ID A0A143XJB4_9FIRM Unreviewed; 316 AA.
AC A0A143XJB4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN Name=dus_1 {ECO:0000313|EMBL:CVI67091.1};
GN ORFNames=BN3660_00745 {ECO:0000313|EMBL:CVI67091.1};
OS Eubacteriaceae bacterium CHKCI004.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI67091.1, ECO:0000313|Proteomes:UP000199324};
RN [1] {ECO:0000313|EMBL:CVI67091.1, ECO:0000313|Proteomes:UP000199324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC4 {ECO:0000313|EMBL:CVI67091.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; FCNR01000023; CVI67091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XJB4; -.
DR STRING; 1780380.BN3660_00745; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000199324; 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:UP000199324};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 5..233
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 94
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 316 AA; 36919 MW; 950F18EC8BF3FA80 CRC64;
MKIYAAPMEG VTGYVYRNAH RHYFQGIDKY YTPFLTPKKG KGWTSREKND IAPEHNQNIN
LVPQILTNQA DDFVRMAEKL ADCGYEEINL NLGCPSGTVV SKGKGCGFLA DREKLLRFFE
QVFDKVTVKV SVKTRLGLDS PEEIEPLMAI YNQFPLSEVI IHARIHKDFY KRPVNREAFR
KGFLLCRHPV CYNGDIFAKA DFERFREEFP EVDRIMIGRG LIANPQLAEM FTEDGRPDKV
RWKAFHDEIC AGYEDIMSGE RNVLFKMKEL WNYMLPMFED GEKIGKKIKK SVRLQTYKEL
VDMLFREKDF RQHVES
//
