THY_BPT5
ID THY_BPT5 Reviewed; 279 AA.
AC Q6QGJ5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable thymidylate synthase {ECO:0000303|PubMed:3973984};
DE EC=2.1.1.45 {ECO:0000269|PubMed:3973984};
GN Name=thy {ECO:0000312|EMBL:AAS77138.1};
GN Synonyms=thyA {ECO:0000312|EMBL:AAU05229.1};
GN ORFNames=T5.092 {ECO:0000312|EMBL:AAS77138.1},
GN T5p090 {ECO:0000312|EMBL:AAU05229.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12024.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3973984; DOI=10.1128/jvi.54.1.86-91.1985;
RA Swart W.J. Jr., Warner H.R.;
RT "Isolation and partial characterization of a bacteriophage T5 mutant unable
RT to induce thymidylate synthetase and its use in studying the effect of
RT uracil incorporation into DNA on early gene expression.";
RL J. Virol. 54:86-91(1985).
CC -!- FUNCTION: Sythesizes the thymine necessary for the viral DNA
CC replication. {ECO:0000269|PubMed:3973984}.
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; Evidence={ECO:0000269|PubMed:3973984};
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305|PubMed:15661140}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; AY543070; AAS77138.1; -; Genomic_DNA.
DR EMBL; AY692264; AAU05229.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12024.1; -; Genomic_DNA.
DR RefSeq; YP_006920.1; NC_005859.1.
DR SMR; Q6QGJ5; -.
DR GeneID; 2777594; -.
DR KEGG; vg:2777594; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0004799; F:thymidylate synthase activity; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; 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 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.
PE 1: Evidence at protein level;
KW DNA replication; Early protein; Methyltransferase; Reference proteome;
KW Transferase; Viral DNA replication.
FT CHAIN 1..279
FT /note="Probable thymidylate synthase"
FT /id="PRO_0000435562"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 21
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 136..137
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 177..180
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 180
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 188
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 218..220
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 279 AA; 31919 MW; 7FC80AE8D79A55A9 CRC64;
MQQYLKILTD VILLGEPRND RTGTGTVSIF DSYAKFDLRE GFPAVTTKRL AWKSVVGELL
WFLSGSTNLH DLRVFTFGRD EGQWTIWTPN YEDQAISMGY DKGNLGPVYG KQWRNFGGRD
QILELIEGLK NNPHGRRHLV SAWNVAELDK MALPPCHYGF QCYVSNDGYL DLKWTQRSVD
CFLGLPFNIA SYALLTHILA KLTGLKPRYL IFSGGDTHIY NDHMEQVEEQ VKRKPRPLPT
LVMPEFVDLY DLLENNTAAW SFHLEGYDPH PALKAKMSS
