ID TYSY_ALCBS Reviewed; 277 AA. AC Q0VM06; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.45; GN Name=thyA; OrderedLocusNames=ABO_2344; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- FUNCTION: Provides the sole de novo source of dTMP for DNA CC biosynthesis (By similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = CC dihydrofolate + dTMP. CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial- CC type thyA subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL17792.1; -; Genomic_DNA. DR RefSeq; YP_694064.1; -. DR GeneID; 4211942; -. DR GenomeReviews; AM286690_GR; ABO_2344. DR KEGG; abo:ABO_2344; -. DR NMPDR; fig|393595.12.peg.2345; -. DR HOGENOM; Q0VM06; -. DR OMA; Q0VM06; LGPVYGH. DR BioCyc; ABOR393595:ABO_2344-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004799; F:thymidylate synthase activity; IEA:HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00008; -; 1. DR InterPro; IPR000398; Thymidylat_synth_C. DR Gene3D; G3DSA:3.30.572.10; Thymidylat_synth_C; 1. DR PANTHER; PTHR11549:SF2; Thymidylat_synth_C; 1. DR Pfam; PF00303; Thymidylat_synt; 1. DR PRINTS; PR00108; THYMDSNTHASE. DR ProDom; PD001180; Thymidylat_synth; 1. DR TIGRFAMs; TIGR03284; thym_sym; 1. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW Nucleotide biosynthesis; Transferase. FT CHAIN 1 277 Thymidylate synthase. FT /FTId=PRO_1000000571. FT ACT_SITE 159 159 By similarity. SQ SEQUENCE 277 AA; 31049 MW; 7807D5D137C0D0A3 CRC64; MKQYLDLLRH VREHGTYKED RTGTGTYAVF GYQMRYDLSQ GFPMLTTKKL HLRSIIHELL WFLSGDTNIR YLKENGVSIW DGWATPEGEL GPVYGEQWRS WKTADGGVID QITEVLKEIK RNPDSRRLVV SAWNPAVLPD PSISPDANAA AGKQALPPCH CLFQFYVADG KLSCQLYQRS GDIFLGVPFN IASYALLTLM MAQVCDLQPG DFVHTLGDAH LYSNHLEQAD TQLARTPGPL PTMTLNPAVK DLFAFTFDDF TVSNYNPDAH IKAPVAI //