ID A0A0K8P2H2_IDESA Unreviewed; 296 AA.
AC A0A0K8P2H2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ISF6_2712 {ECO:0000313|EMBL:GAP36872.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP36872.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP36872.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
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: 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:GAP36872.1}.
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DR EMBL; BBYR01000039; GAP36872.1; -; Genomic_DNA.
DR RefSeq; WP_054020830.1; NZ_BBYR01000039.1.
DR AlphaFoldDB; A0A0K8P2H2; -.
DR STRING; 1547922.ISF6_2712; -.
DR OrthoDB; 9774633at2; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000037660; 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; 2.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR PANTHER; PTHR11548:SF1; THYMIDYLATE SYNTHASE-RELATED; 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:UP000037660};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00008}.
FT DOMAIN 28..296
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 46
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 76
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 151..152
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 198..201
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 201
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 209
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 239..241
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 295
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 296 AA; 32971 MW; C7117ACC22300670 CRC64;
MSSVLVPPSS PAAADPSPAL PPRPVRRQYE DFASHVITHG VSKGDRTGTG TTSVFGYQMR
FDLREGFPLV TTKKVHLKSV VLELLWFLRG DGNARWLQER GVTIWDEWAA PNGDLGPVYG
VQWRSWPTPD GGHVDQIADV IRTLRSNPDS RRIVVSAWNV AALPQMALMP CHAFFQFYVA
PAEAPGGRGR LSCQLYQRSA DVFLGVPFNI ASYALLTHLV AAQCDLDVGE FIWTGGDCHV
YDNHREQIAL QLSREPLPYP VLQLKRQPAS IFDYAYEDIE VLDYRHHPPI KGAVAV
//
