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Database: UniProt
Entry: A0A5R9EGL7_9LACT
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Original site: A0A5R9EGL7_9LACT 
ID   A0A5R9EGL7_9LACT        Unreviewed;       314 AA.
AC   A0A5R9EGL7;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=FEZ33_00855 {ECO:0000313|EMBL:TLQ49564.1};
OS   Ruoffia tabacinasalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ruoffia.
OX   NCBI_TaxID=87458 {ECO:0000313|EMBL:TLQ49564.1, ECO:0000313|Proteomes:UP000306420};
RN   [1] {ECO:0000313|EMBL:TLQ49564.1, ECO:0000313|Proteomes:UP000306420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAM 24227 {ECO:0000313|EMBL:TLQ49564.1,
RC   ECO:0000313|Proteomes:UP000306420};
RA   Roder T., Wuthrich D., Sattari Z., Von Ah U., Bar C., Ronchi F.,
RA   Macpherson A.J., Ganal-Vonarburg S.C., Bruggmann R., Vergeres G.;
RT   "The metagenome of a microbial culture collection derived from dairy
RT   environment covers the genomic content of the human microbiome.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TLQ49564.1}.
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DR   EMBL; VBSP01000001; TLQ49564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5R9EGL7; -.
DR   OrthoDB; 9774633at2; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000306420; Unassembled WGS sequence.
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   NCBIfam; TIGR03284; thym_sym; 1.
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   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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          4..314
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         22
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         177..178
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         217..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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         220
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         228
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         258..260
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         313
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   314 AA;  36176 MW;  42BC1EBCE71E31BB CRC64;
     MTTQYQDLVR KVLNEGTKKE DRTGVGTLSI FGHQMRFNLQ EGFPLLTSKR VPFGLIKSEL
     LWFLRGDTNI RYLLENNNHI WDEWAFKNYV ESDAYEGPDM TDFGRRALVD EAFKVQYDEE
     MTNFQNEILT NDDFSEEFGH LGDVYGKQWR AWQLRNGETL DQIKVVIDQI KTNPDSRRHI
     VSAWNPEDVP SMALPPCHTL FQFYVADGKL SCQLYQRSGD IFLGIPFNIA SYALITHLIA
     RETGLDVGDF VHTIGDAHIY SNHLEQAKLL LERDVRPLPQ LVIQSEAKLD EIESNEIKVE
     NYNPHPSIKA PIAV
//
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