TYSY_CRYNJ
ID TYSY_CRYNJ Reviewed; 317 AA.
AC P0CS12; P45351; Q55KW0; Q5KAL9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Thymidylate synthase;
DE Short=TS;
DE Short=TSase;
DE EC=2.1.1.45;
GN Name=TMP1; OrderedLocusNames=CNJ01230;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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; AE017350; AAW45984.1; -; Genomic_DNA.
DR RefSeq; XP_567501.1; XM_567501.1.
DR PDB; 2AAZ; X-ray; 2.08 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-317.
DR PDBsum; 2AAZ; -.
DR AlphaFoldDB; P0CS12; -.
DR SMR; P0CS12; -.
DR STRING; 5207.AAW45984; -.
DR PaxDb; P0CS12; -.
DR EnsemblFungi; AAW45984; AAW45984; CNJ01230.
DR GeneID; 3254191; -.
DR KEGG; cne:CNJ01230; -.
DR VEuPathDB; FungiDB:CNJ01230; -.
DR eggNOG; KOG0673; Eukaryota.
DR HOGENOM; CLU_021669_0_2_1; -.
DR InParanoid; P0CS12; -.
DR OMA; KQYLDLC; -.
DR OrthoDB; 684306at2759; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; P0CS12; -.
DR Proteomes; UP000002149; Chromosome 10.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004799; F:thymidylate synthase activity; IBA:GO_Central.
DR GO; GO:0006231; P:dTMP biosynthetic process; IBA:GO_Central.
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..317
FT /note="Thymidylate synthase"
FT /id="PRO_0000140910"
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"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2AAZ"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2AAZ"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:2AAZ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 245..259
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:2AAZ"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2AAZ"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2AAZ"
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
