DUSC_CUPNH
ID DUSC_CUPNH Reviewed; 322 AA.
AC O68273; Q0KBP3;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=H16_A1443;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9555876; DOI=10.1128/jb.180.8.1979-1987.1998;
RA Slater S., Houmiel K.L., Tran M., Mitsky T.A., Taylor N.B., Padgette S.R.,
RA Gruys K.J.;
RT "Multiple beta-ketothiolases mediate poly(beta-hydroxyalkanoate) copolymer
RT synthesis in Ralstonia eutropha.";
RL J. Bacteriol. 180:1979-1987(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AF026544; AAC38320.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ92578.1; -; Genomic_DNA.
DR RefSeq; WP_011615087.1; NZ_CP039287.1.
DR AlphaFoldDB; O68273; -.
DR SMR; O68273; -.
DR STRING; 381666.H16_A1443; -.
DR EnsemblBacteria; CAJ92578; CAJ92578; H16_A1443.
DR GeneID; 57643542; -.
DR KEGG; reh:H16_A1443; -.
DR PATRIC; fig|381666.6.peg.1832; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_4_4; -.
DR OMA; YRPPAHW; -.
DR OrthoDB; 1710586at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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..322
FT /note="tRNA-dihydrouridine(16) synthase"
FT /id="PRO_0000162107"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 8..10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT BINDING 140
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 36
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 96
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 177
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 276
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 278
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 283
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT SITE 299
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT CONFLICT 284
FT /note="L -> F (in Ref. 1; AAC38320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 34780 MW; 71B430FF3AFFCCE1 CRC64;
MSRLFLAPME GLADYVLRDV LTDTGGYDGC VSEFVRVTGS LLPARVYERE TPEILAGGYT
RSGTPMVIQL LGSDPEWLAR NAAYAATLSP HGIDLNFGCP AKVVNRHGGG AMLLTNPELL
NRIVASVRAA VPAHIAVTAK MRLGVSDASL AIDCATALAE GGAASLVVHA RTRDHGYRPP
AHWDWIARIA AAVDVPVIAN GDVWTVADWE RCRAVSGCAD VMIGRGAVSD PFLALRIRGL
MDGSPSDQEW PLVLRQIATY LKKLHARIAS CHEHGRVKLW LSYLKRTWPQ AAELHAAIRR
MQDSLEIERV LEGLPGAATA PE
