ID THYX_PYRAB Reviewed; 244 AA. AC Q9UZ51; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-JAN-2010, entry version 50. DE RecName: Full=Thymidylate synthase thyX; DE Short=TS; DE Short=TSase; DE EC=2.1.1.148; GN Name=thyX; OrderedLocusNames=PYRAB13030; ORFNames=PAB0861; OS Pyrococcus abyssi. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=29292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX MEDLINE=22511545; PubMed=12622808; RX 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). CC -!- FUNCTION: Catalyzes the formation of dTMP and tetrahydrofolate CC from dUMP and methylenetetrahydrofolate (By similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP + CC FADH(2) = dTMP + tetrahydrofolate + FAD. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the thymidylate synthase thyX family. CC -!- SIMILARITY: Contains 1 thyX (flavin-dependent thymidylate CC synthase) domain. 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 PIR; C75039; C75039. DR RefSeq; NP_126978.1; -. DR SMR; Q9UZ51; 3-195. DR GeneID; 1496690; -. DR GenomeReviews; AL096836_GR; PYRAB13030. DR KEGG; pab:PAB0861; -. DR NMPDR; fig|272844.1.peg.1383; -. DR HOGENOM; HBG458114; -. DR OMA; HESILEH; -. DR BioCyc; PABY272844:PAB0861-MONOMER; -. DR BRENDA; 2.1.1.148; 262861. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01408; ThyX; 1; -. DR InterPro; IPR003669; Thymidylate_synthase_ThyX. DR Pfam; PF02511; Thy1; 1. DR PROSITE; PS51331; THYX; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Methyltransferase; KW Nucleotide biosynthesis; Transferase. FT CHAIN 1 244 Thymidylate synthase thyX. FT /FTId=PRO_0000175591. FT DOMAIN 2 207 ThyX. FT MOTIF 80 90 ThyX motif. 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 //