UniProtKB - P32695 (DUSA_ECOLI)
Protein
tRNA-dihydrouridine(20/20a) synthase
Gene
dusA
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. Specifically modifies U20 and U20a in tRNAs.UniRule annotation1 Publication2 Publications
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
Catalytic activityi
- 5,6-dihydrouridine20 in tRNA + NADP+ = H+ + NADPH + uridine20 in tRNAUniRule annotation2 PublicationsEC:1.3.1.91UniRule annotation2 Publications
- EC:1.3.1.91UniRule annotation2 Publications
- 5,6-dihydrouridine20a in tRNA + NADP+ = H+ + NADPH + uridine20a in tRNAUniRule annotation1 Publication
- 5,6-dihydrouridine20a in tRNA + NAD+ = H+ + NADH + uridine20a in tRNAUniRule annotation1 Publication
Cofactori
FMNUniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 84 | FMNUniRule annotation | 1 | |
Sitei | 111 | Interacts with tRNAUniRule annotation | 1 | |
Active sitei | 114 | Proton donorUniRule annotation | 1 | |
Binding sitei | 153 | FMNUniRule annotation | 1 | |
Binding sitei | 186 | FMNUniRule annotation | 1 | |
Sitei | 198 | Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation | 1 | |
Sitei | 201 | Interacts with tRNAUniRule annotation | 1 | |
Sitei | 314 | Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation | 1 | |
Sitei | 317 | Interacts with tRNA; defines subfamily-specific binding signatureUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 32 – 34 | FMNUniRule annotation | 3 | |
Nucleotide bindingi | 226 – 228 | FMNUniRule annotation | 3 | |
Nucleotide bindingi | 248 – 249 | FMNUniRule annotation | 2 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: InterPro
- FMN binding Source: UniProtKB-UniRule
- tRNA binding Source: UniProtKB-UniRule
- tRNA-dihydrouridine20 synthase activity Source: UniProtKB-EC
- tRNA dihydrouridine synthase activity Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase, RNA-binding, tRNA-binding |
Biological process | tRNA processing |
Ligand | Flavoprotein, FMN, NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11932-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 |
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 (PubMed:11983710). Cells lacking this gene can introduce D modification at neither 20 or 20a in tRNA (PubMed:22123979).2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 114 | C → A: Loss of enzymatic activity; when associated with Ala-153. 1 Publication | 1 | |
Mutagenesisi | 153 | K → A: Loss of the ability to bind FMN. Loss of enzymatic activity; when associated with Ala-114. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162063 | 1 – 345 | tRNA-dihydrouridine(20/20a) synthaseAdd BLAST | 345 |
Proteomic databases
jPOSTi | P32695 |
PaxDbi | P32695 |
PRIDEi | P32695 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 4259608, 5 interactors |
STRINGi | 511145.b4049 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0042, Bacteria |
HOGENOMi | CLU_013299_2_1_6 |
InParanoidi | P32695 |
Family and domain databases
CDDi | cd02801, DUS_like_FMN, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_02041, DusA_subfam, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR035587, DUS-like_FMN-bd IPR001269, DUS_fam IPR004653, DusA IPR018517, tRNA_hU_synthase_CS |
PANTHERi | PTHR42907, PTHR42907, 1 hit |
Pfami | View protein in Pfam PF01207, Dus, 1 hit |
PIRSFi | PIRSF006621, Dus, 1 hit |
TIGRFAMsi | TIGR00742, yjbN, 1 hit |
PROSITEi | View protein in PROSITE PS01136, UPF0034, 1 hit |
i Sequence
Sequence statusi: Complete.
P32695-1 [UniParc]FASTAAdd to basket
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
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 |
RefSeqi | NP_418473.3, NC_000913.3 WP_001298868.1, NZ_STEB01000022.1 |
Genome annotation databases
EnsemblBacteriai | AAC77019; AAC77019; b4049 BAE78051; BAE78051; BAE78051 |
GeneIDi | 948558 |
KEGGi | ecj:JW5950 eco:b4049 |
PATRICi | fig|511145.12.peg.4167 |
Similar proteinsi
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 |
RefSeqi | NP_418473.3, NC_000913.3 WP_001298868.1, NZ_STEB01000022.1 |
3D structure databases
SMRi | P32695 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4259608, 5 interactors |
STRINGi | 511145.b4049 |
Proteomic databases
jPOSTi | P32695 |
PaxDbi | P32695 |
PRIDEi | P32695 |
Genome annotation databases
EnsemblBacteriai | AAC77019; AAC77019; b4049 BAE78051; BAE78051; BAE78051 |
GeneIDi | 948558 |
KEGGi | ecj:JW5950 eco:b4049 |
PATRICi | fig|511145.12.peg.4167 |
Organism-specific databases
EchoBASEi | EB1876 |
Phylogenomic databases
eggNOGi | COG0042, Bacteria |
HOGENOMi | CLU_013299_2_1_6 |
InParanoidi | P32695 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11932-MONOMER MetaCyc:EG11932-MONOMER |
Miscellaneous databases
PROi | PR:P32695 |
Family and domain databases
CDDi | cd02801, DUS_like_FMN, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_02041, DusA_subfam, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR035587, DUS-like_FMN-bd IPR001269, DUS_fam IPR004653, DusA IPR018517, tRNA_hU_synthase_CS |
PANTHERi | PTHR42907, PTHR42907, 1 hit |
Pfami | View protein in Pfam PF01207, Dus, 1 hit |
PIRSFi | PIRSF006621, Dus, 1 hit |
TIGRFAMsi | TIGR00742, yjbN, 1 hit |
PROSITEi | View protein in PROSITE PS01136, UPF0034, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DUSA_ECOLI | |
Accessioni | P32695Primary (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: | April 7, 2021 | |
This is version 145 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families