ID THYX_PYRAB STANDARD; PRT; 244 AA. AC Q9UZ51; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Thymidylate synthase thyX (EC 2.1.1.-) (TS) (TSase). GN THYX OR PYRAB13030 OR PAB0861. OS Pyrococcus abyssi. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=29292; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=GE5 / Orsay; RA Heilig R.; RT "Pyrococcus abyssi genome sequence: insights into archaeal chromosome RT structure and evolution."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of dTMP and tetrahydrofolate CC from dUMP and methylenetetrahydrofolate (By similarity). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: BELONGS TO THE THYMIDYLATE SYNTHASE THYX/THY1 FAMILY. 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; -. DR HAMAP; MF_01408; -; 1. DR InterPro; IPR003669; Thy1. DR Pfam; PF02511; Thy1; 1. KW Transferase; Methyltransferase; Nucleotide biosynthesis; FAD; KW Flavoprotein; Complete proteome. FT SITE 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 //