ID A0A0A1HTB8_9PSED Unreviewed; 323 AA.
AC A0A0A1HTB8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=BN844_4625 {ECO:0000313|EMBL:CDF93713.1};
OS Pseudomonas sp. SHC52.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF93713.1, ECO:0000313|Proteomes:UP000031550};
RN [1] {ECO:0000313|EMBL:CDF93713.1, ECO:0000313|Proteomes:UP000031550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF93713.1,
RC ECO:0000313|Proteomes:UP000031550};
RA Van der Voort M., Mendes R., Raaijmakers J.M.;
RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL Submitted (MAY-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}.
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:CDF93713.1}.
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DR EMBL; CBLV010000135; CDF93713.1; -; Genomic_DNA.
DR RefSeq; WP_041021509.1; NZ_CBLV010000135.1.
DR AlphaFoldDB; A0A0A1HTB8; -.
DR OrthoDB; 9774633at2; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000031550; 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 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.
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}; Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00008};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00008}.
FT DOMAIN 2..323
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT ACT_SITE 192
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 172..173
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 214..217
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 217
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 225
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 255..257
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 322
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 323 AA; 36587 MW; 4C15B4DD4384D752 CRC64;
MKQYLDLVAH VIKNGTKQAN RTGVNTISFP GAMLRYDLKD GFPAITTRKM AFKSAIGEMC
GFLRGVNNAA EFRALGCKVW DQNANENSQW LANPFRQGED DLGEIYGVQW RKWPAYKQIP
VSNPAAIEQT LAQGYRQIAE GEENGQAYVV LYKAIDQVRQ CVDTIIKDPG SRRILFHGWN
CAQLDEMALP PCHLLYQFHP NVETKEISLT LYIRSNDLGL GTPFNLTEGA ALLSLIGRLT
GYTPRWFTYF IGDAHVYENH LDMLKEQLTR EPFPMPRLVI SERVPEFAKT GVYQPEWLEL
VEPGDFSLEG YQHHAPMTAP MAV
//
