TYSY_BRAHW
ID TYSY_BRAHW Reviewed; 266 AA.
AC C0QWM9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_00008};
DE Short=TS {ECO:0000255|HAMAP-Rule:MF_00008};
DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_00008};
DE EC=2.1.1.45 {ECO:0000255|HAMAP-Rule:MF_00008};
GN Name=thyA {ECO:0000255|HAMAP-Rule:MF_00008}; OrderedLocusNames=BHWA1_00171;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_00008};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00008}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type
CC ThyA subfamily. {ECO:0000255|HAMAP-Rule:MF_00008}.
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DR EMBL; CP001357; ACN82671.1; -; Genomic_DNA.
DR RefSeq; WP_012669724.1; NC_012225.1.
DR AlphaFoldDB; C0QWM9; -.
DR SMR; C0QWM9; -.
DR STRING; 565034.BHWA1_00171; -.
DR EnsemblBacteria; ACN82671; ACN82671; BHWA1_00171.
DR GeneID; 63963964; -.
DR KEGG; bhy:BHWA1_00171; -.
DR eggNOG; COG0207; Bacteria.
DR HOGENOM; CLU_021669_0_0_12; -.
DR OMA; KQYLDLC; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000001803; 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; -; 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 PANTHER; PTHR11548; PTHR11548; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; SSF55831; 1.
DR TIGRFAMs; TIGR03284; thym_sym; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleotide biosynthesis; Transferase.
FT CHAIN 1..266
FT /note="Thymidylate synthase"
FT /id="PRO_1000197233"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00008"
FT BINDING 127..128
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00008"
FT BINDING 168..171
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:0000255|HAMAP-Rule:MF_00008"
FT BINDING 171
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00008"
FT BINDING 179
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:0000255|HAMAP-Rule:MF_00008"
FT BINDING 209..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:0000255|HAMAP-Rule:MF_00008"
FT BINDING 265
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00008"
SQ SEQUENCE 266 AA; 30799 MW; 73D9BCC21F8D76C5 CRC64;
MQNYLDLLKK VLEEGEETKD RTGVGTRRIF GPQLRFKFEG NKIPIITTKR VFMKGVIIEL
LWFLQGSTNI KFLLENNVHI WDEWADDMGE LGPVYGKQWR AWETKEGNKI DQISNIVNTL
RNNPASRRII LNAWNVGEID QMHLPPCHMM CQFSVNSKGG IITHLYQRSA DLFLGVPFNI
SSYAILTRLL AMHSGLHASE LIMTFGDAHI YNNHIEQVKL QLSREPLEQT TELFIDNRPN
IFSHVYEDFK LEGYKYYPTI KAEVAV
