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Article

A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis.

The Journal of biological chemistry - 25 Apr 1990

Xia Z G, Storm D R

Abstract excerpt

Analysis of the predicted amino acid sequence of Bacillus anthracis adenylyl cyclase revealed sequences with homology to consensus sequences for A- and B-type ATP binding domains found in many ATP binding proteins. Based on the analysis of nucleotide binding proteins, a conserved basic amino acid residue in the A-type consensus sequence and a conserved acidic amino acid residue in the B-type consensus sequence...

Topics

Adenosine Triphosphate
Adenylyl Cyclases
Amino Acid Sequence
Bacillus anthracis
Base Sequence
Binding Sites
Calmodulin
Cloning, Molecular
Escherichia coli
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotide Probes

Plasmids

Source

Identifiers

PMID: 2108958

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2108958-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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