UniProtKB - P0ABT5 (DUSB_ECOLI)
Protein
tRNA-dihydrouridine synthase B
Gene
dusB
Organism
Escherichia coli (strain K12)
Status
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
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
Catalytic activityi
- a 5,6-dihydrouridine in tRNA + NADP+ = a uridine in tRNA + H+ + NADPHUniRule annotationBy similarity
Cofactori
FMNUniRule annotationBy similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 70 | FMNUniRule annotationBy similarity | 1 | |
Active sitei | 100 | Proton donorUniRule annotationBy similarity | 1 | |
Binding sitei | 139 | FMNUniRule annotationBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 16 – 18 | FMNUniRule annotationBy similarity | 3 | |
Nucleotide bindingi | 200 – 202 | FMNUniRule annotationBy similarity | 3 | |
Nucleotide bindingi | 224 – 225 | FMNUniRule annotationBy similarity | 2 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: InterPro
- FMN binding Source: UniProtKB-UniRule
- tRNA binding Source: UniProtKB-UniRule
- tRNA dihydrouridine synthase activity Source: EcoCyc
GO - Biological processi
- response to radiation Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase, RNA-binding, tRNA-binding |
Biological process | tRNA processing |
Ligand | Flavoprotein, FMN, NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11311-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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162084 | 1 – 321 | tRNA-dihydrouridine synthase BAdd BLAST | 321 |
Proteomic databases
jPOSTi | P0ABT5 |
PaxDbi | P0ABT5 |
PRIDEi | P0ABT5 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 4261865, 16 interactors |
DIPi | DIP-48240N |
IntActi | P0ABT5, 4 interactors |
STRINGi | 511145.b3260 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ABT5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0042, Bacteria |
HOGENOMi | CLU_013299_0_1_6 |
InParanoidi | P0ABT5 |
PhylomeDBi | P0ABT5 |
Family and domain databases
CDDi | cd02801, DUS_like_FMN, 1 hit |
Gene3Di | 1.10.1200.80, 1 hit 3.20.20.70, 1 hit |
HAMAPi | MF_02042, DusB_subfam, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR035587, DUS-like_FMN-bd IPR032887, DusB IPR024036, tRNA-dHydroUridine_Synthase_C IPR004652, tRNA_dU_NifR3 IPR001269, tRNA_hU_synthase IPR018517, tRNA_hU_synthase_CS |
Pfami | View protein in Pfam PF01207, Dus, 1 hit |
PIRSFi | PIRSF006621, Dus, 1 hit |
TIGRFAMsi | TIGR00737, nifR3_yhdG, 1 hit |
PROSITEi | View protein in PROSITE PS01136, UPF0034, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ABT5-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 131 | A → R in CAA44270 (PubMed:1547773).Curated | 1 | |
Sequence conflicti | 267 | H → D in CAA44270 (PubMed:1547773).Curated | 1 |
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 |
PIRi | B47043 |
RefSeqi | NP_417726.1, NC_000913.3 WP_001219652.1, NZ_STEB01000012.1 |
Genome annotation databases
EnsemblBacteriai | AAC76292; AAC76292; b3260 BAE77301; BAE77301; BAE77301 |
GeneIDi | 52075159 947707 |
KEGGi | ecj:JW3228 eco:b3260 |
PATRICi | fig|1411691.4.peg.3468 |
Similar proteinsi
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 |
PIRi | B47043 |
RefSeqi | NP_417726.1, NC_000913.3 WP_001219652.1, NZ_STEB01000012.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6EI9 | X-ray | 2.55 | A/B | 1-321 | [»] | |
SMRi | P0ABT5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261865, 16 interactors |
DIPi | DIP-48240N |
IntActi | P0ABT5, 4 interactors |
STRINGi | 511145.b3260 |
Proteomic databases
jPOSTi | P0ABT5 |
PaxDbi | P0ABT5 |
PRIDEi | P0ABT5 |
Genome annotation databases
EnsemblBacteriai | AAC76292; AAC76292; b3260 BAE77301; BAE77301; BAE77301 |
GeneIDi | 52075159 947707 |
KEGGi | ecj:JW3228 eco:b3260 |
PATRICi | fig|1411691.4.peg.3468 |
Organism-specific databases
EchoBASEi | EB1287 |
Phylogenomic databases
eggNOGi | COG0042, Bacteria |
HOGENOMi | CLU_013299_0_1_6 |
InParanoidi | P0ABT5 |
PhylomeDBi | P0ABT5 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11311-MONOMER MetaCyc:EG11311-MONOMER |
Miscellaneous databases
PROi | PR:P0ABT5 |
Family and domain databases
CDDi | cd02801, DUS_like_FMN, 1 hit |
Gene3Di | 1.10.1200.80, 1 hit 3.20.20.70, 1 hit |
HAMAPi | MF_02042, DusB_subfam, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR035587, DUS-like_FMN-bd IPR032887, DusB IPR024036, tRNA-dHydroUridine_Synthase_C IPR004652, tRNA_dU_NifR3 IPR001269, tRNA_hU_synthase IPR018517, tRNA_hU_synthase_CS |
Pfami | View protein in Pfam PF01207, Dus, 1 hit |
PIRSFi | PIRSF006621, Dus, 1 hit |
TIGRFAMsi | TIGR00737, nifR3_yhdG, 1 hit |
PROSITEi | View protein in PROSITE PS01136, UPF0034, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DUSB_ECOLI | |
Accessioni | P0ABT5Primary (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: | December 2, 2020 | |
This is version 109 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families