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Database: UniProt/TrEMBL
Entry: E4T9U1_RIEAD
LinkDB: E4T9U1_RIEAD
Original site: E4T9U1_RIEAD 
ID   E4T9U1_RIEAD            Unreviewed;       264 AA.
AC   E4T9U1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   30-NOV-2016, entry version 46.
DE   RecName: Full=Thymidylate synthase {ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS00633410};
DE            Short=TS {ECO:0000256|HAMAP-Rule:MF_00008};
DE            Short=TSase {ECO:0000256|HAMAP-Rule:MF_00008};
DE            EC=2.1.1.45 {ECO:0000256|HAMAP-Rule:MF_00008};
GN   Name=thyA {ECO:0000256|HAMAP-Rule:MF_00008};
GN   ORFNames=RA0C_0840 {ECO:0000313|EMBL:AFD55782.1};
OS   Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 /
OS   NCTC 11014).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Riemerella.
OX   NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD55782.1, ECO:0000313|Proteomes:UP000010093};
RN   [1] {ECO:0000313|EMBL:AFD55782.1, ECO:0000313|Proteomes:UP000010093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX   PubMed=22628503; DOI=10.1128/JB.00366-12;
RA   Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA   Liu F., Wang Y., Chen X.Y.;
RT   "Complete genome sequence of Riemerella anatipestifer reference
RT   strain.";
RL   J. Bacteriol. 194:3270-3271(2012).
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:0000256|HAMAP-Rule:MF_00008}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP =
CC       dihydrofolate + dTMP. {ECO:0000256|HAMAP-Rule:MF_00008,
CC       ECO:0000256|SAAS:SAAS00633317}.
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00008, ECO:0000256|SAAS:SAAS00635248}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00008,
CC       ECO:0000256|SAAS:SAAS00633361}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-
CC       type ThyA subfamily. {ECO:0000256|HAMAP-Rule:MF_00008}.
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DR   EMBL; CP003388; AFD55782.1; -; Genomic_DNA.
DR   RefSeq; WP_013446852.1; NC_017045.1.
DR   ProteinModelPortal; E4T9U1; -.
DR   EnsemblBacteria; AFD55782; AFD55782; RA0C_0840.
DR   KEGG; rai:RA0C_0840; -.
DR   KEGG; ran:Riean_0607; -.
DR   PATRIC; 45351892; VBIRieAna155424_0612.
DR   HOGENOM; HOG000257900; -.
DR   KO; K00560; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000010093; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-HAMAP.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010093};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00633371};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00635234};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00633353}.
FT   DOMAIN        2    264       Thymidylat_synt. {ECO:0000259|Pfam:
FT                                PF00303}.
FT   NP_BIND     126    127       dUMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   NP_BIND     166    169       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   NP_BIND     207    209       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   ACT_SITE    146    146       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00008}.
FT   BINDING      21     21       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING      51     51       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     169    169       5,10-methylenetetrahydrofolate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     177    177       dUMP. {ECO:0000256|HAMAP-Rule:MF_00008}.
FT   BINDING     263    263       5,10-methylenetetrahydrofolate; via
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00008}.
SQ   SEQUENCE   264 AA;  30062 MW;  7510D72A5775F120 CRC64;
     MQNYLDLLQH ILDHGTDKTD RTGTGTRSVF GYQLRYDLSK GFPLVTTKKV HLKSIIYELL
     WFLKGDTNIK YLNDNGVSIW DEWADDNGNL GPVYGAQWRS WKGANGKVID QISEVIHQIK
     TNPDSRRLIV SAWNAAEIPN MALAPCHALF QFYVADGRLS LQLYQRSADV FLGVPFNIAS
     YALLTMMVAQ VCGLQVGEYI HSFGDVHIYN NHFEQVQKQL SREPRPLPTM KLNPSVKDLF
     DFKFEDFTLE NYHPHSGIKA PVAV
//
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