(data stored in ACNUC7421 zone)

SWISSPROT: Q750R5_ASHGO

ID   Q750R5_ASHGO            Unreviewed;       139 AA.
AC   Q750R5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=Cytidine deaminase {ECO:0000256|RuleBase:RU364006};
DE            EC=3.5.4.5 {ECO:0000256|RuleBase:RU364006};
DE   AltName: Full=Cytidine aminohydrolase {ECO:0000256|RuleBase:RU364006};
GN   ORFNames=AGOS_AGL123W {ECO:0000313|EMBL:AAS54368.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54368.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54368.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC       2'-deoxycytidine for UMP synthesis. {ECO:0000256|RuleBase:RU364006}.
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|RuleBase:RU364006};
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|RuleBase:RU364006};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|RuleBase:RU364006}.
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; AE016820; AAS54368.1; -; Genomic_DNA.
DR   RefSeq; NP_986544.1; NM_211606.1.
DR   STRING; 33169.AAS54368; -.
DR   EnsemblFungi; AAS54368; AAS54368; AGOS_AGL123W.
DR   GeneID; 4622843; -.
DR   KEGG; ago:AGOS_AGL123W; -.
DR   HOGENOM; HOG000014707; -.
DR   InParanoid; Q750R5; -.
DR   KO; K01489; -.
DR   OMA; LTHFTCV; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0009972; P:cytidine deamination; IBA:GO_Central.
DR   GO; GO:0006217; P:deoxycytidine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0008655; P:pyrimidine-containing compound salvage; IEA:EnsemblFungi.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR01354; cyt_deam_tetra; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750R5.
DR   SWISS-2DPAGE; Q750R5.
KW   Hydrolase {ECO:0000256|RuleBase:RU364006};
KW   Metal-binding {ECO:0000256|RuleBase:RU364006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Zinc {ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN          7..136
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   139 AA;  14850 MW;  842AD6331039B4BB CRC64;
     MPSTQGEPYQ GAVARALAAK ELSYSPYSKF RVGCCILTAS GEYIVGANVE NASYPAGICA
     ERTAVVKAVT AGHTNWVCIA LSGDSSDVVT PCGICRQVLR EFVDPKKLTV IMMNADGSKV
     LQRTLEELLP YSFGPDSLR
//

If you have problems or comments...

PBIL Back to PBIL home page