(data stored in SCRATCH3701 zone)

SWISSPROT: THYX_RICTY

ID   THYX_RICTY              Reviewed;         294 AA.
AC   Q68X70;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=Flavin-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=FDTS {ECO:0000255|HAMAP-Rule:MF_01408};
DE            EC=2.1.1.148 {ECO:0000255|HAMAP-Rule:MF_01408};
DE   AltName: Full=FAD-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE   AltName: Full=Thymidylate synthase ThyX {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=TS {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=TSase {ECO:0000255|HAMAP-Rule:MF_01408};
GN   Name=thyX {ECO:0000255|HAMAP-Rule:MF_01408}; OrderedLocusNames=RT0292;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-
CC       monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while
CC       utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor,
CC       and NADPH and FADH(2) as the reductant. {ECO:0000255|HAMAP-
CC       Rule:MF_01408}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) +
CC         NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+);
CC         Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC       Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC       monomers. {ECO:0000255|HAMAP-Rule:MF_01408};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01408}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01408}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC       {ECO:0000255|HAMAP-Rule:MF_01408}.
DR   EMBL; AE017197; AAU03772.1; -; Genomic_DNA.
DR   RefSeq; WP_011190756.1; NC_006142.1.
DR   SMR; Q68X70; -.
DR   STRING; 257363.RT0292; -.
DR   EnsemblBacteria; AAU03772; AAU03772; RT0292.
DR   KEGG; rty:RT0292; -.
DR   eggNOG; ENOG4107R2U; Bacteria.
DR   eggNOG; COG1351; LUCA.
DR   HOGENOM; HOG000021807; -.
DR   KO; K03465; -.
DR   OMA; WSYNEES; -.
DR   OrthoDB; 896350at2; -.
DR   BioCyc; RTYP257363:G1G0L-297-MONOMER; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.170; -; 1.
DR   HAMAP; MF_01408; ThyX; 1.
DR   InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR   InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR   PANTHER; PTHR34934; PTHR34934; 1.
DR   Pfam; PF02511; Thy1; 1.
DR   SUPFAM; SSF69796; SSF69796; 1.
DR   TIGRFAMs; TIGR02170; thyX; 1.
DR   PROSITE; PS51331; THYX; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68X70.
DR   SWISS-2DPAGE; Q68X70.
KW   FAD; Flavoprotein; Methyltransferase; NADP; Nucleotide biosynthesis;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Flavin-dependent thymidylate synthase"
FT                   /id="PRO_0000175574"
FT   DOMAIN          27..250
FT                   /note="ThyX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT   NP_BIND         93..96
FT                   /note="dUMP; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   NP_BIND         96..98
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   NP_BIND         104..108
FT                   /note="dUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   NP_BIND         205..207
FT                   /note="FAD; shared with neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   MOTIF           96..106
FT                   /note="ThyX motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   ACT_SITE        216
FT                   /note="Involved in ionization of N3 of dUMP, leading to its
FT                   activation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         73
FT                   /note="FAD; shared with neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         104
FT                   /note="FAD; shared with neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         189
FT                   /note="dUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         211
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         216
FT                   /note="dUMP; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
SQ   SEQUENCE   294 AA;  34445 MW;  929DAE351867E142 CRC64;
     MHNTTKRVTV PALEAMLYET IKVLDHGFIR VIDYMGDDSS IVQAARVSYG KGTKQLNQDK
     GLINYLLRHY HTTPFEMCDI KFHIKLPIFI ARQWIRHRTA SVNEYSARYS ILGNEFYLPE
     PTDIASQSAI NKQCRAGDSL PKKVSEKVLA ILEEDARRCY MHYKELMNAD EDGNIIDENV
     AGIARELARM NLTLNYYTEW YWKINLHNLL HFLRLRTDSK AQYEIRVYAG KILDIVKAWV
     PFTYEAFEEY RLQGANISRK GLEVIKRMIQ GEKVIHETSG MNKREWEELV KIFR
//

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