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Database: UniProt
Entry: V5RWE8_9BACT
LinkDB: V5RWE8_9BACT
Original site: V5RWE8_9BACT 
ID   V5RWE8_9BACT            Unreviewed;       306 AA.
AC   V5RWE8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
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=RAAC3_TM7C00001G0731 {ECO:0000313|EMBL:AHB42572.1};
OS   Candidatus Saccharibacteria bacterium RAAC3_TM7_1.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=1394711 {ECO:0000313|EMBL:AHB42572.1, ECO:0000313|Proteomes:UP000018523};
RN   [1] {ECO:0000313|EMBL:AHB42572.1, ECO:0000313|Proteomes:UP000018523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAAC3_TM7_1 {ECO:0000313|EMBL:AHB42572.1,
RC   ECO:0000313|Proteomes:UP000018523};
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT   four candidate phyla.";
RL   Submitted (NOV-2013) 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}.
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DR   EMBL; CP006915; AHB42572.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5RWE8; -.
DR   STRING; 1394711.RAAC3_TM7C00001G0731; -.
DR   KEGG; sbe:RAAC3_TM7C01G0731; -.
DR   PATRIC; fig|1394711.4.peg.659; -.
DR   HOGENOM; CLU_021669_0_2_0; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000018523; 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   NCBIfam; TIGR03284; thym_sym; 1.
DR   PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR   PANTHER; PTHR11548:SF1; 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|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}; Reference proteome {ECO:0000313|Proteomes:UP000018523};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00008}.
FT   DOMAIN          2..306
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT   ACT_SITE        188
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         164..165
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         208..211
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         211
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         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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         249..251
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         305
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   306 AA;  34897 MW;  FBA3FA874BADB238 CRC64;
     MRQYLDLLRD IKENGVIKSD RTGTGTKSVF GRQVRYDLAD GFPAVTTKKL YFNSVVHELL
     WFLKGTGNIE YLAQNNVHIW DEWPFKAYLE KNNLPIPEVN SDEWKAQMKV FIGKVATDHD
     FATKWGDLGP VYGVQWRHWP DGRGGEIDQI ANVIEMIKKS PDSRRMIVTA WNPGEIDEIV
     RIGGLPPCHS LFQFYVADGK LSLHLYQRSA DTFLGVPFNI ASYSLLLAMV AQVTGLEAGE
     FVHTLADTHI YSNHFEQVNE QLARTPKELP TLWLNPDVKN IDVFTFDDIR LENYYPDPAI
     KAPIAV
//
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