ID A0A0S7BNK1_9BACT Unreviewed; 321 AA.
AC A0A0S7BNK1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=TBC1_11154 {ECO:0000313|EMBL:GAP42026.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42026.1};
RN [1] {ECO:0000313|EMBL:GAP42026.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42026.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; DF968182; GAP42026.1; -; Genomic_DNA.
DR RefSeq; WP_062037084.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7BNK1; -.
DR STRING; 1678841.TBC1_11154; -.
DR Proteomes; UP000053091; 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 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.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|PIRNR:PIRNR006621};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 9..236
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 321 AA; 35951 MW; 6555ADBC998E70E8 CRC64;
MNLQTAIFFA PFQGITTKAF RLVYARHFAG VDKLFTPYFA NIAVDYPLPA LKMKALQHQS
ESGISVVPQI LSKSAPEILS FARSCAALGF GELNWNLGCP YPQVARKKRG SGMLPFPEMV
DEILDQVMPH MPLSFSVKCR LGYAKAAEIM DLVPVFNRYP VAELTIHART GKQLYSGKTD
PDAFGAALEG LQVPVVYNGD IFTTEDFGHI SGLFPGISRF MIGRGILKDP FLPARIKGLP
QPGDSRAVLR GFLDDLYFET RREKKDSPSA LNAMKECWTY LMFAFEEPVV VFRRLKKAGN
FDDYEDAIKE VFANDRLKIQ E
//
