TYSY_CORGL
ID TYSY_CORGL Reviewed; 266 AA.
AC Q8NS38;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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};
GN OrderedLocusNames=Cgl0844, cg0966;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB98237.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19550.1; -; Genomic_DNA.
DR RefSeq; NP_600073.1; NC_003450.3.
DR RefSeq; WP_003862391.1; NC_006958.1.
DR PDB; 4H0R; X-ray; 2.30 A; A/B=1-266.
DR PDB; 4H0U; X-ray; 2.75 A; A/B/C/D=1-266.
DR PDBsum; 4H0R; -.
DR PDBsum; 4H0U; -.
DR AlphaFoldDB; Q8NS38; -.
DR SMR; Q8NS38; -.
DR STRING; 196627.cg0966; -.
DR KEGG; cgb:cg0966; -.
DR KEGG; cgl:Cgl0844; -.
DR PATRIC; fig|196627.13.peg.828; -.
DR eggNOG; COG0207; Bacteria.
DR HOGENOM; CLU_021669_0_0_11; -.
DR OMA; KQYLDLC; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000000582; 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; 2.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..266
FT /note="Thymidylate synthase"
FT /id="PRO_0000140952"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00008"
FT BINDING 24
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 54
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 129..130
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 169..172
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 172
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 180
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 210..212
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"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4H0U"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:4H0R"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4H0R"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:4H0R"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 198..212
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4H0R"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4H0R"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4H0R"
SQ SEQUENCE 266 AA; 30230 MW; E63BA3445460DF09 CRC64;
MTVPTPYEDL LRKIAEEGSH KDDRTGTGTT SLFGQQIRFD LNEGFPLLTT KKVHFHSVVG
ELLWFLQGDS NVKWLQDNNI RIWNEWADED GELGPVYGVQ WRSWPTPDGR HIDQISGALE
TLRNNPDSRR NIVSAWNVSE LENMALPPCH LLFQLYVADG KLSCQLYQRS ADMFLGVPFN
IASYALLTHM FAQQAGLEVG EFIWTGGDCH IYDNHKEQVA EQLSREARPY PTLELNKAAS
MFEYSFDDIT VSGYDPHPLI RGKVAV
