FCYS_SCHPO
ID FCYS_SCHPO Reviewed; 162 AA.
AC O59834;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable cytosine deaminase;
DE EC=3.5.4.1;
DE AltName: Full=Cytosine aminohydrolase;
GN ORFNames=SPCC965.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA19074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:Q12178}.
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:0000250|UniProtKB:Q12178}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255}.
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DR EMBL; CU329672; CAA19074.1; -; Genomic_DNA.
DR PIR; T41667; T41667.
DR RefSeq; NP_588524.1; NM_001023513.2.
DR AlphaFoldDB; O59834; -.
DR SMR; O59834; -.
DR BioGRID; 276153; 5.
DR STRING; 4896.SPCC965.14c.1; -.
DR MaxQB; O59834; -.
DR PaxDb; O59834; -.
DR EnsemblFungi; SPCC965.14c.1; SPCC965.14c.1:pep; SPCC965.14c.
DR GeneID; 2539595; -.
DR KEGG; spo:SPCC965.14c; -.
DR PomBase; SPCC965.14c; -.
DR VEuPathDB; FungiDB:SPCC965.14c; -.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_025810_5_1_1; -.
DR InParanoid; O59834; -.
DR OMA; GDHPENP; -.
DR PhylomeDB; O59834; -.
DR UniPathway; UPA00574; UER00635.
DR PRO; PR:O59834; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0102480; F:5-fluorocytosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004131; F:cytosine deaminase activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0019858; P:cytosine metabolic process; ISO:PomBase.
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..162
FT /note="Probable cytosine deaminase"
FT /id="PRO_0000310831"
FT DOMAIN 8..132
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 59
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 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
SQ SEQUENCE 162 AA; 17882 MW; 5CF5389CE67308D4 CRC64;
MSSTELSEKD LAYLREAIKV SQQARDEGQH PFGCIIVDEN DNVIMSAGNR VPDGDVTQHA
ETRAVGLITK TRRDLEKCTL YTSTEPCAMC SGAIFWSGIR RMIFGLSNEN LIKLTQKSGE
CPPLYINSRD ILGAASHPIE VVGPYIEDEA IIPHKGFWDG GR
