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TYSY_BPPHT
ID   TYSY_BPPHT              Reviewed;         279 AA.
AC   P07606;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Thymidylate synthase;
DE            Short=TS;
DE            Short=TSase;
DE            EC=2.1.1.45;
GN   Name=thyP3;
OS   Bacillus phage phi3T (Bacteriophage phi-3T).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Spbetavirus; unclassified Spbetavirus.
OX   NCBI_TaxID=10736;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3924741; DOI=10.1016/0378-1119(85)90142-8;
RA   Kenny E., Atkinson T., Hartley B.S.;
RT   "Nucleotide sequence of the thymidylate synthetase gene (thyP3) from the
RT   Bacillus subtilis phage phi 3T.";
RL   Gene 34:335-342(1985).
CC   -!- FUNCTION: Provides the sole de novo source of dTMP for DNA
CC       biosynthesis.
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; M10122; AAA32353.1; -; Genomic_DNA.
DR   PIR; A22800; SYBP3T.
DR   SMR; P07606; -.
DR   UniPathway; UPA00575; -.
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; Transferase.
FT   CHAIN           1..279
FT                   /note="Thymidylate synthase"
FT                   /id="PRO_0000141060"
FT   ACT_SITE        161
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
FT   BINDING         141..142
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         181..184
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         184
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         192
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         222..224
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         278
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT                   /evidence="ECO:0000250|UniProtKB:P0A884"
SQ   SEQUENCE   279 AA;  32785 MW;  F8FC67BD2DF7A727 CRC64;
     MTQFDKQYNS IIKDIINNGI SDEEFDVRTK WDSDGTPAHT LSVMSKQMRF DNSEVPILTT
     KKVAWKTAIK ELLWIWQLKS NDVTELNKMG VHIWDQWKQE DGTIGHAYGF QLGKKNRSLN
     GEKVDQVDYL LHQLKNNPSS RRHITMLWNP DDLDAMALTP CVYETQWYVK QGKLHLEVRA
     RSNDMALGNP FNVFQYNVLQ RMIAQVTGYE LGEYIFNIGD CHVYTRHIDN LKIQMEREQF
     EAPELWINPE VKDFYNFTVD DFKLINYKHG DKLLFEVAV
 
 
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