ID   TYS3_ENCCU              Reviewed;         294 AA.
AC   Q8SRG2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Thymidylate synthase 3;
DE            Short=TS 3;
DE            Short=TSase 3;
DE            EC=2.1.1.45;
GN   Name=TS-3; OrderedLocusNames=ECU08_0090;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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;
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR   EMBL; AL590448; CAD26314.1; -; Genomic_DNA.
DR   RefSeq; NP_597138.1; NM_001041747.1.
DR   AlphaFoldDB; Q8SRG2; -.
DR   SMR; Q8SRG2; -.
DR   STRING; 284813.Q8SRG2; -.
DR   GeneID; 859560; -.
DR   KEGG; ecu:ECU08_0090; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_0090; -.
DR   HOGENOM; CLU_021669_0_2_1; -.
DR   InParanoid; Q8SRG2; -.
DR   OMA; WNEWEVG; -.
DR   OrthoDB; 1197342at2759; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
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; -; 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   PANTHER; PTHR11548; PTHR11548; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; SSF55831; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Nucleotide biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Thymidylate synthase 3"
FT                   /id="PRO_0000140907"
FT   ACT_SITE        174
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         29
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         154..155
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         194..197
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         197
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         205
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         235..237
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
SQ   SEQUENCE   294 AA;  33098 MW;  B2521707E86C157E CRC64;
     MPQDPRHPEH QYLDLVKHIL ENGARRMDRT GTGTLSVFGA TMRFSLEDNT FPLLTTRRVF
     YRGVVEELLF FLRGETDSKV LEKKGVRIWE KNGAKQFLQS VGIDREEGDL GPIYGFQWRH
     FGARYETSAS SYEGKGVDQI ASAIAAIRAN PASRRIVVSA WNPTDLGSMA LPPCHVLFQF
     NVTDGKLSCA MYQRSGDMGL GVPFNIASYS LLTILVAHLT GLQPGEFVHF LGDAHVYLDH
     VDSLRQQVQR PPRAFPKLFV SPKGPRTEPE HFQYEDFELV GYDPHPAIKM NMSA