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-APR-2013, entry version 69. 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 (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 formation of dTMP and tetrahydrofolate CC from dUMP and methylenetetrahydrofolate (By similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP + NADPH CC = dTMP + tetrahydrofolate + NADP(+). 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 EMBL; HE613800; CCE70744.1; -; Genomic_DNA. DR PIR; C75039; C75039. DR RefSeq; NP_126978.1; NC_000868.1. DR ProteinModelPortal; Q9UZ51; -. DR STRING; 272844.PAB0861; -. DR EnsemblBacteria; CAB50208; CAB50208; PAB0861. DR GeneID; 1496690; -. DR GenomeReviews; AL096836_GR; PYRAB13030. DR KEGG; pab:PAB0861; -. DR eggNOG; COG1351; -. DR HOGENOM; HOG000047391; -. DR KO; K03465; -. DR OMA; QRYVRYK; -. DR ProtClustDB; PRK00847; -. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP. 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 SUPFAM; SSF69796; Thy1; 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 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 //