(data stored in ACNUC7421 zone)

SWISSPROT: D6XV68_BACIE

ID   D6XV68_BACIE            Unreviewed;       332 AA.
AC   D6XV68;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=Bsel_0076 {ECO:0000313|EMBL:ADH97626.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97626.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97626.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a
CC       modified base found in the D-loop of most tRNAs, via the reduction
CC       of the C5-C6 double bond in target uridines.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP001791; ADH97626.1; -; Genomic_DNA.
DR   RefSeq; WP_013171056.1; NC_014219.1.
DR   STRING; 439292.Bsel_0076; -.
DR   EnsemblBacteria; ADH97626; ADH97626; Bsel_0076.
DR   KEGG; bse:Bsel_0076; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217853; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   BioCyc; BSEL439292:G1GLR-83-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; D6XV68.
DR   SWISS-2DPAGE; D6XV68.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   ACT_SITE    103    103       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006621-1}.
SQ   SEQUENCE   332 AA;  36552 MW;  D047F408073D85EC CRC64;
     MTLSIGEITL KNPVVLAPMA GVCNPAFRLI AKEFGTGLVC AEMVSDKAIL HQNKRSINML
     YVAEREKPLS LQIFGGTKET LVEAAKIVDT QTNADIIDIN MGCPVPKVTS CDAGARWLLN
     PDRIYEMVDA VVQAVDKPVT VKMRKGWDDD TVYAVDNAKA VEAAGGKAIA LHGRTRVQMY
     EGEADWSIIK TVKEAVGIPI IGNGDVQTPE DAKRMMTETG ADGVMIGRAA LGNPWMLYRT
     IHFLETGENI AEPSPEEKMR VAILHMDRLI DWKGERVAVK EMRKHASYYM RGIRGAAKLR
     DQVNQMETRE EMAGVMERIG LLDQERIPAG GS
//

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