The putative acetyl-CoA synthetase gene of Cryptosporidium parvum and a new conserved protein motif in acetyl-CoA synthetases

• Published in: The Journal of parasitology Vol. 82; no. 3; p. 423
• Main Authors: Khramtsov, N.V. (Kansas State University, Manhattan, KS.), Blunt, D.S, Montelone, B.A, Upton, S.J
• Format: Journal Article
• Language: English
• Published: United States 01.06.1996
• Subjects: ACETATE-COA LIGASE; Acetate-CoA Ligase - chemistry; Acetate-CoA Ligase - genetics; Amino Acid Sequence; AMINO ACID SEQUENCES; Animals; Base Sequence; Blotting, Southern; CHEMICAL COMPOSITION; Codon - chemistry; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; Conserved Sequence; CRYPTOSPORIDIUM PARVUM; Cryptosporidium parvum - enzymology; Cryptosporidium parvum - genetics; DNA, Protozoan - analysis; DNA, Protozoan - chemistry; GENBANK/U24082; GENE; GENES; Genes, Protozoan; LIGASAS; LIGASE; LIGASES; MOLECULAR SEQUENCE DATA; Molecular Weight; NUCLEOTIDE SEQUENCE; SECUENCIA NUCLEOTIDICA; Sequence Alignment; Sequence Homology, Amino Acid; SEQUENCE NUCLEOTIDIQUE
• ISSN: 0022-3395; 1937-2345
• DOI: 10.2307/3284079

We determined the nucleotide (nt) sequence of the putative gene encoding acetyl-coenzyme A synthetase (ACS) from the parasitic protozoan Cryptosporidium parvum. The gene is single copy, located on a chromosome of approximately 1.08 mb, and has no introns. The gene is characterized by low codon usage bias and encodes a 694-amino acid (aa) protein with a predicted molecular size of 78 kDa, similar to other ACSs from different prokaryotic and eukaryotic species. Comparison of multiple protein alignments of ACSs revealed a new conserved sequence motif PKT(R/V/L)SGK(I/V/T)(T/M/V/K)R(R/N) near the C-terminus, which may be a signature for ACSs. This motif shares significant homology with sequences from other members of the AMP-binding family, has secondary structure similar to the purine-binding motif of ATP- and GTP-ases, and may play a role in the enzymatic activity of proteins from the AMP-binding family.