A0A2I0A4S2 · A0A2I0A4S2_9ASPA
- ProteinAdenylyltransferase and sulfurtransferase MOCS3
- GeneMOCS3-2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids473 (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.
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 | 108 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 129 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 136-140 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NNLHR | ||||||
Binding site | 153 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 197-198 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DN | ||||||
Binding site | 238 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 241 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 255 | Glycyl thioester intermediate; for adenylyltransferase activity | ||||
Sequence: C | ||||||
Binding site | 313 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 316 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 431 | Cysteine persulfide intermediate; for sulfurtransferase activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | molybdopterin-synthase adenylyltransferase activity | |
Molecular Function | molybdopterin-synthase sulfurtransferase activity | |
Molecular Function | thiosulfate sulfurtransferase activity | |
Molecular Function | URM1 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 MOCS3
- 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 > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Orchidaceae > Apostasioideae > Apostasia
Accessions
- Primary accessionA0A2I0A4S2
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 10-44 | |||||
Sequence: YADIIREIEKLKVEKEEIENRISKLEAQLDRKPDE | ||||||
Domain | 371-471 | Rhodanese | ||||
Sequence: EHEEHVLLDVRPAHHFRITAIPGSINLPLSVLVENISSIDSALKAAVPEASGEAASLYVVCRRGNDSQRAVECLRKNGFPLAKDIIGGLEAWSRDVDPSFP |
Sequence similarities
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)51,340
- Last updated2018-02-28 v1
- Checksum5A9BCF8B89A23CC0
Keywords
- Technical term