A0A8T0TFK0 · A0A8T0TFK0_PANVG

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

Type
IDPosition(s)Description
Binding site117ATP (UniProtKB | ChEBI)
Binding site138ATP (UniProtKB | ChEBI)
Binding site145-149ATP (UniProtKB | ChEBI)
Binding site162ATP (UniProtKB | ChEBI)
Binding site206-207ATP (UniProtKB | ChEBI)
Binding site247Zn2+ (UniProtKB | ChEBI)
Binding site250Zn2+ (UniProtKB | ChEBI)
Active site264Glycyl thioester intermediate; for adenylyltransferase activity
Binding site322Zn2+ (UniProtKB | ChEBI)
Binding site325Zn2+ (UniProtKB | ChEBI)
Active site438Cysteine persulfide intermediate; for sulfurtransferase activity

GO annotations

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

Keywords

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
      CNX5
      , UBA4
    • ORF names
      PVAP13_4KG056799

Organism names

  • Taxonomic identifier
  • Strain
    • AP13
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Panicodae > Paniceae > Panicinae > Panicum > Panicum sect. Hiantes

Accessions

  • Primary accession
    A0A8T0TFK0

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for coiled coil, domain.

Type
IDPosition(s)Description
Coiled coil11-38
Domain377-478Rhodanese

Sequence similarities

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    480
  • Mass (Da)
    51,733
  • Last updated
    2022-10-12 v1
  • Checksum
    FDE95D918DCBD1E9
MDGGRRGGGRREAIEKELNKLRAEREELDGRIRLLESQLEVGPEGVDGAAAVEGAVDGSCDGGVACRRRSANGFAPDGGLPADMIYRYSRHLLLPDFGVEGQRKLSQSSILVVGAGGLGSPVALYLAACGVGCLGIVDGDDVELNNLHRQIIHKEAYLGQPKVKSAADACREINSFIKVVDHHHTLKPCNALEIVRKYDIVVDATDNLPTRYMISDCCVLLNKPLVSGAALGLEGQLTVYHHNGSPCYRCLFPSPPPVAACQRCSDSGVLGVVPGVIGCLQALEAIKVATAVGEPLCGRMLLFDALSARIRIVKLRGSLPDCTICGENSVFTEQDFQKFDYEHFTQSPMSDKTAPSVNLLPENARITSRDYKRLVNNGEPHLLLDVRPTHHFQIASISRSLNIPLSMLEEKLPTLKTLLKETGAASASGKEPALVVLCRRGNDSQRAVQLLHDNGFASAKDIIGGLQAWGQDVDPDFPVY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM029043
EMBL· GenBank· DDBJ
KAG2609730.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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