TYSY_SCHPO
ID TYSY_SCHPO Reviewed; 625 AA.
AC Q9UTI7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable thymidylate synthase;
DE Short=TS;
DE Short=TSase;
DE EC=2.1.1.45;
GN ORFNames=SPAC15E1.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB52423.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for both nuclear and mitochondrial DNA synthesis.
CC {ECO:0000250|UniProtKB:P06785}.
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:0000250|UniProtKB:P06785};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC oligomeric flavin containing Cys decarboxylase) superfamily.
CC {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thymidylate
CC synthase family. {ECO:0000255}.
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DR EMBL; CU329670; CAB52423.1; -; Genomic_DNA.
DR PIR; T37719; T37719.
DR RefSeq; NP_594305.1; NM_001019728.2.
DR AlphaFoldDB; Q9UTI7; -.
DR SMR; Q9UTI7; -.
DR BioGRID; 279249; 8.
DR STRING; 4896.SPAC15E1.04.1; -.
DR MoonProt; Q9UTI7; -.
DR iPTMnet; Q9UTI7; -.
DR MaxQB; Q9UTI7; -.
DR PaxDb; Q9UTI7; -.
DR EnsemblFungi; SPAC15E1.04.1; SPAC15E1.04.1:pep; SPAC15E1.04.
DR GeneID; 2542801; -.
DR KEGG; spo:SPAC15E1.04; -.
DR PomBase; SPAC15E1.04; -.
DR VEuPathDB; FungiDB:SPAC15E1.04; -.
DR eggNOG; KOG0672; Eukaryota.
DR eggNOG; KOG0673; Eukaryota.
DR HOGENOM; CLU_028985_0_0_1; -.
DR InParanoid; Q9UTI7; -.
DR OMA; AEWRNIV; -.
DR PhylomeDB; Q9UTI7; -.
DR Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00575; -.
DR PRO; PR:Q9UTI7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IDA:PomBase.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IDA:PomBase.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IDA:PomBase.
DR GO; GO:0004799; F:thymidylate synthase activity; IGI:PomBase.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IC:PomBase.
DR GO; GO:0006231; P:dTMP biosynthetic process; IGI:PomBase.
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 Gene3D; 3.40.50.1950; -; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
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; PF02441; Flavoprotein; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF52507; SSF52507; 1.
DR SUPFAM; SSF55831; SSF55831; 1.
DR TIGRFAMs; TIGR03284; thym_sym; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..625
FT /note="Probable thymidylate synthase"
FT /id="PRO_0000310825"
FT REGION 224..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 350
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 477..478
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 524..527
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 527
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 535
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 565..567
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 625 AA; 69893 MW; B3BC6034BF26F61E CRC64;
MSQPLHARFA TRAVKNPMIL EKERQLTDSK YHILVAATGS VAAIKLTLIV KSLLTYKGVD
VQVVLTDPAR NFVEKEDLTA LGVNVYNNAD DWKNWDGLEC PITHIELRRW AHLLLIAPLS
ANTMAKMANG LCDNLLTSLI RAWAPLKPIL LAPAMNTLMW TNPITQEHLS AISRIYKNSE
FIMPIEKVLA CGDIGMGGMA EWRNIVGRVA DKLQLEQKSV LPNAVKNIDG QDDDSSEQTA
AFEEYDDDDD DDVDDNEQSN SMIETSANAD ITPKASLLPS TTESSISKDH ETSQAPLGSE
SVDTQASENV TTKPEPPVPF TSSEYRNTEE EQYLNLIRYI LENGQSRPDR TGTGTRSVFA
PPQLRFSLRN NTLPLLTTKR VFLRGVLEEL LWFIHGDTNA NHLSEKGIHI WDGNGSREFL
DSRGLTDRKV GDLGPIYGFQ WRHFGAQYVD CDTDYTNKGV DQLAQVISTL KLNPYDRRII
LSAWNPLAIP EMALPPCHIF CQFYVSEPCK PGGKPQLSSM MYQRSADMGL GVPFNIASYS
LLTHMIAHMC GYEAAEFVHV MGDCHIYNDH LEALQTQLER VPKAFPKLFF KRDAKDIGSI
DSFSVDDFAV EGYNPYGPIK MKMSV
