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THYX_WOLPM
ID   THYX_WOLPM              Reviewed;         284 AA.
AC   Q73FX5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=WD_1198;
OS   Wolbachia pipientis wMel.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=163164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA   Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(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}.
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DR   EMBL; AE017196; AAS14844.1; -; Genomic_DNA.
DR   RefSeq; WP_010082033.1; NC_002978.6.
DR   AlphaFoldDB; Q73FX5; -.
DR   SMR; Q73FX5; -.
DR   STRING; 163164.WD_1198; -.
DR   EnsemblBacteria; AAS14844; AAS14844; WD_1198.
DR   GeneID; 29555733; -.
DR   KEGG; wol:WD_1198; -.
DR   eggNOG; COG1351; Bacteria.
DR   OMA; EWARLMP; -.
DR   OrthoDB; 896350at2; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000008215; 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;
KW   FAD; Flavoprotein; Methyltransferase; NADP; Nucleotide biosynthesis;
KW   Transferase.
FT   CHAIN           1..284
FT                   /note="Flavin-dependent thymidylate synthase"
FT                   /id="PRO_0000175586"
FT   DOMAIN          27..237
FT                   /note="ThyX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT   REGION          122..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..106
FT                   /note="ThyX motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   COMPBIAS        122..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        203
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                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         93..96
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         96..98
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         104..108
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         176
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         192..194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         198
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         203
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
SQ   SEQUENCE   284 AA;  33247 MW;  F4AF0BC577596BB3 CRC64;
     MNEATKRTIV KEIDAILYEE HKVLDHGFIR VVDYMGSDSA IVQAARVSYG KGTKQISQDE
     ALIKYLMRHH HTTPFEMCEI KFHVKLPIFV ARQWIRHRTA NVNEYSARYS ILDNEFYTPK
     PEQVAKQSDN NKQGSGEAFD PDTSKEIIDS LINDSNLVYS HYEKFIEQGL AREIARTNLM
     LNYYTQFYWK IDLHNLLHFL KLRADKHAQY EIRVYAEVML DIIKKWVPLA YNAFVEYCLE
     SACISRTGLE IIRKLIKGEN VTREESNIGK REWGELMSIL DKQS
 
 
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