre-Nitschke S.E., Grienenberger J.M., Gualberto J.M.;
RT "Cloning and characterisation of a cytidine deaminase gene family from
RT Arabidopsis thaliana.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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).
CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC 2'-deoxycytidine for UMP synthesis. {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AF121877; AAD30441.1; -; Genomic_DNA.
DR EMBL; AF080676; AAD39263.1; -; Genomic_DNA.
DR EMBL; AL079344; CAB45317.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79715.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85646.1; -; Genomic_DNA.
DR PIR; T09920; T09920.
DR RefSeq; NP_194686.1; NM_119102.3.
DR AlphaFoldDB; Q9XEX4; -.
DR SMR; Q9XEX4; -.
DR STRING; 3702.AT4G29570.1; -.
DR PaxDb; Q9XEX4; -.
DR PRIDE; Q9XEX4; -.
DR ProteomicsDB; 223923; -.
DR EnsemblPlants; AT4G29570.1; AT4G29570.1; AT4G29570.
DR GeneID; 829078; -.
DR Gramene; AT4G29570.1; AT4G29570.1; AT4G29570.
DR KEGG; ath:AT4G29570; -.
DR Araport; AT4G29570; -.
DR TAIR; locus:2134413; AT4G29570.
DR eggNOG; KOG0833; Eukaryota.
DR HOGENOM; CLU_052424_1_0_1; -.
DR InParanoid; Q9XEX4; -.
DR OMA; KIADPDC; -.
DR OrthoDB; 1400471at2759; -.
DR PhylomeDB; Q9XEX4; -.
DR BioCyc; ARA:AT4G29570-MON; -.
DR PRO; PR:Q9XEX4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEX4; baseline and differential.
DR Genevisible; Q9XEX4; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0009972; P:cytidine deamination; IBA:GO_Central.
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 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; Reference proteome; Zinc.
FT CHAIN 1..293
FT /note="Cytidine deaminase 8"
FT /id="PRO_0000429150"
FT DOMAIN 20..151
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 181..293
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
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 BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="H -> Q (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="N -> I (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="R -> H (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="R -> G (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> I (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="H -> Q (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..151
FT /note="LISQ -> FISL (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="C -> Y (in Ref. 2; AAD39263)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32276 MW; 82162EDB87537256 CRC64;
MAQPMRFMLN HIETESYGAF TPQNLSPLIN RAIPHTRAQI SGSPVVAVGR GSSGRTFFGV
NVELPGLPLD HSIHAEQFLL ANLALHFEQK LECIAISTNG YYFQEPCGHC CQLLHKIRDM
SDTKILLTNP TGQKGTYMNL STFLPQGLIS QANVPRLLER NFNCIELINH SLYMDICSYS
EHCNHLNCRA LKAATISYAP DSKCPSGVAL IDHRGKVYSG GYMESVAHNT SLGPVQAALV
DFVANGDGQE FKNIVEAVLV EKKCGVLSQE ATARMILEKI ADPDCIFRVL HCK
