Gene Ontology annotation through association of InterPro records with GO terms

Gene Ontology annotation based on Enzyme Commission mapping

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

GO_REF:0000116

Automatic Gene Ontology annotation based on Rhea mapping

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:11983710

Identification of the tRNA-dihydrouridine synthase family.

Deletion of the three E. coli COG0042 genes (dusA/yjbN, dusB/yhdG, dusC/yohI) showed that this family makes dihydrouridine in tRNA, with non-redundant site-specific roles.

PMID:22123979

Molecular basis of dihydrouridine formation on tRNA.

Crystal structures of Thermus thermophilus Dus (the D20/D20a enzyme) with tRNA show FMN as cofactor, U20 stacked on the flavin, and C5 of U20 cross-linked to the catalytic Cys93.

PMID:25902496

Major reorientation of tRNA substrates defines specificity of dihydrouridine synthases.

DusA and DusC bind tRNA in almost reversed orientations, set by subfamily-specific binding-signature residues, which explains their U20 versus U16 specificity.

PMID:29294097

Unveiling structural and functional divergences of bacterial tRNA dihydrouridine synthases: perspectives on the evolution scenario.

In E. coli, DusA is the U20/U20a bi-site enzyme, while DusB and DusC make D17 and D16.

"DusC and DusB are mono-site specific flavoenzymes involved in D16 and D17 biosynthesis, respectively, while DusA is a U20/U20a bi-site specific enzyme"

PMID:39460624

Differential redox sensitivity of tRNA dihydrouridylation.

DusA is the most active of the three E. coli Dus enzymes in vivo and in vitro, and Dus activity depends on NADPH availability.

"revealing DusA as the most active enzyme, followed by DusB"

PMID:42080256

The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.

E. coli DusA binds tRNA in a two-step mechanism, prefers pre-modified tRNA, and improves translation at specific codons.

PMID:25883135

A novel family of integrases associated with prophages and genomic islands integrated within the tRNA-dihydrouridine synthase A (dusA) gene.

dusA-associated integrases insert genomic islands at the 5' end of dusA, and the island supplies a new 5' end for the gene.

"The 5′ portion of the dusA gene affected by the integration is replaced by a new 5′ end (white) provided by the GEI"

PMID:35315701

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries.

Brucella ovis BOV_RS04255 (dusA; 56.4% identical to the query per the KBase dashboard PaperBLAST panel; same order) is assigned as a tRNA dihydrouridine20/20a synthase in a curated flavoproteome.

PMID:36551188

Evolutionary Diversity of Dus2 Enzymes Reveals Novel Structural and Functional Features among Members of the RNA Dihydrouridine Synthases Family.

file:RHIME/dusA/dusA-uniprot.txt

UniProtKB entry Q92P85 (SMc04235)

file:RHIME/dusA/dusA-bioinformatics/RESULTS.md

dusA gene model, upstream context and residue conservation analysis

The KBase protein NZ_RPHN01000062.1_55 contains Q92P85 exactly as residues 40-398; Q92P85 is N-terminally truncated relative to RefSeq WP_015241224.1 and lacks the residue equivalent to E. coli DusA FMN-binding Pro32.
Q92P85 conserves the E. coli DusA catalytic Cys114 (as Cys83), the FMN-binding residues and the subfamily tRNA-binding signature (53.1% identity).