FCA1_CANAL
ID FCA1_CANAL Reviewed; 150 AA.
AC P78594; A0A1D8PPD4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cytosine deaminase {ECO:0000303|PubMed:9000374};
DE EC=3.5.4.1;
DE AltName: Full=Cytosine aminohydrolase;
GN Name=FCA1 {ECO:0000303|PubMed:9000374}; ORFNames=CAALFM_C600620WA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9000374; DOI=10.1007/s002940050169;
RA Erbs P., Exinger F., Jund R.;
RT "Characterization of the Saccharomyces cerevisiae FCY1 gene encoding
RT cytosine deaminase and its homologue FCA1 of Candida albicans.";
RL Curr. Genet. 31:1-6(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of cytosine to uracil or
CC 5-methylcytosine to thymine. Is involved in the pyrimidine salvage
CC pathway, which allows the cell to utilize cytosine for pyrimidine
CC nucleotide synthesis. {ECO:0000269|PubMed:9000374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytosine + H(+) + H2O = NH4(+) + uracil; Xref=Rhea:RHEA:20605,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16040,
CC ChEBI:CHEBI:17568, ChEBI:CHEBI:28938; EC=3.5.4.1;
CC Evidence={ECO:0000250|UniProtKB:Q12178};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q12178};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from cytosine: step 1/1. {ECO:0000305|PubMed:9000374}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12178}. Nucleus
CC {ECO:0000250|UniProtKB:Q12178}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; U55194; AAC15782.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30008.1; -; Genomic_DNA.
DR RefSeq; XP_019330987.1; XM_019475442.1.
DR AlphaFoldDB; P78594; -.
DR SMR; P78594; -.
DR STRING; 237561.A0A1D8PPD4; -.
DR GeneID; 30515327; -.
DR KEGG; cal:CAALFM_C600620WA; -.
DR CGD; CAL0000189710; FCA1.
DR VEuPathDB; FungiDB:C6_00620W_A; -.
DR VEuPathDB; FungiDB:CAWG_05296; -.
DR OrthoDB; 1616309at2759; -.
DR PhylomeDB; P78594; -.
DR UniPathway; UPA00574; UER00635.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0102480; F:5-fluorocytosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004131; F:cytosine deaminase activity; IGI:CGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019858; P:cytosine metabolic process; IGI:CGD.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..150
FT /note="Cytosine deaminase"
FT /id="PRO_0000171701"
FT DOMAIN 3..121
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
SQ SEQUENCE 150 AA; 16500 MW; BC83199148A87B59 CRC64;
MTFDDKKGLQ VALDQAKKSY SEGGIPIGSC IISSDDTVLG QGHNERIQKH SAILHGEMSA
LENAGRLPGK TYKDCTIYTT LSPCSMCTGA ILLYGFKRVV MGENVNFLGN EKLLIENGVE
VVNLNDQECI DLMAKFIKEK PQDWNEDIGE
