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Database: UniProt
Entry: A0A0L0KMJ5_9ACTN
LinkDB: A0A0L0KMJ5_9ACTN
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ID   A0A0L0KMJ5_9ACTN        Unreviewed;       265 AA.
AC   A0A0L0KMJ5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=IQ63_06160 {ECO:0000313|EMBL:KND38825.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND38825.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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: 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:KND38825.1}.
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DR   EMBL; JPPY01000038; KND38825.1; -; Genomic_DNA.
DR   RefSeq; WP_050369739.1; NZ_KQ257805.1.
DR   AlphaFoldDB; A0A0L0KMJ5; -.
DR   PATRIC; fig|42234.21.peg.1269; -.
DR   OrthoDB; 9774633at2; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000037151; 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:UP000037151};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00008}.
FT   DOMAIN          5..265
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT   ACT_SITE        148
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         23
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         53
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         128..129
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         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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00008"
FT   BINDING         264
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   265 AA;  29912 MW;  1E397C0C49D06409 CRC64;
     MADTQYEDLL RQVLTSGTAK ADRTGTGTRS VFGHQLRYDL AQGFPLVTTK KVHLKSIVYE
     LLWFLRGDSN VKWLRDNGVS IWDEWADADG ELGPVYGVQW RSWPTPDGGH IDQLTEVLDT
     LRSDPDSRRI IVSAWNVAQL SEMALAPCHA FFQFYVADGR LSCQLYQRSA DLFLGVPFNI
     ASYALLTHMV AQQTGLEPGD FIWTGGDCHI YDNHVDQVTE QLSRTPYAFP ELKLHQAEDL
     FSYTYDDVEV TGYKHHPAIK APVAV
//
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