MetaCyc Enzyme: adenylylsulfate:phosphate adenylyltransferase

Gene: apt Accession Number: G-9571 (MetaCyc)

Species: Thiobacillus denitrificans

Subunit composition of adenylylsulfate:phosphate adenylyltransferase = [Apt]2
         adenylylsulfate:phosphate adenylyltransferase subunit = Apt

adenylylsulfate:phosphate adenylyltransferase (APAT) was isolated from the chemolithoautotroph Thiobacillus denitrificans, and the apt gene encoding it was cloned [Bruser00].

The enzyme is homodimeric and exhibits a specific activity of 2100 μmol/min/mg. Catalysis occurs by a ping-pong mechanism with a covalently bound AMP as reaction intermediate. adenylylsulfate:phosphate adenylyltransferase is highly similar to galactose-1-phosphate uridylyltransferase and is also related to ATP adenylyltransferase. The active site residues of galactose-1-phosphate uridylyltransferase are conserved in all three enzymes, suggesting a histidine as the nucleotide-binding residue in all of them [Bruser00].

Molecular Weight of Polypeptide: 41.518 kD (from nucleotide sequence), 41.387 kD (experimental) [Bruser00 ]

Unification Links: Protein Model Portal:Q9LA72 , UniProt:Q9LA72

Relationship Links: Entrez-Nucleotide:PART-OF:AF148553 , InterPro:IN-FAMILY:IPR001937 , InterPro:IN-FAMILY:IPR005849 , InterPro:IN-FAMILY:IPR011146 , Panther:IN-FAMILY:PTHR11943 , Pfam:IN-FAMILY:PF01087

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 11-Sep-2006 by Caspi R , SRI International

Enzymatic reaction of: adenylylsulfate:phosphate adenylyltransferase

EC Number:

sulfate + ADP + H+ <=> adenosine 5'-phosphosulfate + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the opposite direction.

In Pathways: sulfite oxidation II

Kinetic Parameters:

Km (μM)
adenosine 5'-phosphosulfate


Bruser00: Bruser T, Selmer T, Dahl C (2000). ""ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases." J Biol Chem 275(3);1691-8. PMID: 10636864

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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