(data stored in SCRATCH3701 zone)

SWISSPROT: DUS_RICTY

ID   DUS_RICTY               Reviewed;         327 AA.
AC   Q68XZ3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 83.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
GN   Name=dus; OrderedLocusNames=RT0010;
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 synthesis of 5,6-dihydrouridine (D), a modified
CC       base found in the D-loop of most tRNAs, via the reduction of the C5-C6
CC       double bond in target uridines. {ECO:0000250|UniProtKB:P33371}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC         H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC         H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- SIMILARITY: Belongs to the Dus family. {ECO:0000305}.
DR   EMBL; AE017197; AAU03499.1; -; Genomic_DNA.
DR   RefSeq; WP_011190486.1; NC_006142.1.
DR   SMR; Q68XZ3; -.
DR   STRING; 257363.RT0010; -.
DR   EnsemblBacteria; AAU03499; AAU03499; RT0010.
DR   KEGG; rty:RT0010; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217855; -.
DR   OMA; FRNCVNT; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; RTYP257363:G1G0L-10-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   InterPro; IPR004652; tRNA_dU_NifR3.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00737; nifR3_yhdG; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68XZ3.
DR   SWISS-2DPAGE; Q68XZ3.
KW   Flavoprotein; FMN; NADP; Oxidoreductase; RNA-binding; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..327
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000280961"
FT   NP_BIND         17..19
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   NP_BIND         202..204
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   NP_BIND         226..227
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         72
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         141
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   327 AA;  35691 MW;  AB4DD899752814E5 CRC64;
     MIKIGNIELS SNVILAPMSN ITDLEFRKLV KRFGAGLVVS EMIASRAMIM KSRQSMQKCA
     IMHDDPTSAC VQLAGCEPDV IADAAKMNED MGAKIIDLNF GCPAKKVVGG YAGSALMRDE
     RLATKIFEAT VKAVKIPVTV KMRMGWDDNT KNAPTLAVIA ASSGVQMVTV HGRTRCQFYS
     GNANWDFIRV VKEAVKIPVI ANGDITNFAK AKEALQKSGA DGIMVGRGVY GKPWLISQIA
     YYLKTGKEKP APSIAEQLDI IIKHYDAIID YYGKSVGVPI ARKHIIWYSS GLPSSAEFRC
     AVNLMNDPIA VKEKIAEFYM SVMDANK
//

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