ID TYSY_BPPHT Reviewed; 279 AA. AC P07606; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.45; GN Name=thyP3; OS Bacillus phage phi3T (Bacteriophage phi-3T). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Spbetavirus. OX NCBI_TaxID=10736; OH NCBI_TaxID=1423; Bacillus subtilis. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3924741; DOI=10.1016/0378-1119(85)90142-8; RA Kenny E., Atkinson T., Hartley B.S.; RT "Nucleotide sequence of the thymidylate synthetase gene (thyP3) from the RT Bacillus subtilis phage phi 3T."; RL Gene 34:335-342(1985). CC -!- FUNCTION: Provides the sole de novo source of dTMP for DNA CC biosynthesis. 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 -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}. 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; M10122; AAA32353.1; -; Genomic_DNA. DR PIR; A22800; SYBP3T. DR SMR; P07606; -. DR UniPathway; UPA00575; -. 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; 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; 1. DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1. DR PANTHER; PTHR11548:SF1; THYMIDYLATE SYNTHASE-RELATED; 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; Nucleotide biosynthesis; Transferase. FT CHAIN 1..279 FT /note="Thymidylate synthase" FT /id="PRO_0000141060" FT ACT_SITE 161 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P0A884" FT BINDING 141..142 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 181..184 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 184 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 192 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 222..224 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 278 FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:15636" FT /evidence="ECO:0000250|UniProtKB:P0A884" SQ SEQUENCE 279 AA; 32785 MW; F8FC67BD2DF7A727 CRC64; MTQFDKQYNS IIKDIINNGI SDEEFDVRTK WDSDGTPAHT LSVMSKQMRF DNSEVPILTT KKVAWKTAIK ELLWIWQLKS NDVTELNKMG VHIWDQWKQE DGTIGHAYGF QLGKKNRSLN GEKVDQVDYL LHQLKNNPSS RRHITMLWNP DDLDAMALTP CVYETQWYVK QGKLHLEVRA RSNDMALGNP FNVFQYNVLQ RMIAQVTGYE LGEYIFNIGD CHVYTRHIDN LKIQMEREQF EAPELWINPE VKDFYNFTVD DFKLINYKHG DKLLFEVAV //