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Database: UniProt/TrEMBL
Entry: E4TRW9_MARTH
LinkDB: E4TRW9_MARTH
Original site: E4TRW9_MARTH 
ID   E4TRW9_MARTH            Unreviewed;       264 AA.
AC   E4TRW9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   30-NOV-2016, entry version 44.
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   OrderedLocusNames=Ftrac_0718 {ECO:0000313|EMBL:ADR20720.1};
OS   Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB
OS   1408 / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter
OS   tractuosus).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Marivirga.
OX   NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR20720.1, ECO:0000313|Proteomes:UP000008720};
RN   [1] {ECO:0000313|Proteomes:UP000008720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC   H-43 {ECO:0000313|Proteomes:UP000008720};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schroeder M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Marivirga tractuosa DSM 4126.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002349; ADR20720.1; -; Genomic_DNA.
DR   RefSeq; WP_013452871.1; NC_014759.1.
DR   STRING; 643867.Ftrac_0718; -.
DR   EnsemblBacteria; ADR20720; ADR20720; Ftrac_0718.
DR   KEGG; mtt:Ftrac_0718; -.
DR   PATRIC; 45214663; VBIMarTra126157_0755.
DR   eggNOG; ENOG4105C0V; Bacteria.
DR   eggNOG; COG0207; LUCA.
DR   HOGENOM; HOG000257899; -.
DR   KO; K00560; -.
DR   OMA; IVYELLW; -.
DR   OrthoDB; POG091H02L6; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000008720; 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:UP000008720};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00633371, ECO:0000313|EMBL:ADR20720.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00635234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008720};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00008,
KW   ECO:0000256|SAAS:SAAS00633353, ECO:0000313|EMBL:ADR20720.1}.
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;  30353 MW;  68297BF7C67FBB86 CRC64;
     MKQYHELMKH ILDKGVQKGD RTGTGTISVF GYQMRFDLSE GFPVVTTKKL HLRSIIHELL
     WFLKGETNIK YLKENGVSIW DEWADENGEL GPVYGSQWRN WPTPDGQHID QISQIIDQIK
     NTPNSRRIMV SAWNVADVPN MALPPCHALF QFYVADGKLS CQLYQRSADV FLGVPFNIAS
     YALLTMMVAQ VCDLEPGDFI HTLGDAHLYS NHLEQTELQL SREPYPLPKM KINPNVKNIF
     DFKFEDFELV DYQYHPHIKA PVAV
//
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