ID   A0A7D7U4F8_9MOLU        Unreviewed;       289 AA.
AC   A0A7D7U4F8;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JUN-2023, entry version 12.
DE   RecName: Full=Thymidylate synthase {ECO:0000256|ARBA:ARBA00011947, ECO:0000256|HAMAP-Rule:MF_00008};
DE            Short=TS {ECO:0000256|HAMAP-Rule:MF_00008};
DE            Short=TSase {ECO:0000256|HAMAP-Rule:MF_00008};
DE            EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947, ECO:0000256|HAMAP-Rule:MF_00008};
GN   Name=thyA {ECO:0000256|HAMAP-Rule:MF_00008};
GN   ORFNames=H3143_00225 {ECO:0000313|EMBL:QMT98570.1};
OS   Mycoplasma tullyi.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1612150 {ECO:0000313|EMBL:QMT98570.1, ECO:0000313|Proteomes:UP000514704};
RN   [1] {ECO:0000313|EMBL:QMT98570.1, ECO:0000313|Proteomes:UP000514704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56A97T {ECO:0000313|EMBL:QMT98570.1,
RC   ECO:0000313|Proteomes:UP000514704};
RX   PubMed=28895509;
RA   Yavari C.A., Ramirez A.S., Nicholas R.A.J., Radford A.D., Darby A.C.,
RA   Bradbury J.M.;
RT   "Mycoplasma tullyi sp. nov., isolated from penguins of the genus
RT   Spheniscus.";
RL   Int. J. Syst. Evol. Microbiol. 67:3692-3698(2017).
CC   -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-
CC       monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while
CC       utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and
CC       reductant in the reaction, yielding dihydrofolate (DHF) as a by-
CC       product. This enzymatic reaction provides an intracellular de novo
CC       source of dTMP, an essential precursor for DNA biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00008}.
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:0000256|HAMAP-Rule:MF_00008};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00008}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type
CC       ThyA subfamily. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00008}.
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DR   EMBL; CP059674; QMT98570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7D7U4F8; -.
DR   KEGG; mtuy:H3143_00225; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000514704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
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; Thymidylate synthase/dCMP hydroxymethylase domain; 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:SF9; THYMIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00008};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_00008};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00008}.
FT   DOMAIN          2..289
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         150..151
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         191..194
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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         194
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         202
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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         232..234
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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         288
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
SQ   SEQUENCE   289 AA;  33718 MW;  3D041CDD8C82A9BE CRC64;
     MKTYLGLLEK VMTKGEVKKD RTNTGTISYF GTQGRYDLRE GFPLLTTKKM AWKSICHELL
     WFLKGDTNIK YLVDHNVNIW NEWPYEAFKK SSDYNDETLQ EFVDKIKADD QFAQVYGKLG
     PVYGKQWRNF NGVDQIEWVI NEIKNNPFSR RLIVSAWNPS EIKDMALPPC HSFFQFFVNE
     KYEISLQLYQ RSGDMFLGVP FNIASYSLLL LMVAQVTGLK PAEFVHTIGD THIYSNHVDQ
     VKIQLQREPK KLPKVSLNPD IKNIFDFKFE DISLENYEHH DPIKGKVAV
//