A0A3Q0S6N8 · A0A3Q0S6N8_AMPCI
- ProteinAdenylyltransferase and sulfurtransferase MOCS3
- GeneMOCS3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids457 (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 | 90 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 111 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 118-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SNLHR | ||||||
Binding site | 135 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 179-180 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DN | ||||||
Binding site | 220 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 223 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 237 | Glycyl thioester intermediate; for adenylyltransferase activity | ||||
Sequence: C | ||||||
Binding site | 295 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 298 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 410 | 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 | 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 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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Cichlomorphae > Cichliformes > Cichlidae > New World cichlids > Cichlasomatinae > Heroini > Amphilophus
Accessions
- Primary accessionA0A3Q0S6N8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 314↔322 | Alternate | ||||
Sequence: CGSAATDKC |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 1-35 | |||||
Sequence: LSAMAQEVRSLKAQLSDKEKEIAALKSKLSHASSL | ||||||
Domain | 345-455 | Rhodanese | ||||
Sequence: SAEPHLLLDVRPLVEVDICRLPFSLNIPLSSLQERKPEHLQLLQERISQLKQQMAGDCRPPVYVICKQGNDSQKAVQILERLSGSEVERVTVKDISGGLMAWARRIEHTFP |
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
- Length457
- Mass (Da)50,010
- Last updated2019-04-10 v1
- Checksum593F38DB5CBB129D