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 05-DEC-2018, entry version 98. 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}; GN OrderedLocusNames=PYRAB13030; 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., RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic RT archaeon 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 RT and Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). CC -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine- CC 5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate CC (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as CC the methyl donor, and NADPH and FADH(2) as the reductant. CC {ECO:0000255|HAMAP-Rule:MF_01408}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + CC H(+) + 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 CC three monomers. {ECO:0000255|HAMAP-Rule:MF_01408}; CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC {ECO:0000255|HAMAP-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 ProteinModelPortal; Q9UZ51; -. DR SMR; Q9UZ51; -. DR STRING; 272844.PAB0861; -. DR EnsemblBacteria; CAB50208; CAB50208; PAB0861. DR GeneID; 1496690; -. DR KEGG; pab:PAB0861; -. DR PATRIC; fig|272844.11.peg.1387; -. DR eggNOG; arCOG01883; Archaea. DR eggNOG; COG1351; LUCA. DR HOGENOM; HOG000047391; -. DR KO; K03465; -. DR OMA; VLPNACE; -. DR OrthoDB; POG093Z0AV3; -. DR BioCyc; PABY272844:G1GT8-1432-MONOMER; -. 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 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 Complete proteome; FAD; Flavoprotein; Methyltransferase; NADP; KW Nucleotide biosynthesis; Transferase. FT CHAIN 1 244 Flavin-dependent thymidylate synthase. FT /FTId=PRO_0000175591. FT DOMAIN 2 207 ThyX. {ECO:0000255|PROSITE- FT ProRule:PRU00661}. FT NP_BIND 77 80 dUMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01408}. FT NP_BIND 80 82 FAD. {ECO:0000255|HAMAP-Rule:MF_01408}. FT NP_BIND 88 92 dUMP. {ECO:0000255|HAMAP-Rule:MF_01408}. FT NP_BIND 162 164 FAD; shared with neighboring subunits. FT {ECO:0000255|HAMAP-Rule:MF_01408}. FT MOTIF 80 90 ThyX motif. {ECO:0000255|HAMAP- FT Rule:MF_01408}. FT ACT_SITE 173 173 Involved in ionization of N3 of dUMP, FT leading to its activation. FT {ECO:0000255|HAMAP-Rule:MF_01408}. FT BINDING 56 56 FAD; shared with neighboring subunits. FT {ECO:0000255|HAMAP-Rule:MF_01408}. FT BINDING 88 88 FAD; shared with neighboring subunits. FT {ECO:0000255|HAMAP-Rule:MF_01408}. FT BINDING 146 146 dUMP. {ECO:0000255|HAMAP-Rule:MF_01408}. FT BINDING 168 168 FAD. {ECO:0000255|HAMAP-Rule:MF_01408}. FT BINDING 173 173 dUMP; shared with dimeric partner. FT {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 //