ID A0A1H4D152_9BACT Unreviewed; 352 AA.
AC A0A1H4D152;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=SAMN04487851_11095 {ECO:0000313|EMBL:SEA66179.1};
OS Prevotella sp. tc2-28.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761888 {ECO:0000313|EMBL:SEA66179.1, ECO:0000313|Proteomes:UP000199625};
RN [1] {ECO:0000313|EMBL:SEA66179.1, ECO:0000313|Proteomes:UP000199625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC2-28 {ECO:0000313|EMBL:SEA66179.1,
RC ECO:0000313|Proteomes:UP000199625};
RA de Groot N.N.;
RL Submitted (OCT-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; FNRE01000010; SEA66179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4D152; -.
DR STRING; 1761888.SAMN04487851_11095; -.
DR Proteomes; UP000199625; 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:UP000199625};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 25..332
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 352 AA; 39458 MW; 3169064D9DEDC1CE CRC64;
MNYFRTFAPA MRIGNIDLGE RPVFLAPMED VTDIGFRLLC KRFGASMVYT EFVSAEALVR
DVKSTVNKLK IADEERPVGI QIYGRDIDAM VEAAKIVEQA GPDVIDLNFG CPVKKVAGKG
AGAGMLQNIM LPDGSINPDA KLLEITRKVV DAVRVPVTAK TRLGWNHEQL CITSLAEQLQ
DCGIRALTIH GRTRSQMYTG EADWTLIGEV KRNPRIHIPI IGNGDIKSLS DADRAFDTYG
VDAVMIGRAT FGCPWIFSRQ ELTLDEKIDV LEEQLRINIE RCDTEEIRKS KKSAELCGIL
HTRRHLAASP VFKGIPNFRE TRIQMLRAEK KDDLIAILEN CRERLRSEPL HQ
//
