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Protein

tRNA-dihydrouridine(20/20a) synthase

Gene

dusA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication2 Publications

Catalytic activityi

5,6-dihydrouracil(20) in tRNA + NAD(P)+ = uracil(20) in tRNA + NAD(P)H.UniRule annotation2 Publications
5,6-dihydrouracil(20a) in tRNA + NAD(P)+ = uracil(20a) in tRNA + NAD(P)H.UniRule annotation1 Publication

Cofactori

FMNUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841FMNUniRule annotation
Sitei111 – 1111Interacts with tRNAUniRule annotation
Active sitei114 – 1141Proton donorUniRule annotation
Binding sitei153 – 1531FMNUniRule annotation
Binding sitei186 – 1861FMNUniRule annotation
Sitei198 – 1981Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation
Sitei201 – 2011Interacts with tRNAUniRule annotation
Sitei314 – 3141Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation
Sitei317 – 3171Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 343FMNUniRule annotation
Nucleotide bindingi226 – 2283FMNUniRule annotation
Nucleotide bindingi248 – 2492FMNUniRule annotation

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • FMN binding Source: UniProtKB-HAMAP
  • tRNA binding Source: UniProtKB-HAMAP
  • tRNA dihydrouridine synthase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Flavoprotein, FMN, NADP, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11932-MONOMER.
ECOL316407:JW5950-MONOMER.
MetaCyc:EG11932-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(20/20a) synthaseUniRule annotation1 Publication (EC:1.3.1.-UniRule annotation1 Publication, EC:1.3.1.91UniRule annotation2 Publications)
Alternative name(s):
U20-specific dihydrouridine synthase1 PublicationUniRule annotation
Short name:
U20-specific Dus1 PublicationUniRule annotation
tRNA-dihydrouridine synthase A1 PublicationUniRule annotation
Gene namesi
Name:dusA1 PublicationUniRule annotation
Synonyms:yjbN
Ordered Locus Names:b4049, JW5950
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11932. dusA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

A dusA dusB dusC triple mutant exhibits a complete lack of 5,6-dihydrouridine modification in cellular tRNA, whereas each single mutant exhibits a partial reduction, compared to wild type (PubMed:11983710). Cells lacking this gene can introduce D modification at neither 20 or 20a in tRNA (PubMed:22123979).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141C → A: Loss of enzymatic activity; when associated with Ala-153. 1 Publication
Mutagenesisi153 – 1531K → A: Loss of the ability to bind FMN. Loss of enzymatic activity; when associated with Ala-114. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345tRNA-dihydrouridine(20/20a) synthasePRO_0000162063Add
BLAST

Proteomic databases

PaxDbiP32695.
PRIDEiP32695.

Interactioni

Protein-protein interaction databases

BioGridi4259608. 5 interactions.
STRINGi511145.b4049.

Structurei

3D structure databases

ProteinModelPortaliP32695.
SMRiP32695. Positions 27-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Dus family. DusA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000259834.
InParanoidiP32695.
KOiK05539.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02041. DusA_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004653. DusA.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
TIGRFAMsiTIGR00742. yjbN. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGNSEMQKI NQTSAMPEKT DVHWSGRFSV APMLDWTDRH CRYFLRLLSR
60 70 80 90 100
NTLLYTEMVT TGAIIHGKGD YLAYSEEEHP VALQLGGSDP AALAQCAKLA
110 120 130 140 150
EARGYDEINL NVGCPSDRVQ NGMFGACLMG NAQLVADCVK AMRDVVSIPV
160 170 180 190 200
TVKTRIGIDD QDSYEFLCDF INTVSGKGEC EMFIIHARKA WLSGLSPKEN
210 220 230 240 250
REIPPLDYPR VYQLKRDFPH LTMSINGGIK SLEEAKAHLQ HMDGVMVGRE
260 270 280 290 300
AYQNPGILAA VDREIFGSSD TDADPVAVVR AMYPYIEREL SQGTYLGHIT
310 320 330 340
RHMLGLFQGI PGARQWRRYL SENAHKAGAD INVLEHALKL VADKR
Length:345
Mass (Da):38,468
Last modified:March 19, 2014 - v4
Checksum:i1FD687C1D0B764D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43143.1.
U00096 Genomic DNA. Translation: AAC77019.3.
AP009048 Genomic DNA. Translation: BAE78051.1.
RefSeqiNP_418473.3. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77019; AAC77019; b4049.
BAE78051; BAE78051; BAE78051.
GeneIDi948558.
KEGGiecj:JW5950.
eco:b4049.
PATRICi32123637. VBIEscCol129921_4167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43143.1.
U00096 Genomic DNA. Translation: AAC77019.3.
AP009048 Genomic DNA. Translation: BAE78051.1.
RefSeqiNP_418473.3. NC_000913.3.

3D structure databases

ProteinModelPortaliP32695.
SMRiP32695. Positions 27-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259608. 5 interactions.
STRINGi511145.b4049.

Proteomic databases

PaxDbiP32695.
PRIDEiP32695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77019; AAC77019; b4049.
BAE78051; BAE78051; BAE78051.
GeneIDi948558.
KEGGiecj:JW5950.
eco:b4049.
PATRICi32123637. VBIEscCol129921_4167.

Organism-specific databases

EchoBASEiEB1876.
EcoGeneiEG11932. dusA.

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000259834.
InParanoidiP32695.
KOiK05539.

Enzyme and pathway databases

BioCyciEcoCyc:EG11932-MONOMER.
ECOL316407:JW5950-MONOMER.
MetaCyc:EG11932-MONOMER.

Miscellaneous databases

PROiP32695.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02041. DusA_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004653. DusA.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
TIGRFAMsiTIGR00742. yjbN. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUSA_ECOLI
AccessioniPrimary (citable) accession number: P32695
Secondary accession number(s): P76786, Q2M6Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 19, 2014
Last modified: September 7, 2016
This is version 119 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

DusB and DusC together account for about half of the 5,6-dihydrouridine modification observed in wild-type cellular tRNA, and DusA accounts for the other half. These three enzymes seem to act site-specifically on the tRNA D-loop and contain nonredundant catalytic functions in vivo.1 Publication

Caution

The U21 position mentioned in PubMed:11983710 corresponds in fact to U20 with the conventional numbering.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.