S8C3F5 · S8C3F5_DACHA

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

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.
heme (UniProtKB | Rhea| CHEBI:30413 )

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 site417Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site576ATP (UniProtKB | ChEBI)
Binding site597ATP (UniProtKB | ChEBI)
Binding site604-608ATP (UniProtKB | ChEBI)
Binding site621ATP (UniProtKB | ChEBI)
Binding site665-666ATP (UniProtKB | ChEBI)
Binding site708Zn2+ (UniProtKB | ChEBI)
Binding site711Zn2+ (UniProtKB | ChEBI)
Active site725Glycyl thioester intermediate; for adenylyltransferase activity
Binding site815Zn2+ (UniProtKB | ChEBI)
Binding site818Zn2+ (UniProtKB | ChEBI)
Active site944Cysteine persulfide intermediate; for sulfurtransferase activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmolybdopterin-synthase adenylyltransferase activity
Molecular Functionmolybdopterin-synthase sulfurtransferase activity
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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
      H072_3792

Organism names

Accessions

  • Primary accession
    S8C3F5

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region506-535Disordered
Compositional bias518-535Basic and acidic residues
Region758-783Disordered
Compositional bias767-783Polar residues
Domain868-987Rhodanese

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
    989
  • Mass (Da)
    110,679
  • Last updated
    2013-10-16 v1
  • Checksum
    FC3AB81A8A4E262A
MFPAPSRLACVSEWYQFYWNFIRGGKYIFKIEEWHKASGPIIRVGPNELHINDPEFYNTCYTTNYKLKVYTPHYQFMGPANVLEELGSDSLHGCRKAILGPLFTRTSIQKTDKTLRNHVEALVERISQEGKGVNAVCATKLFRCTTVDYVSEYVLGSERRFDTVHGDLNAPFHTFFRNAIKYVWFVRFFWPVMRPFTVVPYSLMTIVGSRYSLFGLGQVVVDRTTTLAAGIANEKKIDKPMADIQEENMKEWPSSASVLSVILENRHSGNWVSQKDLMSSLVTLIGGGTETSANTMAVAIYEACLDSSIQDKLHEELVEFFPDLGVEITHLQTEKLPYLSGFIKETLRMAPGLPGRLPRIVQEGGLTIVSMSAYLMHRNPTAYPNPDKFSPDRWLTTSPSSPEEKYLVPFSKGSRSCIGINVVWAQLYITLAVLFRRFRFSLHKNNTLTHHWADNYTRDIQADLVVSVDDGSPARPGAMEKFSLGSENFDLRKRIAELEKELAEYRSGSFASSNGTATEEPERDETEKLQEDENKPVRLDLEEFRRYGRQMIMTEVGLDGQLQLKRSKVLLIGAGGLGCPAAAYLAGAGIGTIGIVDHDLVEPSNLHRQIMHTVDRVGRPKVESIIESLKEINPYPKYIAHNYALSTENAIETVGKYDLILDCTDSPQTRYMISDACVLLGKPLVSASALRSDGQLVVLNNPPGEGPCYRCVFPRPPPPDSVLSCGEGGVLGPVVGAMGVLMSTEALKVLLAKADRKKRRKPAHLSNDGTQADSAPTTNATTTTPEQKKFYMTIYSAFSDTPFRTIRMFGKRKTCQACSKDATITKESMKNGSLDYVAFCGGKASGRYPPLTKEEIVDVEEYQKLREGNKGGLLIDVRDDVQYGMCSLEDSINVPITTILTLPIAREDKKEGEEGKEQEEEEVKPIPIPSWLPRDTSTPIYFICRLGNDSRLAVQRLKQSGLVKGNVIRDVRGGLWEWSRKVDKSFPIY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias518-535Basic and acidic residues
Compositional bias767-783Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AQGS01000127
EMBL· GenBank· DDBJ
EPS42247.1
EMBL· GenBank· DDBJ
Genomic DNA

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