TYSY_SHV21
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 03-AUG-2022, entry version 107.
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; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
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}.
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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; Genome.
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"
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
