A0A3Q0S6N8 · A0A3Q0S6N8_AMPCI

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

TypeIDPosition(s)Description
Binding site90ATP (UniProtKB | ChEBI)
Binding site111ATP (UniProtKB | ChEBI)
Binding site118-122ATP (UniProtKB | ChEBI)
Binding site135ATP (UniProtKB | ChEBI)
Binding site179-180ATP (UniProtKB | ChEBI)
Binding site220Zn2+ (UniProtKB | ChEBI)
Binding site223Zn2+ (UniProtKB | ChEBI)
Active site237Glycyl thioester intermediate; for adenylyltransferase activity
Binding site295Zn2+ (UniProtKB | ChEBI)
Binding site298Zn2+ (UniProtKB | ChEBI)
Active site410Cysteine persulfide intermediate; for sulfurtransferase activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionmolybdopterin-synthase adenylyltransferase activity
Molecular Functionmolybdopterin-synthase sulfurtransferase activity
Molecular Functionthiosulfate sulfurtransferase activity
Molecular FunctionURM1 activating enzyme activity
Biological ProcessMo-molybdopterin cofactor biosynthetic process
Biological Processprotein urmylation
Biological ProcesstRNA wobble position uridine thiolation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylyltransferase and sulfurtransferase MOCS3
  • Alternative names
    • Molybdenum cofactor synthesis protein 3

Including 2 domains:

  • Recommended name
    Molybdopterin-synthase adenylyltransferase
  • EC number
  • Alternative names
    • Adenylyltransferase MOCS3
    • Sulfur carrier protein MOCS2A adenylyltransferase
  • Recommended name
    Molybdopterin-synthase sulfurtransferase
  • EC number
  • Alternative names
    • Sulfurtransferase MOCS3
    • Sulfur carrier protein MOCS2A sulfurtransferase

Gene names

    • Name
      MOCS3
    • Synonyms
      UBA4

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Cichlomorphae > Cichliformes > Cichlidae > New World cichlids > Cichlasomatinae > Heroini > Amphilophus

Accessions

  • Primary accession
    A0A3Q0S6N8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond314↔322Alternate

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for coiled coil, domain.

TypeIDPosition(s)Description
Coiled coil1-35
Domain345-455Rhodanese

Sequence similarities

In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    457
  • Mass (Da)
    50,010
  • Last updated
    2019-04-10 v1
  • Checksum
    593F38DB5CBB129D
LSAMAQEVRSLKAQLSDKEKEIAALKSKLSHASSLELHHEVTALTPLTGRSALSNEDIMRYSRQLLLPQLGVQGQLNLSRTSVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDEVELSNLHRQVLHGEENQGQAKALSAASAVQRLNSTVECIPYRLQLSPENALQLIQQYDIVADCSDNVPTRYLVNDACVLSGKPLVSASALRMEGQLTVYNYRGGPCYRCLYPVPPPPETVTNCSDGGVLGVVPGIMGCFQALEVLKIASGKSSSCGQQLVMFDAEDARFRSIRLRPKQAGCAACGENPSVTRLLDYEAFCGSAATDKCRKLNVLSEHQRITVQDYKSIMDSAEPHLLLDVRPLVEVDICRLPFSLNIPLSSLQERKPEHLQLLQERISQLKQQMAGDCRPPVYVICKQGNDSQKAVQILERLSGSEVERVTVKDISGGLMAWARRIEHTFPQY

Genome annotation databases

Similar Proteins

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