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Database: UniProt
Entry: A0A1D8FZZ1_9ACTN
LinkDB: A0A1D8FZZ1_9ACTN
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ID   A0A1D8FZZ1_9ACTN        Unreviewed;       378 AA.
AC   A0A1D8FZZ1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   Name=dus {ECO:0000313|EMBL:AOT58771.1};
GN   ORFNames=A4G23_01590 {ECO:0000313|EMBL:AOT58771.1};
OS   Streptomyces rubrolavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT58771.1, ECO:0000313|Proteomes:UP000095349};
RN   [1] {ECO:0000313|EMBL:AOT58771.1, ECO:0000313|Proteomes:UP000095349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJM4426 {ECO:0000313|EMBL:AOT58771.1,
RC   ECO:0000313|Proteomes:UP000095349};
RA   Kim J.-G.;
RT   "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002790,
CC       ECO:0000256|PIRNR:PIRNR006621}.
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:0000256|ARBA:ARBA00001387};
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:0000256|ARBA:ARBA00001183};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP017316; AOT58771.1; -; Genomic_DNA.
DR   RefSeq; WP_037939195.1; NZ_CP017316.1.
DR   AlphaFoldDB; A0A1D8FZZ1; -.
DR   STRING; 285473.A4G23_01590; -.
DR   KEGG; srn:A4G23_01590; -.
DR   PATRIC; fig|285473.5.peg.1649; -.
DR   OrthoDB; 9764501at2; -.
DR   Proteomes; UP000095349; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
DR   InterPro; IPR004652; DusB-like.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   NCBIfam; TIGR00737; nifR3_yhdG; 1.
DR   PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          20..321
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   378 AA;  40670 MW;  B6E6A33B8C837F83 CRC64;
     MTAFSPLSIG PHTVLPPVVL APMAGITNAP FRTLCREFSG GRGLFVSEMI TTRALVERNE
     KTMQLIHFDA TETPRSIQLY GVDPVTVGKA VRMIVDEDLA DHIDLNFGCP VPKVTRKGGG
     SALPFKRPLL RAILHEAVTN AGDLPVTMKM RKGIDDDHLT YLDAGRIAVE EGVTAIALHG
     RTAAQHYGGT ADWDAIARLK EHVPEIPVLG NGDIWSAGDA LRMMRETGCD GVVVGRGCLG
     RPWLFGDLVA AFEGTGAAAA PTLREVADVM VRHARLLGEW IGDESRGVID FRKHVAWYLK
     GFAVGSEMRR RLAVTSSLDE LRAGLDELDL GQPWPAGADG PRGRTSGNNR VVLPDGWLKD
     PWDCSAVSAD AELDTSGG
//
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