DUSB_PSEPK
ID DUSB_PSEPK Reviewed; 337 AA.
AC Q88DK5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000255|HAMAP-Rule:MF_02042};
DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02042};
GN Name=dusB {ECO:0000255|HAMAP-Rule:MF_02042}; OrderedLocusNames=PP_4820;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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:0000255|HAMAP-Rule:MF_02042}.
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; Evidence={ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02042};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02042};
CC -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02042}.
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DR EMBL; AE015451; AAN70389.1; -; Genomic_DNA.
DR RefSeq; NP_746925.1; NC_002947.4.
DR RefSeq; WP_010955431.1; NC_002947.4.
DR AlphaFoldDB; Q88DK5; -.
DR SMR; Q88DK5; -.
DR STRING; 160488.PP_4820; -.
DR EnsemblBacteria; AAN70389; AAN70389; PP_4820.
DR KEGG; ppu:PP_4820; -.
DR PATRIC; fig|160488.4.peg.5143; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_1_6; -.
DR OMA; RPWLFAD; -.
DR PhylomeDB; Q88DK5; -.
DR BioCyc; PPUT160488:G1G01-5157-MON; -.
DR Proteomes; UP000000556; 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; 1.10.1200.80; -; 1.
DR Gene3D; 3.20.20.70; -; 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; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR004652; tRNA_dU_NifR3.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR TIGRFAMs; TIGR00737; nifR3_yhdG; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; RNA-binding;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..337
FT /note="tRNA-dihydrouridine synthase B"
FT /id="PRO_0000162094"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 19..21
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 73
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 203..205
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 227..228
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
SQ SEQUENCE 337 AA; 36489 MW; 3516CD7088B98938 CRC64;
MSAVRIGQYT LRNNLILAPM AGVTDQPFRT LCQRLGAGMV VSEMVSSDMS LWNSRKSSLR
RIHEGDPEPR SVQIAGGDAQ MMAAAAKANV EAGAQIIDIN MGCPAKKVCN KAAGSALLRD
EALVSEILHA VVSAVDVPVT LKIRTGWDRA NKNGLNVAKI AEQAGIQALA VHGRTRADLY
TGEAEYDTIG AIKQAVSIPV FANGDITSPE KARAVLETTG VDGLLIGRAA QGRPWIFREI
EHYLRTGEHL PAPQLDEVER ILLEHLAALH AFYGDVMGVR IARKHVGWYL ATRPGGKEFR
ARFNALEDTQ AQCANVRAFF SERRQSLETE DGQGVAA
