(data stored in SCRATCH zone)

SWISSPROT: A0LF98_SYNFM

ID   A0LF98_SYNFM            Unreviewed;       338 AA.
AC   A0LF98;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=Thymidylate synthase complementing protein ThyX {ECO:0000313|EMBL:ABK16100.1};
GN   OrderedLocusNames=Sfum_0400 {ECO:0000313|EMBL:ABK16100.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16100.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16100.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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 NADPH and FADH(2) as the reductant.
CC       {ECO:0000256|PROSITE-ProRule:PRU00661}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP +
CC         H(+) + 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:0000256|PROSITE-ProRule:PRU00661};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00661};
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DR   EMBL; CP000478; ABK16100.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0400; -.
DR   EnsemblBacteria; ABK16100; ABK16100; Sfum_0400.
DR   KEGG; sfu:Sfum_0400; -.
DR   eggNOG; ENOG4107WS4; Bacteria.
DR   eggNOG; COG1351; LUCA.
DR   OMA; LPNSCKT; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR   InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR   PANTHER; PTHR34934; PTHR34934; 1.
DR   Pfam; PF02511; Thy1; 2.
DR   SUPFAM; SSF69796; SSF69796; 1.
DR   PROSITE; PS51331; THYX; 1.
PE   4: Predicted;
DR   PRODOM; A0LF98.
DR   SWISS-2DPAGE; A0LF98.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   FAD {ECO:0000256|PROSITE-ProRule:PRU00661};
KW   Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00661};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00661};
KW   Nucleotide biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00661};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00661}.
FT   MOTIF       209    219       ThyX motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00661}.
SQ   SEQUENCE   338 AA;  38156 MW;  3DEE087B7EF363B2 CRC64;
     MSVQFVKTRV QPQGIAPAEE GRALQLVELC GRTAYKSEDK ITPDSARNFV LMLKSHGHLS
     VLEHSNIVLE IEATPSSGAT QALSSISELY GALLDGLGFR TAYHRIHLSA RTSPGALFIA
     GNLRSWIETL THLGNGGSPL HALLSAALRD FFPIIFGGEE TVSSNLSFKV TLVREDEQLA
     LLRRDAACDL PVFVFKFVCD RGITHEVVRH RVLSFTQEST RYVNYKNKGM VLILPEELYP
     FYDDATQQLT GRSPLVDMWI DRAEKLFAWY REDLDREKPE IARDILPNLL KSEIFVSGRW
     SGWKHFVQLR DSKHAHPRIR AIAKEVRNHF DSLGMTVE
//

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