ID A0A1P8R2B9_9GAMM Unreviewed; 346 AA.
AC A0A1P8R2B9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000256|HAMAP-Rule:MF_02042};
DE EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02042};
GN Name=dusB {ECO:0000256|HAMAP-Rule:MF_02042};
GN ORFNames=BWR19_07595 {ECO:0000313|EMBL:APX92803.1};
OS Halomonas sp. 1513.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1883416 {ECO:0000313|EMBL:APX92803.1, ECO:0000313|Proteomes:UP000187327};
RN [1] {ECO:0000313|Proteomes:UP000187327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1513 {ECO:0000313|Proteomes:UP000187327};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-2017) 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|HAMAP-Rule:MF_02042, 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, ECO:0000256|HAMAP-
CC Rule:MF_02042};
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, ECO:0000256|HAMAP-
CC Rule:MF_02042};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02042}.
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP019326; APX92803.1; -; Genomic_DNA.
DR RefSeq; WP_076747479.1; NZ_CP019326.1.
DR AlphaFoldDB; A0A1P8R2B9; -.
DR STRING; 1883416.BWR19_07595; -.
DR KEGG; halo:BWR19_07595; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000187327; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02042; DusB_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR032887; DusB.
DR InterPro; IPR004652; DusB-like.
DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR NCBIfam; TIGR00737; nifR3_yhdG; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_02042};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02042};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02042};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02042}; Reference proteome {ECO:0000313|Proteomes:UP000187327};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_02042};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_02042}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}.
FT DOMAIN 21..328
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042,
FT ECO:0000256|PIRSR:PIRSR006621-1"
FT BINDING 24..26
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT BINDING 78
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT BINDING 147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT BINDING 208..210
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT BINDING 232..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
SQ SEQUENCE 346 AA; 37636 MW; 3903E5D324E91E28 CRC64;
MPIDASALPS IGRHRLPNRV ILAPMAGVTD RPFRQLCRRL GAGLVVGEMV TSDPSLWHTR
KSRLRMDHRG EPGPRAVQIA GGDAAMLAEA ARLNAEQGAE IIDINMGCPA KKVCNKAAGS
ALLRDERLVA EILDAVVAAV DVPVTLKIRT GWCAESNNGL RIARLAEDAG IQALAVHGRT
REQRYTGHAE YDTIAAIKAA ISIPVFANGD IDSPEKAARV LDYTGADAVM VGRGAQGNPW
LFAEIDHYLR HGQRLAAPSA AQRREVMQDH LATLHAFYGE HMGVRIARKH LGWYLARHAA
DDHAVKALRA RFNALERAQA QQHFVDQLFR HPADIRQMAS DGISAA
//
