ID V8QLJ9_9BURK Unreviewed; 337 AA. AC V8QLJ9; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 02-OCT-2024, entry version 38. 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=W822_21015 {ECO:0000313|EMBL:ETF00846.1}; OS Advenella kashmirensis W13003. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae. OX NCBI_TaxID=1424334 {ECO:0000313|EMBL:ETF00846.1, ECO:0000313|Proteomes:UP000018733}; RN [1] {ECO:0000313|EMBL:ETF00846.1, ECO:0000313|Proteomes:UP000018733} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W13003 {ECO:0000313|EMBL:ETF00846.1, RC ECO:0000313|Proteomes:UP000018733}; RX PubMed=24482505; RA Wang X., Jin D., Zhou L., Wu L., An W., Zhao L.; RT "Draft Genome Sequence of Advenella kashmirensis Strain W13003, a RT Polycyclic Aromatic Hydrocarbon-Degrading Bacterium."; RL Genome Announc. 2:e00003-14(2014). 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 ECO:0000256|PIRSR:PIRSR006621-2}; 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ETF00846.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AYXT01000013; ETF00846.1; -; Genomic_DNA. DR RefSeq; WP_024007124.1; NZ_KI650982.1. DR AlphaFoldDB; V8QLJ9; -. DR STRING; 1424334.W822_21015; -. DR PATRIC; fig|1424334.3.peg.4216; -. DR eggNOG; COG0042; Bacteria. DR HOGENOM; CLU_013299_0_1_4; -. DR OrthoDB; 9764501at2; -. DR Proteomes; UP000018733; Unassembled WGS sequence. 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR006621-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_02042}; 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 14..322 FT /note="DUS-like FMN-binding" FT /evidence="ECO:0000259|Pfam:PF01207" FT ACT_SITE 100 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-1" FT BINDING 16..18 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-2" FT BINDING 70 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-2" FT BINDING 142 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-2" FT BINDING 172 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|PIRSR:PIRSR006621-2" FT BINDING 203..205 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042" FT BINDING 227..228 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-2" SQ SEQUENCE 337 AA; 37128 MW; 693299B77C5A580F CRC64; MQIGAWTLPN PVFVAPMAGV TDRPFRQLCK QLGAGYAVSE MAASNPALWD SVKTSRRLNH DGEIDPIAVQ IAGADPVMLA EAAVFNIRKG ARIIDINMGC PVKKVCHVAS GSALLRDEEL VARILQTVVD ACRPFDVPVT LKTRTGWDRQ SRNALRIARL AEDAGIAALT LHGRTRCDLY AGQAEYDTIA AVKAAISIPV IANGDITDPL KAQYVLNYTG ADAIMIGRAA QGNPWIFREI NHYLETGTFL APPSWAHMRD VLLAHLDHHY QFYGEYTGVR TARKHIGWYI GNLPDAELFR QQMNCLETCQ AQYNAVNQWF TKLVNESAPR VPLAAVH //