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tRNA-dihydrouridine(20/20a) synthase (EC 1.3.1.-) (EC 1.3.1.91) (U20-specific dihydrouridine synthase) (U20-specific Dus) (tRNA-dihydrouridine synthase A)

 F4AHR9_GLAS4            Unreviewed;       345 AA.
F4AHR9;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 39.
RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041};
EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02041};
EC=1.3.1.91 {ECO:0000256|HAMAP-Rule:MF_02041};
AltName: Full=U20-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02041};
Short=U20-specific Dus {ECO:0000256|HAMAP-Rule:MF_02041};
AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000256|HAMAP-Rule:MF_02041};
Name=dusA {ECO:0000256|HAMAP-Rule:MF_02041};
OrderedLocusNames=Glaag_0237 {ECO:0000313|EMBL:AEE21206.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE21206.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE21206.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE21206.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a
modified base found in the D-loop of most tRNAs, via the reduction
of the C5-C6 double bond in target uridines. Specifically modifies
U20 and U20a in tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}.
-!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20) in tRNA + NAD(P)(+) =
uracil(20) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}.
-!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) =
uracil(20a) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
-!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
{ECO:0000256|HAMAP-Rule:MF_02041}.
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EMBL; CP002526; AEE21206.1; -; Genomic_DNA.
RefSeq; WP_013752599.1; NC_015497.1.
STRING; 983545.Glaag_0237; -.
EnsemblBacteria; AEE21206; AEE21206; Glaag_0237.
KEGG; gag:Glaag_0237; -.
eggNOG; ENOG4105CEH; Bacteria.
eggNOG; COG0042; LUCA.
KO; K05539; -.
OrthoDB; POG091H068N; -.
BioCyc; GSP983545:GH3Q-243-MONOMER; -.
Proteomes; UP000006544; Chromosome.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
CDD; cd02801; DUS_like_FMN; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_02041; DusA_subfam; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR035587; DUS-like_FMN-bd.
InterPro; IPR004653; DusA.
InterPro; IPR001269; tRNA_hU_synthase.
InterPro; IPR018517; tRNA_hU_synthase_CS.
PANTHER; PTHR42907; PTHR42907; 1.
Pfam; PF01207; Dus; 1.
TIGRFAMs; TIGR00742; yjbN; 1.
PROSITE; PS01136; UPF0034; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000006544};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02041};
FMN {ECO:0000256|HAMAP-Rule:MF_02041};
NADP {ECO:0000256|HAMAP-Rule:MF_02041};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02041};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_02041};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_02041};
tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 16 18 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 209 211 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 231 232 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
ACT_SITE 98 98 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_02041}.
BINDING 68 68 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
BINDING 137 137 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
BINDING 169 169 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 95 95 Interacts with tRNA. {ECO:0000256|HAMAP-
Rule:MF_02041}.
SITE 181 181 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 184 184 Interacts with tRNA. {ECO:0000256|HAMAP-
Rule:MF_02041}.
SITE 297 297 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 300 300 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SEQUENCE 345 AA; 38323 MW; 774AF79DFE3F007F CRC64;
MNTPSAPLNR TISVAPMLDW TDKHCRYFLR QISKHALLYT EMVTTGAIIF GKGDYLAFNE
AEHPVALQLG GSDPADMARC AVLAQERGYD EVNINVGCPS DRVQNGRFGA CLMAEPKTVA
DCINAMQKEV DIPVTVKSRI GIDDMDEYKD LTDFIQVIAD AGCEIFTVHA RKAWLKGLSP
KENRDIPPLM YDRVYALKEE FPHLNLSING GVKTLDDAAL HLDKLDGVMI GREVYSNPYI
LADVDKRFYQ DQTPVPSREE IVHAMLPYVE KQMASGARAW NIARHMLGLF QGQPGGRVWR
RYLSQHGTGQ SKNGLQVGPE LLVNALAAVN EARATAKAYQ DSRVS


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