ID TYSY_SHV21 Reviewed; 294 AA. AC P06854; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 24-JAN-2024, entry version 112. DE RecName: Full=Thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.45; GN Name=70; Synonyms=ECLF4; OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Rhadinovirus; OC Rhadinovirus saimiriinegamma2; Saimiriine herpesvirus 2. OX NCBI_TaxID=10383; OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3012520; DOI=10.1073/pnas.83.11.3604; RA Honess R.W., Bodemer W., Cameron K.R., Niller H.H., Fleckenstein B., RA Randall R.E.; RT "The A+T-rich genome of Herpesvirus saimiri contains a highly conserved RT gene for thymidylate synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3604-3608(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3018278; DOI=10.1128/jvi.60.1.114-123.1986; RA Bodemer W., Niller H.H., Nitsche N., Scholz B., Fleckenstein B.; RT "Organization of the thymidylate synthase gene of herpesvirus saimiri."; RL J. Virol. 60:114-123(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992; RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B., RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B., RA Honess R.W.; RT "Primary structure of the herpesvirus saimiri genome."; RL J. Virol. 66:5047-5058(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i; RA Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.; RT "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus RT saimiri (HVS) L-DNA: general conservation of genetic organization between RT HVS and Epstein-Barr virus."; RL Virology 188:296-310(1992). 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; X64346; CAA45693.1; -; Genomic_DNA. DR EMBL; M14080; AAA46174.1; -; Genomic_DNA. DR EMBL; M13190; AAA46175.1; -; Genomic_DNA. DR EMBL; M86409; AAA46146.1; -; Genomic_DNA. DR RefSeq; NP_040272.1; NC_001350.1. DR SMR; P06854; -. DR GeneID; 1682482; -. DR KEGG; vg:1682482; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000587; Segment. 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: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; Nucleotide biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1..294 FT /note="Thymidylate synthase" FT /id="PRO_0000141063" FT ACT_SITE 176 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P0A884" FT BINDING 31 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 156..157 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 196..199 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 199 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 207 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 237..239 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 293 FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:15636" FT /evidence="ECO:0000250|UniProtKB:P0A884" FT CONFLICT 226 FT /note="P -> L (in Ref. 2; AAA46174)" FT /evidence="ECO:0000305" SQ SEQUENCE 294 AA; 33497 MW; CC583E13AC0A0930 CRC64; MSTHTEEQHG EHQYLSQVQH ILNYGSFKND RTGTGTLSIF GTQSRFSLEN EFPLLTTKRV FWRGVVEELL WFIRGSTDSK ELSAAGVHIW DANGSRSFLD KLGFYDRDEG DLGPVYGFQW RHFGAEYKGV GRDYKGEGVD QLKQLIDTIK TNPTDRRMLM CAWNVSDIPK MVLPPCHVLS QFYVCDGKLS CQLYQRSADM GLGVPFNIAS YSLLTCMIAH VTNLVPGEFI HTIGDAHIYV DHIDALKMQL TRTPRPFPTL RFARNVSCID DFKADDIILE NYNPHPIIKM HMAV //