A0A165JXZ6 · A0A165JXZ6_XYLHT

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.

TypeIDPosition(s)Description
Binding site101ATP (UniProtKB | ChEBI)
Binding site122ATP (UniProtKB | ChEBI)
Binding site129-133ATP (UniProtKB | ChEBI)
Binding site146ATP (UniProtKB | ChEBI)
Binding site190-191ATP (UniProtKB | ChEBI)
Binding site239Zn2+ (UniProtKB | ChEBI)
Binding site242Zn2+ (UniProtKB | ChEBI)
Active site256Glycyl thioester intermediate; for adenylyltransferase activity
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site327Zn2+ (UniProtKB | ChEBI)
Active site470Cysteine 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
      L228DRAFT_243281

Organism names

Accessions

  • Primary accession
    A0A165JXZ6

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region29-59Disordered
Compositional bias40-54Polar residues
Domain383-515Rhodanese
Region418-440Disordered

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
    517
  • Mass (Da)
    55,262
  • Last updated
    2016-07-06 v1
  • Checksum
    5725DDF3657198A6
MASADTTQESIDSLQARVKGLERELSELKSDLAAANARPSPSLETPTHPDSTDGLTPDGWTWPLAADEYKRYGRQMILPQIGLEGQLKLKSSSVLIVGAGGLGCPAAAYLAGAGVGKLGLVDGDTVEVSNLHRQILHGTHKVDMRKVDSAIQSLKGLNPTIQYVAHREHLTPLTSLDIFAQYDVILDCTDHPTSRYLISDTAVLLGKPLVSASALKTEGQLMVLNDPPLPRGDPSGGPCYRCVFPRPPPAESLVSCGEGGILGPVVGTMGVLQALETIKLITRRAASSSASGSPEKPTPSLLLFSAYGSPPFRSIRLRSRRANCLACSALSPESGCITKESLSSGSLDYVQFCGVTKPVNILAADERVTATEYNNARKTGNTGKEQGVLIDVREKVLYDICHIDNSINIPYSTIVAESRRMPSPSPSPSTPTSSSVEAQNTQNTQNLQEAGNDATWFPNVPSNAPIHVICRLGNDSQLAVRRFQEMGLAQGGNRYIGDIKGGLKAWKDEVDKSWPEV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias40-54Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV407454
EMBL· GenBank· DDBJ
KZF26767.1
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.
FeedbackHelp