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Protein

tRNA-dihydrouridine(16) synthase

Gene

dusC

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. DusC specifically modifies U16 in tRNAs.UniRule annotation2 Publications

Catalytic activityi

5,6-dihydrouracil(16) in tRNA + NAD(P)+ = uracil(16) in tRNA + NAD(P)H.UniRule annotation1 Publication

Cofactori

FMNUniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei35Interacts with tRNA; defines subfamily-specific binding signature1 Publication1
Binding sitei68FMNCombined sources2 Publications1
Sitei95Interacts with tRNA1 Publication1
Active sitei98Proton donorBy similarity1 Publication1
Binding sitei139FMNCombined sources2 Publications1
Sitei176Interacts with tRNA1 Publication1
Sitei272Interacts with tRNA; defines subfamily-specific binding signature1 Publication1
Sitei274Interacts with tRNA; defines subfamily-specific binding signature1 Publication1
Sitei279Interacts with tRNA1 Publication1
Sitei295Interacts with tRNA; defines subfamily-specific binding signature1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 9FMNCombined sources2 Publications3
Nucleotide bindingi200 – 202FMNCombined sources2 Publications3
Nucleotide bindingi224 – 225FMNCombined sources2 Publications2

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • FMN binding Source: UniProtKB
  • tRNA binding Source: UniProtKB
  • tRNA dihydrouridine synthase activity Source: UniProtKB

GO - Biological processi

  • tRNA dihydrouridine synthesis Source: UniProtKB
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:EG12022-MONOMER.
ECOL316407:JW2128-MONOMER.
MetaCyc:EG12022-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(16) synthaseUniRule annotation1 Publication (EC:1.3.1.-UniRule annotation1 Publication)
Alternative name(s):
U16-specific dihydrouridine synthase1 PublicationUniRule annotation
Short name:
U16-specific Dus1 PublicationUniRule annotation
tRNA-dihydrouridine synthase C1 PublicationUniRule annotation
Gene namesi
Name:dusC1 PublicationUniRule annotation
Synonyms:yohI
Ordered Locus Names:b2140, JW2128
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12022. dusC.

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98C → A: Loss of enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001621091 – 315tRNA-dihydrouridine(16) synthaseAdd BLAST315

Proteomic databases

PaxDbiP33371.
PRIDEiP33371.

Interactioni

Protein-protein interaction databases

BioGridi4260457. 10 interactors.
DIPiDIP-12808N.
IntActiP33371. 24 interactors.
STRINGi511145.b2140.

Structurei

Secondary structure

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Turni9 – 11Combined sources3
Helixi14 – 22Combined sources9
Beta strandi27 – 35Combined sources9
Beta strandi37 – 39Combined sources3
Helixi43 – 49Combined sources7
Helixi51 – 55Combined sources5
Beta strandi64 – 70Combined sources7
Helixi74 – 86Combined sources13
Beta strandi90 – 98Combined sources9
Helixi109 – 114Combined sources6
Helixi116 – 129Combined sources14
Beta strandi136 – 142Combined sources7
Beta strandi144 – 147Combined sources4
Helixi150 – 159Combined sources10
Beta strandi163 – 170Combined sources8
Turni173 – 176Combined sources4
Helixi178 – 180Combined sources3
Helixi183 – 192Combined sources10
Beta strandi197 – 201Combined sources5
Helixi206 – 216Combined sources11
Beta strandi219 – 224Combined sources6
Helixi225 – 229Combined sources5
Helixi233 – 239Combined sources7
Helixi246 – 258Combined sources13
Helixi268 – 280Combined sources13
Turni281 – 283Combined sources3
Helixi285 – 294Combined sources10
Helixi300 – 309Combined sources10
Turni312 – 314Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W9ZX-ray2.10A1-315[»]
4BF9X-ray2.60A1-315[»]
4BFAX-ray1.65A/B1-315[»]
4YCOX-ray2.10A/B/C1-315[»]
4YCPX-ray2.55A1-315[»]
ProteinModelPortaliP33371.
SMRiP33371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Is composed of two domains: an N-terminal catalytic domain (residues 1-242) and a C-terminal tRNA recognition domain (residues 245-309).2 Publications

