THYX_PYRAB
ID THYX_PYRAB Reviewed; 244 AA.
AC Q9UZ51; G8ZHA7;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Flavin-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=FDTS {ECO:0000255|HAMAP-Rule:MF_01408};
DE EC=2.1.1.148 {ECO:0000255|HAMAP-Rule:MF_01408};
DE AltName: Full=FAD-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE AltName: Full=Thymidylate synthase ThyX {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=TS {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_01408};
GN Name=thyX {ECO:0000255|HAMAP-Rule:MF_01408}; OrderedLocusNames=PYRAB13030;
GN ORFNames=PAB0861;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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:0000255|HAMAP-
CC Rule:MF_01408}.
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:0000255|HAMAP-Rule:MF_01408};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC monomers. {ECO:0000255|HAMAP-Rule:MF_01408};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01408}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01408}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC {ECO:0000255|HAMAP-Rule:MF_01408}.
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DR EMBL; AJ248287; CAB50208.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70744.1; -; Genomic_DNA.
DR PIR; C75039; C75039.
DR RefSeq; WP_010868418.1; NC_000868.1.
DR AlphaFoldDB; Q9UZ51; -.
DR SMR; Q9UZ51; -.
DR STRING; 272844.PAB0861; -.
DR PRIDE; Q9UZ51; -.
DR EnsemblBacteria; CAB50208; CAB50208; PAB0861.
DR GeneID; 1496690; -.
DR KEGG; pab:PAB0861; -.
DR PATRIC; fig|272844.11.peg.1387; -.
DR eggNOG; arCOG01883; Archaea.
DR HOGENOM; CLU_077585_0_0_2; -.
DR OMA; AKLGPRC; -.
DR OrthoDB; 77034at2157; -.
DR PhylomeDB; Q9UZ51; -.
DR BRENDA; 2.1.1.148; 5242.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
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 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 Transferase.
FT CHAIN 1..244
FT /note="Flavin-dependent thymidylate synthase"
FT /id="PRO_0000175591"
FT DOMAIN 2..207
FT /note="ThyX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT MOTIF 80..90
FT /note="ThyX motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT ACT_SITE 173
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 77..80
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 80..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 88..92
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:0000255|HAMAP-Rule:MF_01408"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 146
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:0000255|HAMAP-Rule:MF_01408"
FT BINDING 162..164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 173
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
SQ SEQUENCE 244 AA; 29193 MW; BD54D9AB170222BD CRC64;
MVRVTLVNYT RRPLETITWA ALVSYWDEWS TESFEKINED DVKAHLPRIL GYGHESILEH
ATFTFSIEGC SRVCTHQLVR HRIASYTQQS QRYIVLNEEN VEETFVIPES IKKDRELYEK
WKKAMAETIK LYKESLKRGI HQEDARFILP QAVRSKIVVT MNLRELKHFF GLRLCERAQW
EIREVAWKML EEIAKREELR PIIKWAKLGP RCIQLGYCPE RELMPPGCFK RTRERWMKLL
EKPL
