(data stored in ACNUC7421 zone)

SWISSPROT: TYSY_PSEAB

ID   TYSY_PSEAB              Reviewed;         264 AA.
AC   Q02U73;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_00008};
DE            Short=TS {ECO:0000255|HAMAP-Rule:MF_00008};
DE            Short=TSase {ECO:0000255|HAMAP-Rule:MF_00008};
DE            EC=2.1.1.45 {ECO:0000255|HAMAP-Rule:MF_00008};
GN   Name=thyA {ECO:0000255|HAMAP-Rule:MF_00008};
GN   OrderedLocusNames=PA14_04480;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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 reductant in the reaction, yielding
CC       dihydrofolate (DHF) as a by-product. This enzymatic reaction
CC       provides an intracellular de novo source of dTMP, an essential
CC       precursor for DNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP =
CC       dihydrofolate + dTMP. {ECO:0000255|HAMAP-Rule:MF_00008}.
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00008}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-
CC       type ThyA subfamily. {ECO:0000255|HAMAP-Rule:MF_00008}.
DR   EMBL; CP000438; ABJ15306.1; -; Genomic_DNA.
DR   RefSeq; WP_003110588.1; NC_008463.1.
DR   ProteinModelPortal; Q02U73; -.
DR   SMR; Q02U73; -.
DR   EnsemblBacteria; ABJ15306; ABJ15306; PA14_04480.
DR   KEGG; pau:PA14_04480; -.
DR   HOGENOM; HOG000257900; -.
DR   KO; K00560; -.
DR   OMA; KQYLDLC; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR   Gene3D; 3.30.572.10; -; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   InterPro; IPR020940; Thymidylate_synthase_AS.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; SSF55831; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 2.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02U73.
DR   SWISS-2DPAGE; Q02U73.
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   Nucleotide biosynthesis; Transferase.
FT   CHAIN         1    264       Thymidylate synthase.
FT                                /FTId=PRO_1000000651.
FT   NP_BIND     126    127       dUMP; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   NP_BIND     166    169       dUMP. {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   NP_BIND     207    209       dUMP. {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   ACT_SITE    146    146       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00008}.
FT   BINDING      21     21       dUMP. {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   BINDING      51     51       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   BINDING     169    169       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   BINDING     177    177       dUMP. {ECO:0000255|HAMAP-Rule:MF_00008}.
FT   BINDING     263    263       5,10-methylenetetrahydrofolate; via
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00008}.
SQ   SEQUENCE   264 AA;  30016 MW;  D34075691D06F352 CRC64;
     MKQYLDLMRH VREHGTFKSD RTGTGTYSVF GHQMRFDLAA GFPLVTTKKC HLKSIVHELL
     WFLKGSTNIA YLKEHGVSIW DEWADENGDL GPVYGYQWRS WPAPDGRHID QIANLMAMLK
     KNPDSRRLIV SAWNPALIDE MALPPCHALF QFYVADGKLS CQLYQRSADI FLGVPFNIAS
     YALLTLMVAQ VAGLQPGEFI WTGGDCHLYA NHLEQADLQL TREPLPLPSM KLNPEVKDLF
     DFRFEDFELV GYEAHPHIKA PVAV
//

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