DUS_HELPY
ID DUS_HELPY Reviewed; 328 AA.
AC O25427;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable tRNA-dihydrouridine synthase;
DE EC=1.3.1.-;
GN Name=dus; OrderedLocusNames=HP_0727;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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:0000250|UniProtKB:P33371}.
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:0000250|UniProtKB:P33371};
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:0000250|UniProtKB:P33371};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P33371};
CC -!- SIMILARITY: Belongs to the Dus family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07774.1; -; Genomic_DNA.
DR PIR; G64610; G64610.
DR RefSeq; NP_207521.1; NC_000915.1.
DR RefSeq; WP_000346174.1; NC_018939.1.
DR AlphaFoldDB; O25427; -.
DR SMR; O25427; -.
DR DIP; DIP-3615N; -.
DR IntAct; O25427; 1.
DR MINT; O25427; -.
DR STRING; 85962.C694_03740; -.
DR PaxDb; O25427; -.
DR EnsemblBacteria; AAD07774; AAD07774; HP_0727.
DR KEGG; hpy:HP_0727; -.
DR PATRIC; fig|85962.47.peg.776; -.
DR eggNOG; COG0042; Bacteria.
DR OMA; FRNCVNT; -.
DR PhylomeDB; O25427; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 1.10.1200.80; -; 1.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 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..328
FT /note="Probable tRNA-dihydrouridine synthase"
FT /id="PRO_0000162134"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 13..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 67
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 198..200
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 222..223
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
SQ SEQUENCE 328 AA; 37150 MW; D4F3494C7CF0B6B3 CRC64;
MDFKNKKWLF LAPLAGYTDL PFRSVVKKFG VDVTTSEMVS SHSLVYAFDK TSKMLEKSPL
EDHFMAQISG SKESVVKEAV EKINALEHVN GIDFNCGCPA PKVANHGNGS GLLKDLNHLV
KLLKTIRENT SKKITSVKVR LGFEKKIPKE IAHALNDAPV DYVVVHGRTR SDKYQKDKID
YESIALMKKI LKKPVIANGE IDSVKKAFEV LQITQADGLM IGRAALRAPW IFWQIRNNTT
KLPAVVKKDL VLEHFDKMVE FYGDMGVIMF RKNLHAYAKG EMQASAFRNC VNTLTEIKSM
RESIEEFFNQ EMLQSEVPLW VELNQKSV
