ID TYSY_CRYNB Reviewed; 317 AA. AC P0CS13; P45351; Q55KW0; Q5KAL9; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 24-JAN-2024, entry version 57. DE RecName: Full=Thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.45; GN Name=TMP1; OrderedLocusNames=CNBJ2230; OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OS (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=283643; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B-3501; RX PubMed=7821787; DOI=10.1016/0378-1119(94)90430-8; RA Livi L.L., Edman U., Schneider G.P., Greene P.J., Santi D.V.; RT "Cloning, expression and characterization of thymidylate synthase from RT Cryptococcus neoformans."; RL Gene 150:221-226(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U12256; AAC48931.1; -; Genomic_DNA. DR EMBL; AAEY01000050; EAL18300.1; -; Genomic_DNA. DR RefSeq; XP_772947.1; XM_767854.1. DR AlphaFoldDB; P0CS13; -. DR SMR; P0CS13; -. DR BindingDB; P0CS13; -. DR ChEMBL; CHEMBL4665; -. DR DrugCentral; P0CS13; -. DR EnsemblFungi; AAW45984; AAW45984; CNJ01230. DR GeneID; 4938566; -. DR KEGG; cnb:CNBJ2230; -. DR VEuPathDB; FungiDB:CNBJ2230; -. DR HOGENOM; CLU_021669_0_2_1; -. DR OrthoDB; 1118873at2759; -. DR BRENDA; 2.1.1.45; 1723. DR UniPathway; UPA00575; -. DR PRO; PR:P0CS13; -. 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; 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; 1. DR PANTHER; PTHR11548:SF2; 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 Methyltransferase; Nucleotide biosynthesis; Transferase. FT CHAIN 1..317 FT /note="Thymidylate synthase" FT /id="PRO_0000410319" FT ACT_SITE 187 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P0A884" FT BINDING 40 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 167..168 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 216..219 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 219 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 227 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 257..259 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" SQ SEQUENCE 317 AA; 35866 MW; E6322588CE1B50B2 CRC64; MTATIDDQEK NQRSNPDHEE YQYLDLIRRI INVGEVRPDR TGTGTVALFA PPSFRFSLAD NTLPLLTTKR VFLRGVIAEL LWFVSGCTDA KMLSSQGVGI WDGNGSKEFL EKVGLGHRRE GDLGPVYGFQ WRHFGAEYTD ADGDYKGKGV DQLQRVIDTI KNNPTDRRII LSAWNPKDLP LMALPPCHMF CQFFVSLPPA DSPGSKPKLS CLMYQRSCDL GLGVPFNIAS YALLTHMIAL ITDTEPHEFI LQMGDAHVYR DHVEPLKTQL EREPRDFPKL KWARSKEEIG DIDGFKVEDF VVEGYKPWGK IDMKMSA //