TYS1_ENCCU
ID TYS1_ENCCU Reviewed; 294 AA.
AC O62584; Q8SQI4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Thymidylate synthase 1/2;
DE Short=TS 1/2;
DE Short=TSase 1/2;
DE EC=2.1.1.45;
GN Name=TS-1; OrderedLocusNames=ECU01_0180;
GN and
GN Name=TS-2; OrderedLocusNames=ECU01_1430;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11013707; DOI=10.1089/omi.1.1998.3.1;
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "First report on the systematic sequencing of the small genome of
RT Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3
RT kbp region on chromosome I.";
RL Microb. Comp. Genomics 3:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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;
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; AJ005644; CAA06648.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24888.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD25016.1; -; Genomic_DNA.
DR RefSeq; XP_965853.1; XM_960760.1.
DR RefSeq; XP_965981.1; XM_960888.1.
DR PDB; 3KGB; X-ray; 2.20 A; A=1-294.
DR PDBsum; 3KGB; -.
DR AlphaFoldDB; O62584; -.
DR SMR; O62584; -.
DR STRING; 284813.O62584; -.
DR GeneID; 860190; -.
DR GeneID; 860191; -.
DR KEGG; ecu:ECU01_0180; -.
DR KEGG; ecu:ECU01_1430; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0180; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1430; -.
DR HOGENOM; CLU_021669_0_2_1; -.
DR InParanoid; O62584; -.
DR OMA; KQYLDLC; -.
DR OrthoDB; 1197342at2759; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; O62584; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="Thymidylate synthase 1/2"
FT /id="PRO_0000140906"
FT ACT_SITE 174
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 29
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:0000250|UniProtKB:P0A884"
FT BINDING 154..155
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 194..197
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:0000250|UniProtKB:P0A884"
FT BINDING 197
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 205
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:0000250|UniProtKB:P0A884"
FT BINDING 235..237
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:0000250|UniProtKB:P0A884"
FT CONFLICT 34
FT /note="T -> A (in Ref. 2; CAA06648)"
FT /evidence="ECO:0000305"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3KGB"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:3KGB"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 201..219
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3KGB"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3KGB"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3KGB"
SQ SEQUENCE 294 AA; 33112 MW; 5FF3C707E86C0C56 CRC64;
MPQDPRHPEH QYLDLVKHIL ENGARRMDRT GTGTLSVFGA TMRFSLEDNT FPLLTTRRVF
YRGVVEELLF FLRGETDSKV LEKKGVRIWE KNGAKQFLQS VGIDREEGDL GPIYGFQWRH
FGARYETSAS SYEGKGVDQI ASAIAAIRAN PASRRIVVSA WNPTDLGSMA LPPCHVLFQF
NVTDGKLSCA MYQRSGDMGL GVPFNIASYS LLTILVAHLT GLQPGEFVHF LGDAHVYLDH
VDSLRQQIQR PPRAFPKLFV SPKGPRTEPE HFQYEDFELV GYDPHPAIKM NMSA
