A0A8J8VWY7 · A0A8J8VWY7_9EURO
- ProteinAdenylyltransferase and sulfurtransferase uba4
- Geneuba4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids483 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
Catalytic activity
- [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H+ = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
Cofactor biosynthesis; molybdopterin biosynthesis.
tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 98 | ATP (UniProtKB | ChEBI) | |||
Binding site | 119 | ATP (UniProtKB | ChEBI) | |||
Binding site | 126-130 | ATP (UniProtKB | ChEBI) | |||
Binding site | 143 | ATP (UniProtKB | ChEBI) | |||
Binding site | 187-188 | ATP (UniProtKB | ChEBI) | |||
Binding site | 236 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 239 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 253 | Glycyl thioester intermediate; for adenylyltransferase activity | |||
Binding site | 314 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 317 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 436 | Cysteine persulfide intermediate; for sulfurtransferase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenylyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | thiosulfate sulfurtransferase activity | |
Molecular Function | URM1 activating enzyme activity | |
Biological Process | Mo-molybdopterin cofactor biosynthetic process | |
Biological Process | protein urmylation | |
Biological Process | tRNA wobble position uridine thiolation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylyltransferase and sulfurtransferase uba4
- Alternative names
Including 2 domains:
- Recommended nameMolybdopterin-synthase adenylyltransferase
- EC number
- Alternative names
- Recommended nameMolybdopterin-synthase sulfurtransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A8J8VWY7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Coiled coil | 8-49 | ||||
Domain | 375-481 | Rhodanese | |||
Sequence similarities
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length483
- Mass (Da)52,509
- Last updated2022-05-25 v1
- Checksum012307E7D057EE5E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
WIWV01000133 EMBL· GenBank· DDBJ | KAF7713098.1 EMBL· GenBank· DDBJ | Genomic DNA |