ID H0UKH3_9BACT Unreviewed; 342 AA.
AC H0UKH3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=JonanDRAFT_0804 {ECO:0000313|EMBL:EHM13182.1};
OS Jonquetella anthropi DSM 22815.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13182.1, ECO:0000313|Proteomes:UP000003806};
RN [1] {ECO:0000313|EMBL:EHM13182.1, ECO:0000313|Proteomes:UP000003806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13182.1,
RC ECO:0000313|Proteomes:UP000003806};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL Submitted (NOV-2011) 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|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CM001376; EHM13182.1; -; Genomic_DNA.
DR AlphaFoldDB; H0UKH3; -.
DR STRING; 885272.JonanDRAFT_0804; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_3_0; -.
DR Proteomes; UP000003806; 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; 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:UP000003806};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 23..321
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 342 AA; 36807 MW; 1D924EC4D3AEE7DA CRC64;
MYRESDSLNI SVGGVRAANP LFLAPMASVT TAAVRRLAVQ LGAGLTHTEM ASATGLVRGG
RQTLRVLDQT NDTRPLVAQL FAGDAESLVR GAEVALTCGP FDALGINMAC PMPKVLKRGA
GSALLDRPDE AASMVRELCR FGFPVWPKVR KEPAGSGITT EEFVQILFEA GASCVAVHGR
TPGQRYEGQA DRKSVKELCR AFPGRILASG DVFTAEDVLD YLSAGAGAVL LARGFIADPF
IVPRSLDLLS GRPEARPSLA SRYEIFCEFA GELERLHGPK MALGMVKRFA PGFFKFQAGA
GALRRTLGPI NDWNEMQIRL DEWFGQSERG KEHARNAAEL DG
//
