THYX_PBCV1
ID THYX_PBCV1 Reviewed; 216 AA.
AC O41156;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable flavin-dependent thymidylate synthase {ECO:0000250|UniProtKB:Q9WYT0};
DE Short=FDTS {ECO:0000250|UniProtKB:Q9WYT0};
DE EC=2.1.1.148 {ECO:0000250|UniProtKB:Q9WYT0};
DE AltName: Full=FAD-dependent thymidylate synthase {ECO:0000250|UniProtKB:Q9WYT0};
GN OrderedLocusNames=A674R;
OS Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=10506;
OH NCBI_TaxID=114055; Chlorella.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9356347; DOI=10.1006/viro.1997.8805;
RA Li Y., Lu Z., Sun L., Ropp S., Kutish G.F., Rock D.L., van Etten J.L.;
RT "Analysis of 74 kb of DNA located at the right end of the 330-kb chlorella
RT virus PBCV-1 genome.";
RL Virology 237:360-377(1997).
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,
CC and NADPH and FADH(2) as the reductant. {ECO:0000250|UniProtKB:Q9WYT0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) +
CC NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+);
CC Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148;
CC Evidence={ECO:0000250|UniProtKB:Q9WYT0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9WYT0};
CC Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC monomers. {ECO:0000250|UniProtKB:Q9WYT0};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000250|UniProtKB:Q9WYT0}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9WYT0}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC {ECO:0000305}.
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DR EMBL; JF411744; AAC96983.1; -; Genomic_DNA.
DR PIR; T18176; T18176.
DR RefSeq; NP_049030.1; NC_000852.5.
DR PDB; 2CFA; X-ray; 2.30 A; A/B=1-216.
DR PDB; 4FZB; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-216.
DR PDBsum; 2CFA; -.
DR PDBsum; 4FZB; -.
DR SMR; O41156; -.
DR BindingDB; O41156; -.
DR ChEMBL; CHEMBL1075203; -.
DR GeneID; 918188; -.
DR KEGG; vg:918188; -.
DR BRENDA; 2.1.1.148; 4540.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; O41156; -.
DR PRO; PR:O41156; -.
DR Proteomes; UP000000862; Genome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050797; F:thymidylate synthase (FAD) 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 Gene3D; 3.30.1360.170; -; 1.
DR InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR PANTHER; PTHR34934; PTHR34934; 1.
DR Pfam; PF02511; Thy1; 1.
DR SUPFAM; SSF69796; SSF69796; 1.
DR TIGRFAMs; TIGR02170; thyX; 1.
DR PROSITE; PS51331; THYX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Methyltransferase; NADP;
KW Nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..216
FT /note="Probable flavin-dependent thymidylate synthase"
FT /id="PRO_0000175603"
FT DOMAIN 1..216
FT /note="ThyX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT MOTIF 78..88
FT /note="ThyX motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT ACT_SITE 182
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 75..78
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 78..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 86..90
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:Q9WYT0"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 155
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:Q9WYT0"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 182
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:2CFA"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2CFA"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2CFA"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4FZB"
FT HELIX 126..146
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2CFA"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:2CFA"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2CFA"
SQ SEQUENCE 216 AA; 24902 MW; 633931516599A46C CRC64;
MSAKLISVTK PVVEGVNTAE ELIAYAARVS NPENQINNKT ASGLLKYCIR HKHWSIFETA
FMTLELKTSR GIAAQVLRHR SFHFQEFSQR YASVMETPPP HQARFQDHKN RQNSLDTVPE
DDQTWWATEQ EKLYAQSMEL YNKALEKGIA KECARFILPL STPTTIYMSG TIRDWIHYIE
LRTSNGTQRE HIDLANACKE IFIKEFPSIA KALDWV
