TYSY_VZVO
ID TYSY_VZVO Reviewed; 301 AA.
AC Q4JQW2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Thymidylate synthase;
DE Short=TS;
DE Short=TSase;
DE EC=2.1.1.45;
GN ORFNames=ORF13;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
CC -!- FUNCTION: Catalyzes the reductive methylation of deoxyuridylate to
CC thymidylate. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57630.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57701.1; -; Genomic_DNA.
DR RefSeq; NP_040136.1; NC_001348.1.
DR PDB; 4XSC; X-ray; 2.90 A; A/B/C/D=8-295.
DR PDB; 4XSD; X-ray; 2.90 A; A/B/C/D=8-295.
DR PDB; 4XSE; X-ray; 3.10 A; A/B/C/D=8-295.
DR PDBsum; 4XSC; -.
DR PDBsum; 4XSD; -.
DR PDBsum; 4XSE; -.
DR SMR; Q4JQW2; -.
DR IntAct; Q4JQW2; 2.
DR DNASU; 1487659; -.
DR GeneID; 1487659; -.
DR KEGG; vg:1487659; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; 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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleotide biosynthesis; Transferase.
FT CHAIN 1..301
FT /note="Thymidylate synthase"
FT /id="PRO_0000385165"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 38
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 163..164
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 203..206
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 206
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 214
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 244..246
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 300
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4XSE"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4XSD"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4XSD"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4XSD"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4XSC"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4XSD"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 195..206
FT /evidence="ECO:0007829|PDB:4XSD"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 210..228
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 232..246
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4XSD"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4XSD"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:4XSD"
SQ SEQUENCE 301 AA; 34533 MW; 8B84C36E79F95861 CRC64;
MGDLSCWTKV PGFTLTGELQ YLKQVDDILR YGVRKRDRTG IGTLSLFGMQ ARYNLRNEFP
LLTTKRVFWR AVVEELLWFI RGSTDSKELA AKDIHIWDIY GSSKFLNRNG FHKRHTGDLG
PIYGFQWRHF GAEYKDCQSN YLQQGIDQLQ TVIDTIKTNP ESRRMIISSW NPKDIPLMVL
PPCHTLCQFY VANGELSCQV YQRSGDMGLG VPFNIAGYAL LTYIVAHVTG LKTGDLIHTM
GDAHIYLNHI DALKVQLARS PKPFPCLKII RNVTDINDFK WDDFQLDGYN PHPPLKMEMA
L
