ID   R5HBZ4_9FIRM            Unreviewed;       330 AA.
AC   R5HBZ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   ORFNames=BN469_01848 {ECO:0000313|EMBL:CCY27013.1};
OS   Firmicutes bacterium CAG:114.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263001 {ECO:0000313|EMBL:CCY27013.1, ECO:0000313|Proteomes:UP000018090};
RN   [1] {ECO:0000313|EMBL:CCY27013.1, ECO:0000313|Proteomes:UP000018090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:114 {ECO:0000313|Proteomes:UP000018090};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR006621}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCY27013.1}.
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DR   EMBL; CAXW010000176; CCY27013.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5HBZ4; -.
DR   STRING; 1263001.BN469_01848; -.
DR   Proteomes; UP000018090; Unassembled WGS sequence.
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; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018090};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          12..237
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   330 AA;  37109 MW;  053090818660112A CRC64;
     MTDPHTLPPL SFAPLEGITG WIFRQVHHAM FPGLSRYYTP FFAPTADSPL TGRGLRDMHP
     DHNRGVPVVP QLLTNRAEDF IASARLLQDL GYKEVNLNLG CPSGTVVAKK KGAGFLSQPQ
     ALARFLDQIF QTLDVNISIK TRIGVENLEE WPPLLDLFQR YPICELIIHP RLRRDFYRGQ
     PRREAFTYAV AHSRLPLCYN GDLFSPQDCW DLVRQFPTVG RLMAGRGLVC NPALGRQLQG
     GPPLTKAELQ AFHDRLLDGY QSVLSGDWPV LGKMKELWSY WARLFPAPEK PLKAMRKAKT
     LTDYTFAAQS LFRDQDLLPG AHFPSAGASS
//