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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)

 B5F1R2_SALA4            Unreviewed;       332 AA.
B5F1R2;
14-OCT-2008, integrated into UniProtKB/TrEMBL.
14-OCT-2008, sequence version 1.
05-DEC-2018, entry version 62.
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=SeAg_B4500 {ECO:0000313|EMBL:ACH48684.1};
Salmonella agona (strain SL483).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH48684.1, ECO:0000313|Proteomes:UP000008819};
[1] {ECO:0000313|EMBL:ACH48684.1, ECO:0000313|Proteomes:UP000008819}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SL483 {ECO:0000313|EMBL:ACH48684.1,
ECO:0000313|Proteomes:UP000008819};
PubMed=21602358; DOI=10.1128/JB.00297-11;
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
Leclerc J.E., Ravel J., Cebula T.A.;
"Comparative genomics of 28 Salmonella enterica isolates: evidence for
CRISPR-mediated adaptive sublineage evolution.";
J. Bacteriol. 193:3556-3568(2011).
-!- 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:
Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
EC=1.3.1.91; Evidence={ECO:0000256|HAMAP-Rule:MF_02041};
-!- CATALYTIC ACTIVITY:
Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-
COMP:13535, Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:65315,
ChEBI:CHEBI:74443; EC=1.3.1.90; Evidence={ECO:0000256|HAMAP-
Rule:MF_02041};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|HAMAP-Rule:MF_02041,
ECO:0000256|PIRNR:PIRNR006621};
-!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
{ECO:0000256|HAMAP-Rule:MF_02041}.
-!- SIMILARITY: Belongs to the dus family.
{ECO:0000256|PIRNR:PIRNR006621}.
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EMBL; CP001138; ACH48684.1; -; Genomic_DNA.
RefSeq; WP_001182229.1; NC_011149.1.
EnsemblBacteria; ACH48684; ACH48684; SeAg_B4500.
KEGG; sea:SeAg_B4500; -.
HOGENOM; HOG000259834; -.
KO; K05539; -.
OMA; TFIIHAR; -.
Proteomes; UP000008819; 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.
PIRSF; PIRSF006621; Dus; 1.
TIGRFAMs; TIGR00742; yjbN; 1.
PROSITE; PS01136; UPF0034; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000008819};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02041,
ECO:0000256|PIRNR:PIRNR006621};
FMN {ECO:0000256|HAMAP-Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621};
NADP {ECO:0000256|HAMAP-Rule:MF_02041};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02041,
ECO:0000256|PIRNR:PIRNR006621, ECO:0000313|EMBL:ACH48684.1};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_02041};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_02041,
ECO:0000256|PIRNR:PIRNR006621};
tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 19 21 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 213 215 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
NP_BIND 235 236 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
ACT_SITE 101 101 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_02041,
ECO:0000256|PIRSR:PIRSR006621-1}.
BINDING 71 71 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
BINDING 140 140 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
BINDING 173 173 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 98 98 Interacts with tRNA. {ECO:0000256|HAMAP-
Rule:MF_02041}.
SITE 185 185 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 188 188 Interacts with tRNA. {ECO:0000256|HAMAP-
Rule:MF_02041}.
SITE 301 301 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SITE 304 304 Interacts with tRNA; defines subfamily-
specific binding signature.
{ECO:0000256|HAMAP-Rule:MF_02041}.
SEQUENCE 332 AA; 36971 MW; 90EDB0F49E4208F7 CRC64;
MQPETQSSAL PAYRFSIAPM LDWTDRHCRY FLRLLSRQTL LYTEMVTTGA IIHGKGDYLA
YSEEEHPVAL QLGGSDPAQL AHCAKLAEAR GYDEINLNVG CPSDRVQNGM FGACLMGNAQ
LVADCVKAMR DVVSIPVTVK TRIGIDDQDS YAFLCDFIDT VSGQGECEMF IIHARKAWLS
GLSPKENREI PPLDYPRVYQ LKRDFPHLTM SINGGIKSLE EAKEHLRHMD GVMVGREAYQ
NPGILAAVDR EIFGADTTDA DPVAVVRAMY PYIERELSQG AYLGHITRHM LGLFQGIPGA
RQWRRYLSEN AHKAGADVAV LEQALKLVAD KR


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