A0A6A6A987 · A0A6A6A987_9PLEO

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 site128ATP (UniProtKB | ChEBI)
Binding site149ATP (UniProtKB | ChEBI)
Binding site156-160ATP (UniProtKB | ChEBI)
Binding site173ATP (UniProtKB | ChEBI)
Binding site217-218ATP (UniProtKB | ChEBI)
Binding site266Zn2+ (UniProtKB | ChEBI)
Binding site269Zn2+ (UniProtKB | ChEBI)
Active site283Glycyl thioester intermediate; for adenylyltransferase activity
Binding site345Zn2+ (UniProtKB | ChEBI)
Binding site348Zn2+ (UniProtKB | ChEBI)
Active site478Cysteine 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 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
      P153DRAFT_48327

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 119687
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Dothidotthiaceae > Dothidotthia

Accessions

  • Primary accession
    A0A6A6A987

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias29-46Polar residues
Region29-53Disordered
Domain406-523Rhodanese

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    525
  • Mass (Da)
    56,764
  • Last updated
    2020-06-17 v1
  • Checksum
    C07C100A7B0B9AE4
MPIIASLHKQIASCEATLIQLRQQLSEAEHTQRQQQKASQQKKSTLDPLGHDMDYGVPDDFRAEVLHVLNHAEERDSQDVNGLAEQRRWPLEHDEYRRYGRQLIMPEVGLQGQLRLREASVLVVGVGGLGCPAAAYLVGAGVGSVGLVDGDVVEESNLHRQILHSTARVGMTKVESAMVALNSLNPNVKLVPHKARLSPENAISIFKDYDIVLDCTDTPASRYLISDTCVATRKPLISASALRIDGQLMVLNNPPLPPGDPNGGPCYRCIFPKPPPPETVVSCGDGGILGPVVGVMGVLQALEAIKVLTRPAPTSPADPPTLLLFSAYSTPLFRSIRLRARKPTCAACSSQATITPETLHSGATDYVQFCGLTRPVDALTPQERVSADSYAKLRSGVNPFTGSLLSKDSHILVDVRERVQFELCSIDGSINIPFSAVSGTPGAAHGSGFRAVDGDMEGQEAEWVARLRGTEKPIFVVCRLGNDSQVTVRKMKELGLGFGGKRFIGDIRGGLSAWRDRVDGEFPNY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias29-46Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ML977509
EMBL· GenBank· DDBJ
KAF2128116.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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