THYX_BPPHC
ID THYX_BPPHC Reviewed; 237 AA.
AC Q9ZX92;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Gp16;
GN Name=16;
OS Streptomyces phage phiC31 (Bacteriophage phi-C31).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lomovskayavirus.
OX NCBI_TaxID=10719;
OH NCBI_TaxID=1902; Streptomyces coelicolor.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Norwich;
RX PubMed=10051617; DOI=10.1073/pnas.96.5.2192;
RA Hendrix R.W., Smith M.C.M., Burns N., Ford M.E., Hatfull G.F.;
RT "Evolutionary relationships among diverse bacteriophages and prophages: all
RT the world's a phage.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2192-2197(1999).
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; AJ006589; CAA07140.1; -; Genomic_DNA.
DR RefSeq; NP_047961.1; NC_001978.3.
DR SMR; Q9ZX92; -.
DR GeneID; 2715864; -.
DR KEGG; vg:2715864; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000002124; 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; 3.30.70.3180; -; 2.
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..237
FT /note="Probable flavin-dependent thymidylate synthase"
FT /id="PRO_0000175602"
FT DOMAIN 22..230
FT /note="ThyX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT MOTIF 100..110
FT /note="ThyX motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT ACT_SITE 196
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000250|UniProtKB:Q9WYT0"
FT BINDING 76
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 97..100
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 100..102
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 110..112
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 169
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 185..187
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 196
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 237 AA; 26016 MW; 3FDEF9BA6DF302C0 CRC64;
MKVNVLATTA LNPSPLLDAY EYRVSGAAYN RDRPTDADAL GEAAGRICYK SFERKNPATA
SNPGYLGNIL AQGHFSVLEH ASVTFLVRDV SRALLTELSR HRHLSFSVVS QRYVDHADTE
PVVPPAIRGT ELEKPFREDY AEALQAYDAG VKLLRARGYG RKQAREAARA LLPNAAPVDM
VVTGNLRAWR DVLGKRWHVA ADAEIREFAG RVLDHLHAVA PNSVQDMPTS PFGSDGK
