ID A0A1S2L610_9BACI Unreviewed; 329 AA.
AC A0A1S2L610;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=AWH56_003705 {ECO:0000313|EMBL:QOY38479.1}, AWH56_19875
GN {ECO:0000313|EMBL:OIJ07908.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ07908.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:OIJ07908.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:OIJ07908.1,
RC ECO:0000313|Proteomes:UP000180175};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY38479.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY38479.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-16(2017).
RN [3] {ECO:0000313|EMBL:QOY38479.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY38479.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN [4] {ECO:0000313|EMBL:QOY38479.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY38479.1};
RA Bassil N.M., Lloyd J.R.;
RL Submitted (OCT-2020) 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|ARBA:ARBA00002790,
CC ECO:0000256|PIRNR:PIRNR006621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001387};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001183};
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; LQXD01000166; OIJ07908.1; -; Genomic_DNA.
DR EMBL; CP063356; QOY38479.1; -; Genomic_DNA.
DR RefSeq; WP_071318706.1; NZ_CP063356.1.
DR AlphaFoldDB; A0A1S2L610; -.
DR KEGG; aia:AWH56_003705; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000180175; Chromosome.
DR Proteomes; UP000180175; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR11082:SF25; DUS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000180175};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 16..319
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 329 AA; 37355 MW; 6D79A8B1707BC026 CRC64;
MIDNFWRDLP RPFFVLAPME DVTDVVFRHV VSAAGRPDVF FTEFANSDSF CHPEGIKSMR
GRLTFTEDEQ PIVAHILGDN PEYFRQMSIG MAELGFKGLD INMGCPVPNV ASRGKGSGLI
LRPDIAAELI QAAKAGGLPV SVKTRLGFKE VNEWEEWLTH ILKQDIANLS IHLRTRKEMS
EVDAHWELIP EIKKLRDRIA PNTLLTINGD IPDRQTGLQL AKQYGIDGVM IGRGIFKNPF
AFEKEPKEHS SKEYLDLLRL QLDLQDQYAE VLPRSITGLH RFFKIYVKGF HGAAELRSQL
MSTKSTEEVR ALLDNFEKAC DEDMLELEK
//