Sequence similaritiesi

Belongs to the Dus family. DusC subfamily.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105FBT. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000217854.
InParanoidiP33371.
KOiK05541.
OMAiGGIDWCV.
PhylomeDBiP33371.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02043. DusC_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR032886. DusC.
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.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLLAPMEG VLDSLVRELL TEVNDYDLCI TEFVRVVDQL LPVKVFHRIC
60 70 80 90 100
PELQNASRTP SGTLVRVQLL GQFPQWLAEN AARAVELGSW GVDLNCGCPS
110 120 130 140 150
KTVNGSGGGA TLLKDPELIY QGAKAMREAV PAHLPVSVKV RLGWDSGEKK
160 170 180 190 200
FEIADAVQQA GATELVVHGR TKEQGYRAEH IDWQAIGDIR QRLNIPVIAN
210 220 230 240 250
GEIWDWQSAQ QCMAISGCDA VMIGRGALNI PNLSRVVKYN EPRMPWPEVV
260 270 280 290 300
ALLQKYTRLE KQGDTGLYHV ARIKQWLSYL RKEYDEATEL FQHVRVLNNS
310
PDIARAIQAI DIEKL
Length:315
Mass (Da):35,199
Last modified:February 1, 1994 - v1
Checksum:i83B33E5034E53565
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00007 Genomic DNA. Translation: AAA60503.1.
U00096 Genomic DNA. Translation: AAC75201.1.
AP009048 Genomic DNA. Translation: BAE76617.1.
PIRiC64982.
RefSeqiNP_416645.1. NC_000913.3.
WP_001264861.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75201; AAC75201; b2140.
BAE76617; BAE76617; BAE76617.
GeneIDi945458.
KEGGiecj:JW2128.
eco:b2140.
PATRICi32119623. VBIEscCol129921_2222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00007 Genomic DNA. Translation: AAA60503.1.
U00096 Genomic DNA. Translation: AAC75201.1.
AP009048 Genomic DNA. Translation: BAE76617.1.
PIRiC64982.
RefSeqiNP_416645.1. NC_000913.3.
WP_001264861.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W9ZX-ray2.10A1-315[»]
4BF9X-ray2.60A1-315[»]
4BFAX-ray1.65A/B1-315[»]
4YCOX-ray2.10A/B/C1-315[»]
4YCPX-ray2.55A1-315[»]
ProteinModelPortaliP33371.
SMRiP33371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260457. 10 interactors.
DIPiDIP-12808N.
IntActiP33371. 24 interactors.
STRINGi511145.b2140.

Proteomic databases

PaxDbiP33371.
PRIDEiP33371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75201; AAC75201; b2140.
BAE76617; BAE76617; BAE76617.
GeneIDi945458.
KEGGiecj:JW2128.
eco:b2140.
PATRICi32119623. VBIEscCol129921_2222.

Organism-specific databases

EchoBASEiEB1957.
EcoGeneiEG12022. dusC.

Phylogenomic databases

eggNOGiENOG4105FBT. Bacteria.
COG0042. LUCA.
HOGENOMiHOG000217854.
InParanoidiP33371.
KOiK05541.
OMAiGGIDWCV.
PhylomeDBiP33371.

Enzyme and pathway databases

BioCyciEcoCyc:EG12022-MONOMER.
ECOL316407:JW2128-MONOMER.
MetaCyc:EG12022-MONOMER.

Miscellaneous databases

PROiP33371.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_02043. DusC_subfam. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR032886. DusC.
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.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUSC_ECOLI
AccessioniPrimary (citable) accession number: P33371
Secondary accession number(s): Q2MAT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 115 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.