A0A1J9R2F6 · A0A1J9R2F6_9PEZI

  • 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.

TypeIDPosition(s)Description
Binding site147ATP (UniProtKB | ChEBI)
Binding site168ATP (UniProtKB | ChEBI)
Binding site175-179ATP (UniProtKB | ChEBI)
Binding site192ATP (UniProtKB | ChEBI)
Binding site236-237ATP (UniProtKB | ChEBI)
Binding site285Zn2+ (UniProtKB | ChEBI)
Binding site288Zn2+ (UniProtKB | ChEBI)
Active site302Glycyl thioester intermediate; for adenylyltransferase activity
Binding site395Zn2+ (UniProtKB | ChEBI)
Binding site398Zn2+ (UniProtKB | ChEBI)
Active site569Cysteine 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 Functionubiquitin-like modifier activating enzyme activity
Biological ProcessMo-molybdopterin cofactor biosynthetic process
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
      BKCO1_2300020

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 112549
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Botryosphaeriales > Botryosphaeriaceae > Diplodia

Accessions

  • Primary accession
    A0A1J9R2F6

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region27-53Disordered
Region332-365Disordered
Domain465-614Rhodanese
Region502-546Disordered

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
    616
  • Mass (Da)
    65,233
  • Last updated
    2017-02-15 v1
  • Checksum
    D10324C1541753FB
MPVDSSIASLQHEIASCERQLQRLKQQLADAEGARSRNRPYSPTAASHAYTPSGSAASLPADAFHGDVHHNRQFLGAALGGGLPDEWQAELWAVLEQPAHDDRGSRPWPLETHEYTRYGRQLIMPEVGLQGQLRLRSSAVLIVGAGGLGCPAAAYIAGAGVGTLGLVDADTVEESNLHRQILHSTSKVGMPKVESALRNLRCLNPNIKYYSYNTRLTPENALDIFSEYDLVLDCTDTPASRYLISDTCVLLGKPLVSASALQTEGQLMVLNNPPRPPGDPDGGPCYRCVFPKPPPADSVISCGEGGILGPVVGVMGVLQALEAIKLIAAGIEKPPSPSSDEMDVDGTSAASDKHHDAAAAAGSKPAGNKPSLLLFSAYSSPQFRSFGLRTRKAKCAACSAQVTVTREALTSGSMDYVQFCGAVSPINALAPEERISALEYEQTRNGLSTAVEESSLSSFSGGMPKNQKHILVDVREKVQFELAHLDGSINIPFSDIVATPIPPPSSLSPPASAASAPATPATDGADSPASPKQAAGGGSVDDQSQSQPLPAWLTQLRQLPSEQPIVVTCRLGNDSQLAVRKMKALGLDEDGTRKIVDVRGGLRSWREDVDADFPNY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNUE01000023
EMBL· GenBank· DDBJ
OJD34426.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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