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Database: UniProt
Entry: G8BCL7_CANPC
LinkDB: G8BCL7_CANPC
Original site: G8BCL7_CANPC 
ID   G8BCL7_CANPC            Unreviewed;       321 AA.
AC   G8BCL7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=thymidylate synthase {ECO:0000256|ARBA:ARBA00011947};
DE            EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN   OrderedLocusNames=CPAR2_206550 {ECO:0000313|CGD:CAL0000155249,
GN   ECO:0000313|EMBL:CCE43012.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE43012.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC         dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC         EC=2.1.1.45; Evidence={ECO:0000256|ARBA:ARBA00001707};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004992}.
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DR   EMBL; HE605206; CCE43012.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8BCL7; -.
DR   STRING; 578454.G8BCL7; -.
DR   EnsemblFungi; CPAR2_206550-T; CPAR2_206550-T-p1; CPAR2_206550.
DR   CGD; CAL0000155249; CPAR2_206550.
DR   VEuPathDB; FungiDB:CPAR2_206550; -.
DR   eggNOG; KOG0673; Eukaryota.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000005221; Chromosome 2.
DR   GO; GO:0010181; F:FMN binding; IEA:EnsemblFungi.
DR   GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:EnsemblFungi.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:EnsemblFungi.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR   Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR   InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   InterPro; IPR020940; Thymidylate_synthase_AS.
DR   NCBIfam; TIGR03284; thym_sym; 2.
DR   PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..321
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
SQ   SEQUENCE   321 AA;  36558 MW;  C47C51652B988B8A CRC64;
     MTVSINKAEQ AYLDLCQKII DEGEHRPDRT GTGTKSLFAP PQLRFDLSND SFPLLTTKRV
     FSKGIIHELL WFIAGSTDAK ILSEKGVKIW EGNGSREFLD NLGLTHRREG DLGPVYGFQW
     RHFGAEYKDC DTDYTGQGFD QLQDVIKKLK TNPYDRRIIM SAWNPPDFSL MALPPCHVFC
     QFYVSFPNES QSASNSNTSN TKKAKISSRP KLSCLLYQRS CDMGLGVPFN IASYALLTKM
     VAHVVDMDCG EFIHTLGDAH VYLDHIDALK EQMTRIPKQF PKLVIKEERK DAIKTIDDFK
     FEDFEIVGYE PYPSIKMKMS V
//
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