D4GSF3 · UBAA_HALVD

Function

function

Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus (PubMed:21368171, PubMed:24097257, PubMed:24906001).
In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171, PubMed:24097257).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site42ATP (UniProtKB | ChEBI)
Binding site63ATP (UniProtKB | ChEBI)
Binding site70-74ATP (UniProtKB | ChEBI)
Binding site87ATP (UniProtKB | ChEBI)
Binding site131-132ATP (UniProtKB | ChEBI)
Binding site171Zn2+ (UniProtKB | ChEBI)
Binding site174Zn2+ (UniProtKB | ChEBI)
Active site188Glycyl thioester intermediate
Binding site245Zn2+ (UniProtKB | ChEBI)
Binding site248Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionnucleotidyltransferase activity
Molecular Functionubiquitin-like modifier activating enzyme activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    SAMP-activating enzyme E1
  • EC number
  • Alternative names
    • Ubiquitin-like activating enzyme of archaea (Ubl-activating enzyme)

Gene names

    • Name
      ubaA
    • Ordered locus names
      HVO_0558

Organism names

Accessions

  • Primary accession
    D4GSF3

Proteomes

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene are deficient in sampylation, i.e. SAMP-protein conjugates. Moreover, they do not grow anaerobically with DMSO and do not show DMSO reductase activity, but their growth in the presence of oxygen is not affected; however, they are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs of the mutant strain appear to be nonthiolated.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis188Loss of activity since this mutant is not able to complement a ubaA deletion in trans to restore sampylation and tRNA thiolation.

PTM/Processing

Features

Showing features for chain, cross-link.

TypeIDPosition(s)Description
ChainPRO_00003971071-270SAMP-activating enzyme E1
Cross-link113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2)

Post-translational modification

Sampylated at Lys-113 with the archaeal ubiquitin-like protein SAMP2. Also sampylated with SAMP1.

Keywords

Proteomic databases

Interaction

Subunit

Interacts with NcsA.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the HesA/MoeB/ThiF family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    270
  • Mass (Da)
    28,704
  • Last updated
    2010-05-18 v1
  • Checksum
    B9DFDCD37024FA32
MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001956
EMBL· GenBank· DDBJ
ADE04227.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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