DUSC_HAEIN
ID DUSC_HAEIN Reviewed; 310 AA.
AC P44606;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000255|HAMAP-Rule:MF_02043};
DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02043};
DE AltName: Full=U16-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02043};
DE Short=U16-specific Dus {ECO:0000255|HAMAP-Rule:MF_02043};
DE AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000255|HAMAP-Rule:MF_02043};
GN Name=dusC {ECO:0000255|HAMAP-Rule:MF_02043}; OrderedLocusNames=HI_0270;
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 U16 in tRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_02043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC -!- SIMILARITY: Belongs to the Dus family. DusC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02043}.
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DR EMBL; L42023; AAC21936.1; -; Genomic_DNA.
DR PIR; F64146; F64146.
DR RefSeq; NP_438439.1; NC_000907.1.
DR RefSeq; WP_005694032.1; NC_000907.1.
DR AlphaFoldDB; P44606; -.
DR SMR; P44606; -.
DR STRING; 71421.HI_0270; -.
DR EnsemblBacteria; AAC21936; AAC21936; HI_0270.
DR KEGG; hin:HI_0270; -.
DR PATRIC; fig|71421.8.peg.285; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_4_6; -.
DR OMA; YRPPAHW; -.
DR PhylomeDB; P44606; -.
DR BioCyc; HINF71421:G1GJ1-285-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:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 1.20.225.30; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02043; DusC_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR032886; DusC.
DR InterPro; IPR042270; DusC_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR11082:SF26; PTHR11082:SF26; 1.
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..310
FT /note="tRNA-dihydrouridine(16) synthase"
FT /id="PRO_0000162113"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 7..9
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 200..202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 224..225
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 35
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 95
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 176
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 272
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 274
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 279
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 295
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
SQ SEQUENCE 310 AA; 35057 MW; 8393D56E26EB6409 CRC64;
MRVILAPMQG VLDPFVRELL TEVNDYDLCI TEFVRVVDQL LPEKVFYRLC PELKNQGFTS
SGTPVRVQLL GQHPKCLAEN AIRAIDLGSH GIDLNCGCPS KTVNGSNGGA ALLKQPELIY
RATQALRRAV PSEFPVSVKV RLGWDDISQA FEIADAVEQG GATEITVHGR TKADGYRADR
INWKKISEVR ERLSIPVIAN GEIWHWQDGQ DCLSQTGCQD LMVGRGALNI PNLSHVLKSN
AEKMPWYEIQ KILQKYANVE NEYDSGFYHV ARIKQWLRYL NKEYNEANQV FDKIKTCQTA
EDLKLRLNEK
