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A0A8H4WDX8 · A0A8H4WDX8_9EURO

  • Protein
    Adenylyltransferase and sulfurtransferase uba4
  • Gene
    uba4
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
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.

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 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 site316Zn2+ (UniProtKB | ChEBI)
Binding site319Zn2+ (UniProtKB | ChEBI)
Active site442Cysteine 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
      HAV15_003684

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • #12
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A8H4WDX8

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias33-47Polar residues
Region33-55Disordered
Domain374-487Rhodanese

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    489
  • Mass (Da)
    52,908
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    F5BB019B4963BC93F1CF5193F29A46C9
MGSLDETCASLRAQIIATEAQLAGLKRDLANAEQAAQSETAPTAEIQHKDQNGEGRRWPLLQEEYKRYGRQMIVSQVGLEGQLKLRSARVLLVGAGGLGCPAAQYLAGAGIGTIGLIDGDTVEVSNLHRQVLHRTKNVRKYKVDSAIESLKELNPHPTYIAHRTHLTPEAAPAVFQDYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRAPGDKTGGPCYRCVFPKPPPADSVVSCADGGILGPVVGTMGVLQALEAIKVITAPEIDGARPRDPPSLYIFSAYSSPLVRTIRLRSRRANCAVCSAEATVTLDTIKSGSMDYVFFCGSTNLPSLLGPEERISAREYNERHPSDSSQLRTIIDVRDEAQFGICSLENSINIPISNILSSGYTSGLQETDNGQQAAKVPSWLPSEVASSESTNPIYVVCRLGNDSQIAVKKMKELGLDQLGKRFIGDIRGGLRSWKEQVDPSWPEY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias33-47Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAASRZ010000049
EMBL· GenBank· DDBJ
KAF4765653.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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