TYSY_BPT4
ID TYSY_BPT4 Reviewed; 286 AA.
AC P00471;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Thymidylate synthase;
DE Short=TS;
DE Short=TSase;
DE EC=2.1.1.45;
GN Name=TD;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6328492; DOI=10.1073/pnas.81.10.3049;
RA Chu F.K., Maley G.F., Maley F., Belfort M.;
RT "Intervening sequence in the thymidylate synthase gene of bacteriophage
RT T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3049-3053(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RX PubMed=6327673; DOI=10.1016/s0021-9258(20)82135-8;
RA Purohit S., Mathews C.K.;
RT "Nucleotide sequence reveals overlap between T4 phage genes encoding
RT dihydrofolate reductase and thymidylate synthase.";
RL J. Biol. Chem. 259:6261-6266(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-188.
RX PubMed=3698096; DOI=10.1016/0092-8674(86)90379-x;
RA Chu F.K., Maley G.F., West D.K., Belfort M., Maley F.;
RT "Characterization of the intron in the phage T4 thymidylate synthase gene
RT and evidence for its self-excision from the primary transcript.";
RL Cell 45:157-166(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-286.
RX PubMed=2846540; DOI=10.1016/s0021-9258(18)37585-9;
RA Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R.;
RT "Total sequence, flanking regions, and transcripts of bacteriophage T4 nrdA
RT gene, coding for alpha chain of ribonucleoside diphosphate reductase.";
RL J. Biol. Chem. 263:16242-16251(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX PubMed=7803410; DOI=10.1021/bi00255a028;
RA Finer-Moore J.S., Maley G.F., Maley F., Montfort W.R., Stroud R.M.;
RT "Crystal structure of thymidylate synthase from T4 phage: component of a
RT deoxynucleoside triphosphate-synthesizing complex.";
RL Biochemistry 33:15459-15468(1994).
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 -!- MISCELLANEOUS: This enzyme is also expressed by the thyA gene of
CC E.coli; the phage and host synthases exhibit striking dissimilarities
CC in both structure and function.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; K02035; AAA32492.1; -; Genomic_DNA.
DR EMBL; K01804; AAA32492.1; JOINED; Genomic_DNA.
DR EMBL; AF158101; AAD42662.1; -; Genomic_DNA.
DR EMBL; M12742; AAC12816.1; -; Genomic_DNA.
DR EMBL; J03968; AAA32525.1; -; Genomic_DNA.
DR PIR; A00550; SYBPT4.
DR RefSeq; NP_049848.1; NC_000866.4.
DR PDB; 1TIS; X-ray; 2.70 A; A=1-286.
DR PDBsum; 1TIS; -.
DR SMR; P00471; -.
DR GeneID; 1258770; -.
DR KEGG; vg:1258770; -.
DR SABIO-RK; P00471; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; P00471; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004799; F:thymidylate synthase activity; IMP:CACAO.
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;
KW Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Thymidylate synthase"
FT /id="PRO_0000141061"
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 176..179
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 179
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 187
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 217..219
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 285
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 3..12
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1TIS"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 166..179
FT /evidence="ECO:0007829|PDB:1TIS"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 184..202
FT /evidence="ECO:0007829|PDB:1TIS"
FT STRAND 205..221
FT /evidence="ECO:0007829|PDB:1TIS"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:1TIS"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1TIS"
SQ SEQUENCE 286 AA; 33073 MW; 9F60863145F5219D CRC64;
MKQYQDLIKD IFENGYETDD RTGTGTIALF GSKLRWDLTK GFPAVTTKKL AWKACIAELI
WFLSGSTNVN DLRLIQHDSL IQGKTVWDEN YENQAKDLGY HSGELGPIYG KQWRDFGGVD
QIIEVIDRIK KLPNDRRQIV SAWNPAELKY MALPPCHMFY QFNVRNGYLD LQWYQRSVDV
FLGLPFNIAS YATLVHIVAK MCNLIPGDLI FSGGNTHIYM NHVEQCKEIL RREPKELCEL
VISGLPYKFR YLSTKEQLKY VLKLRPKDFV LNNYVSHPPI KGKMAV
