S8C3F5 · S8C3F5_DACHA
- ProteinAdenylyltransferase and sulfurtransferase uba4
- Geneuba4
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids989 (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
Protein has several cofactor binding sites:
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 | 417 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C | ||||||
Binding site | 576 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 597 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 604-608 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SNLHR | ||||||
Binding site | 621 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 665-666 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DS | ||||||
Binding site | 708 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 711 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 725 | Glycyl thioester intermediate; for adenylyltransferase activity | ||||
Sequence: C | ||||||
Binding site | 815 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 818 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 944 | Cysteine persulfide intermediate; for sulfurtransferase activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | molybdopterin-synthase adenylyltransferase activity | |
Molecular Function | molybdopterin-synthase sulfurtransferase activity | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
Molecular Function | ubiquitin-like modifier activating enzyme activity | |
Biological Process | Mo-molybdopterin cofactor biosynthetic process | |
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Orbiliomycetes > Orbiliales > Orbiliaceae > Dactylellina
Accessions
- Primary accessionS8C3F5
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 506-535 | Disordered | ||||
Sequence: RSGSFASSNGTATEEPERDETEKLQEDENK | ||||||
Compositional bias | 518-535 | Basic and acidic residues | ||||
Sequence: TEEPERDETEKLQEDENK | ||||||
Region | 758-783 | Disordered | ||||
Sequence: KRRKPAHLSNDGTQADSAPTTNATTT | ||||||
Compositional bias | 767-783 | Polar residues | ||||
Sequence: NDGTQADSAPTTNATTT | ||||||
Domain | 868-987 | Rhodanese | ||||
Sequence: GNKGGLLIDVRDDVQYGMCSLEDSINVPITTILTLPIAREDKKEGEEGKEQEEEEVKPIPIPSWLPRDTSTPIYFICRLGNDSRLAVQRLKQSGLVKGNVIRDVRGGLWEWSRKVDKSFP |
Sequence similarities
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length989
- Mass (Da)110,679
- Last updated2013-10-16 v1
- ChecksumFC3AB81A8A4E262A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 518-535 | Basic and acidic residues | ||||
Sequence: TEEPERDETEKLQEDENK | ||||||
Compositional bias | 767-783 | Polar residues | ||||
Sequence: NDGTQADSAPTTNATTT |
Keywords
- Technical term