Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA-dihydrouridine synthase B

Gene

dusB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.UniRule annotation1 Publication

Catalytic activityi

5,6-dihydrouracil in tRNA + NAD(P)+ = uracil in tRNA + NAD(P)H.UniRule annotationBy similarity

Cofactori

FMNUniRule annotationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70FMNUniRule annotationBy similarity1
Active sitei100Proton donorUniRule annotationBy similarity1
Binding sitei139FMNUniRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 18FMNUniRule annotationBy similarity3
Nucleotide bindingi200 – 202FMNUniRule annotationBy similarity3
Nucleotide bindingi224 – 225FMNUniRule annotationBy similarity2

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:EG11311-MONOMER.
ECOL316407:JW3228-MONOMER.
MetaCyc:EG11311-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine synthase B1 PublicationUniRule annotation (EC:1.3.1.-UniRule annotationCurated)
Gene namesi
Name:dusB1 PublicationUniRule annotation
Synonyms:yhdG
Ordered Locus Names:b3260, JW3228
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11311. dusB.

Subcellular locationi

GO - Cellular componenti

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001620841 – 321tRNA-dihydrouridine synthase BAdd BLAST321

Proteomic databases

PaxDbiP0ABT5.
PRIDEiP0ABT5.

Interactioni

Protein-protein interaction databases

BioGridi4261865. 8 interactors.
DIPiDIP-48240N.
IntActiP0ABT5. 4 interactors.
STRINGi511145.b3260.

Structurei

3D structure databases

ProteinModelPortaliP0ABT5.
SMRiP0ABT5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Dus family. DusB subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000217855.
InParanoidiP0ABT5.
KOiK05540.
OMAiWLFREIE.
PhylomeDBiP0ABT5.

Family and domain databases

Gene3Di1.10.1200.80. 1 hit.
3.20.20.70. 1 hit.
HAMAPiMF_02042. DusB_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR032887. DusB.
IPR024036. tRNA-dHydroUridine_Synthase_C.
IPR004652. tRNA_dU_NifR3.
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.
TIGRFAMsiTIGR00737. nifR3_yhdG. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIGQYQLRN RLIAAPMAGI TDRPFRTLCY EMGAGLTVSE MMSSNPQVWE
60 70 80 90 100
SDKSRLRMVH IDEPGIRTVQ IAGSDPKEMA DAARINVESG AQIIDINMGC
110 120 130 140 150
PAKKVNRKLA GSALLQYPDV VKSILTEVVN AVDVPVTLKI RTGWAPEHRN
160 170 180 190 200
CEEIAQLAED CGIQALTIHG RTRACLFNGE AEYDSIRAVK QKVSIPVIAN
210 220 230 240 250
GDITDPLKAR AVLDYTGADA LMIGRAAQGR PWIFREIQHY LDTGELLPPL
260 270 280 290 300
PLAEVKRLLC AHVRELHDFY GPAKGYRIAR KHVSWYLQEH APNDQFRRTF
310 320
NAIEDASEQL EALEAYFENF A
Length:321
Mass (Da):35,866
Last modified:October 25, 2005 - v1
Checksum:iB9A31AB459825DE5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131A → R in CAA44270 (PubMed:1547773).Curated1
Sequence conflicti267H → D in CAA44270 (PubMed:1547773).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62399 Genomic DNA. Translation: CAA44270.1.
M95784 Genomic DNA. Translation: AAA23782.1.
U18997 Genomic DNA. Translation: AAA58064.1.
U00096 Genomic DNA. Translation: AAC76292.1.
AP009048 Genomic DNA. Translation: BAE77301.1.
S67010 Genomic DNA. Translation: AAB28770.2.
J03816 Genomic DNA. No translation available.
J03245 Genomic DNA. Translation: AAA83855.1.
PIRiB47043.
RefSeqiNP_417726.1. NC_000913.3.
WP_001219652.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76292; AAC76292; b3260.
BAE77301; BAE77301; BAE77301.
GeneIDi947707.
KEGGiecj:JW3228.
eco:b3260.
PATRICi32121950. VBIEscCol129921_3359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62399 Genomic DNA. Translation: CAA44270.1.
M95784 Genomic DNA. Translation: AAA23782.1.
U18997 Genomic DNA. Translation: AAA58064.1.
U00096 Genomic DNA. Translation: AAC76292.1.
AP009048 Genomic DNA. Translation: BAE77301.1.
S67010 Genomic DNA. Translation: AAB28770.2.
J03816 Genomic DNA. No translation available.
J03245 Genomic DNA. Translation: AAA83855.1.
PIRiB47043.
RefSeqiNP_417726.1. NC_000913.3.
WP_001219652.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0ABT5.
SMRiP0ABT5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261865. 8 interactors.
DIPiDIP-48240N.
IntActiP0ABT5. 4 interactors.
STRINGi511145.b3260.

Proteomic databases

PaxDbiP0ABT5.
PRIDEiP0ABT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76292; AAC76292; b3260.
BAE77301; BAE77301; BAE77301.
GeneIDi947707.
KEGGiecj:JW3228.
eco:b3260.
PATRICi32121950. VBIEscCol129921_3359.

Organism-specific databases

EchoBASEiEB1287.
EcoGeneiEG11311. dusB.

Phylogenomic databases

eggNOGiENOG4105CEH. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000217855.
InParanoidiP0ABT5.
KOiK05540.
OMAiWLFREIE.
PhylomeDBiP0ABT5.

Enzyme and pathway databases

BioCyciEcoCyc:EG11311-MONOMER.
ECOL316407:JW3228-MONOMER.
MetaCyc:EG11311-MONOMER.

Miscellaneous databases

PROiP0ABT5.

Family and domain databases

Gene3Di1.10.1200.80. 1 hit.
3.20.20.70. 1 hit.
HAMAPiMF_02042. DusB_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR032887. DusB.
IPR024036. tRNA-dHydroUridine_Synthase_C.
IPR004652. tRNA_dU_NifR3.
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.
TIGRFAMsiTIGR00737. nifR3_yhdG. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUSB_ECOLI
AccessioniPrimary (citable) accession number: P0ABT5
Secondary accession number(s): P25717, Q2M8V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 84 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, 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.