DUSA_HAEIN
ID DUSA_HAEIN Reviewed; 327 AA.
AC P44794;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02041};
DE EC=1.3.1.91 {ECO:0000255|HAMAP-Rule:MF_02041};
DE AltName: Full=U20-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE Short=U20-specific Dus {ECO:0000255|HAMAP-Rule:MF_02041};
DE AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000255|HAMAP-Rule:MF_02041};
GN Name=dusA {ECO:0000255|HAMAP-Rule:MF_02041}; OrderedLocusNames=HI_0634;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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. Specifically modifies U20 and U20a in
CC tRNAs. {ECO:0000255|HAMAP-Rule:MF_02041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02041}.
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DR EMBL; L42023; AAC22293.1; -; Genomic_DNA.
DR PIR; H64155; H64155.
DR RefSeq; NP_438794.1; NC_000907.1.
DR RefSeq; WP_005694659.1; NC_000907.1.
DR AlphaFoldDB; P44794; -.
DR SMR; P44794; -.
DR STRING; 71421.HI_0634; -.
DR EnsemblBacteria; AAC22293; AAC22293; HI_0634.
DR KEGG; hin:HI_0634; -.
DR PATRIC; fig|71421.8.peg.661; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_2_1_6; -.
DR OMA; LIYPYVD; -.
DR PhylomeDB; P44794; -.
DR BioCyc; HINF71421:G1GJ1-665-MON; -.
DR Proteomes; UP000000579; 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:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02041; DusA_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR004653; DusA.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR42907; PTHR42907; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR TIGRFAMs; TIGR00742; yjbN; 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..327
FT /note="tRNA-dihydrouridine(20/20a) synthase"
FT /id="PRO_0000162067"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 170
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 210..212
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 232..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 96
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 182
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 185
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 298
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 301
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
SQ SEQUENCE 327 AA; 37186 MW; 0D086C3385FB43E7 CRC64;
MPQNLPHFYR GRFSVAPMLD WTTRHCRYFH RQFSKHALLY TEMVTAPAII HAKYDHLDFD
LQENPVALQL GGSDPEQLKY CAKLAEERGY HEINLNVGCP SDRVQNGMFG ACLMAKADLV
ADCVEQMQSA VKIPVTVKTR IGIDELDSYE FLCDFIEKVQ GKGCQEFIIH ARKAWLSGLS
PKENREIPPL DYIRVYQLKR DFPHLTIAIN GGIKTIEEMK QHLQYVDGVM VGREAYQNPS
LLGQIDQALF DPNAPIVTAH EAVESMLPYI EQQLSQGIHL NHIVRHILGA FQNCKGARQW
RRYLSENAFK QGAGIEVVET ALSFVES
