THYX_BPMD2
ID THYX_BPMD2 Reviewed; 235 AA.
AC O64238;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
DE AltName: Full=Gp48;
GN Name=48;
OS Mycobacterium phage D29 (Mycobacteriophage D29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Fromanvirus.
OX NCBI_TaxID=28369;
OH NCBI_TaxID=1763; Mycobacterium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT "Genome structure of mycobacteriophage D29: implications for phage
RT evolution.";
RL J. Mol. Biol. 279:143-164(1998).
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; AF022214; AAC18488.1; -; Genomic_DNA.
DR PIR; E72805; E72805.
DR RefSeq; NP_046863.1; NC_001900.1.
DR SMR; O64238; -.
DR PRIDE; O64238; -.
DR GeneID; 1261588; -.
DR KEGG; vg:1261588; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000002131; Genome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050797; F:thymidylate synthase (FAD) activity; IDA:CACAO.
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; 3.30.70.3180; -; 2.
DR HAMAP; MF_01408; ThyX; 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 3: Inferred from homology;
KW FAD; Flavoprotein; Methyltransferase; NADP; Nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..235
FT /note="Probable flavin-dependent thymidylate synthase"
FT /id="PRO_0000175600"
FT DOMAIN 1..229
FT /note="ThyX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT MOTIF 93..103
FT /note="ThyX motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT ACT_SITE 195
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 70
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 90..93
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 93..95
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 103..105
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 168
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 184..186
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 195
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
SQ SEQUENCE 235 AA; 26528 MW; C182EC4A4D3BAB24 CRC64;
MKVQLIASTI LEDPSWAGTD YVGDDETVTS ADELAEFAGR NCYLSFDRPN PKTRENVDYL
NHILDVGHES VLEHSSATFY IEASRSVLTE LERHRHLSFS VVSQRYVDPT ELGIHVPPAF
TELSGSDADK AKEVLLDVQS FAQEAYEYLV HIFSDAGFPR KKAREAARAV LPNMTNSPMV
VTGNHRAWRY VIKNRWHEAA DAEIRELAGE LLRQLREIAP NTYQDIPTEP YSYGG
