ID A0A2X4THV8_SALER Unreviewed; 264 AA.
AC A0A2X4THV8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ECO:0000313|EMBL:SQI21232.1};
GN ORFNames=AHX45_11255 {ECO:0000313|EMBL:EDH0570745.1}, DSQ81_20855
GN {ECO:0000313|EMBL:ECI4938081.1}, F4V61_18440
GN {ECO:0000313|EMBL:KAA8662252.1}, GBZ58_18115
GN {ECO:0000313|EMBL:HAB4462413.1}, NCTC7295_00996
GN {ECO:0000313|EMBL:SUG13421.1}, NCTC7303_03431
GN {ECO:0000313|EMBL:SUG51107.1}, NCTC7304_01060
GN {ECO:0000313|EMBL:SUG31667.1}, NCTC7307_01049
GN {ECO:0000313|EMBL:SQI21232.1}, NCTC8297_01184
GN {ECO:0000313|EMBL:SUG45983.1};
OS Salmonella enterica subsp. arizonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=59203 {ECO:0000313|EMBL:SQI21232.1, ECO:0000313|Proteomes:UP000248731};
RN [1] {ECO:0000313|EMBL:HAB4462413.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Salmonella enterica {ECO:0000313|EMBL:HAB4462413.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [2] {ECO:0000313|Proteomes:UP000248731, ECO:0000313|Proteomes:UP000254124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7295 {ECO:0000313|EMBL:SUG13421.1,
RC ECO:0000313|Proteomes:UP000254124}, NCTC7303
RC {ECO:0000313|EMBL:SUG51107.1, ECO:0000313|Proteomes:UP000255443},
RC NCTC7304 {ECO:0000313|EMBL:SUG31667.1,
RC ECO:0000313|Proteomes:UP000254762}, NCTC7307
RC {ECO:0000313|EMBL:SQI21232.1, ECO:0000313|Proteomes:UP000248731}, and
RC NCTC8297 {ECO:0000313|EMBL:SUG45983.1,
RC ECO:0000313|Proteomes:UP000254741};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EDH0570745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDA00001204 {ECO:0000313|EMBL:EDH0570745.1};
RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ECI4938081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=475813 {ECO:0000313|EMBL:ECI4938081.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:KAA8662252.1, ECO:0000313|Proteomes:UP000322837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 6322T {ECO:0000313|EMBL:KAA8662252.1,
RC ECO:0000313|Proteomes:UP000322837};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:HAB4462413.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Salmonella enterica {ECO:0000313|EMBL:HAB4462413.1};
RG NCBI Pathogen Detection Project;
RL Submitted (OCT-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}.
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DR EMBL; AAIVIG010000042; ECI4938081.1; -; Genomic_DNA.
DR EMBL; AAMGFJ010000011; EDH0570745.1; -; Genomic_DNA.
DR EMBL; DAAGTC010000013; HAB4462413.1; -; Genomic_DNA.
DR EMBL; VXJW01000012; KAA8662252.1; -; Genomic_DNA.
DR EMBL; LS483466; SQI21232.1; -; Genomic_DNA.
DR EMBL; UGWZ01000001; SUG13421.1; -; Genomic_DNA.
DR EMBL; UGXD01000002; SUG31667.1; -; Genomic_DNA.
DR EMBL; UGXG01000002; SUG45983.1; -; Genomic_DNA.
DR EMBL; UGXC01000003; SUG51107.1; -; Genomic_DNA.
DR RefSeq; WP_000816224.1; NZ_VXJW01000012.1.
DR AlphaFoldDB; A0A2X4THV8; -.
DR SMR; A0A2X4THV8; -.
DR OMA; IVYELLW; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000248731; Chromosome 1.
DR Proteomes; UP000254124; Unassembled WGS sequence.
DR Proteomes; UP000254741; Unassembled WGS sequence.
DR Proteomes; UP000254762; Unassembled WGS sequence.
DR Proteomes; UP000255443; Unassembled WGS sequence.
DR Proteomes; UP000322837; Unassembled WGS sequence.
DR Proteomes; UP000839688; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000248731};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00008}.
FT DOMAIN 2..264
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT ACT_SITE 146
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 51
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 126..127
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 166..169
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 169
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 177
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 207..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 263
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 264 AA; 30479 MW; 02A48B6B8CF7F345 CRC64;
MKQYLELMKK VLDEGTQKND RTGTGTLSIF GHQMRFNLQE GFPLVTTKRC HLRSIIHELL
WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA WPTPDGHHID QITTVLSQLK
NDPDSRRIIV SAWNVGELDK MALAPCHAFF QFYVADRKLS CQLYQRSCDV FLGLPFNIAS
YALLVHMMAQ QCDLEAGDFI WTGGDTHLYS NHMEQTHLQL SREPRALPKL VIKRKPDSLF
DYRFDDFEIE GYDPHPGIKA PVAI
//
