A0A7T6XMG6 · A0A7T6XMG6_PENDI

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

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 site97ATP (UniProtKB | ChEBI)
Binding site118ATP (UniProtKB | ChEBI)
Binding site125-129ATP (UniProtKB | ChEBI)
Binding site142ATP (UniProtKB | ChEBI)
Binding site186-187ATP (UniProtKB | ChEBI)
Binding site235Zn2+ (UniProtKB | ChEBI)
Binding site238Zn2+ (UniProtKB | ChEBI)
Active site252Glycyl thioester intermediate; for adenylyltransferase activity
Binding site322Zn2+ (UniProtKB | ChEBI)
Binding site325Zn2+ (UniProtKB | ChEBI)
Active site451Cysteine 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 Processprotein urmylation
Biological ProcesstRNA wobble position uridine thiolation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylyltransferase and sulfurtransferase uba4
  • Alternative names
    • Common component for nitrate reductase and xanthine dehydrogenase protein F
    • Ubiquitin-like protein activator 4

Including 2 domains:

  • Recommended name
    Molybdopterin-synthase adenylyltransferase
  • EC number
  • Alternative names
    • Adenylyltransferase uba4
    • Sulfur carrier protein MOCS2A adenylyltransferase
  • Recommended name
    Molybdopterin-synthase sulfurtransferase
  • EC number
  • Alternative names
    • Sulfurtransferase uba4
    • Sulfur carrier protein MOCS2A sulfurtransferase

Gene names

    • Name
      uba4
    • Synonyms
      cnxF
    • ORF names
      Pdw03_7869

Organism names

  • Taxonomic identifier
  • Strain
    • PdW03
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A7T6XMG6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for coiled coil, domain.

Type
IDPosition(s)Description
Coiled coil8-42
Domain378-496Rhodanese

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
    498
  • Mass (Da)
    53,783
  • Last updated
    2021-06-02 v1
  • Checksum
    F646BDC77978F682
MGSFNETCASLRAQIIATEAQLTELKRDLANAEQAARSETATAAEIHPEDQKVEVRQWPLLQEEYKRYGRQMIVPQVGLNGQLKLRSAKVLLVGAGGLGCPAAQYLAGAGVGTIGLIDGDSVEVSNLHRQVLHRSKNVGKYKVDSAIESLRELNPHLTYIPHRTHLSPETAAAVFQEYDIILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRAPGDKSGGPCYRCVFPKPPPADSVVSCADGGIIGPVVGTMGVLQALEAIKVITVPDIDGGFDMSAARPRDHPSLHIFSAYSSPLVRTIRLRSRRANCAVCSAGATVTLDTIKSGSTDYVFFCGSANPPSLLGPEERISAREYNERHPNLTSDSPQLHTIIDVRDEAQFGICSLKNSINIPISNILSSGYGATLQGCDNGPQAAQLPSWLPSEVVSPESTNPIYVVCRLGNDSQIVVKKMKELGLDQHGKRFIGDIRGGLRSWREQVDSSWPEY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP060776
EMBL· GenBank· DDBJ
QQK43968.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help