Analysis of ancient sequence motifs in the H+-PPase family

Joel Hedlund, Roberto Cantoni, Margareta Baltscheffsky, Herrick Baltscheffsky, Bengt Persson*

*Autor corresponent d’aquest treball

Producció científica: Article en revista indexadaArticleAvaluat per experts

13 Cites (Scopus)

Resum

The unique family of membrane-bound proton-pumping inorganic pyrophosphatases, involving pyrophosphate as the alternative to ATP, was investigated by characterizing 166 members of the UniProtKB/Swiss-Prot + UniProtKB/TrEMBL databases and available completed genomes, using sequence comparisons and a hidden Markov model based upon a conserved 57-residue region in the loop between transmembrane segments 5 and 6. The hidden Markov model was also used to search the approximately one million sequences recently reported from a large-scale sequencing project of organisms in the Sargasso Sea, resulting in additional 164 partial pyrophosphatase sequences. The strongly conserved 57-residue region was found to contain two nonapeptidyl sequences, mainly consisting of the four 'very early' proteinaceous amino acid residues Gly, Ala, Val and Asp, compatible with an ancient origin of the inorganic pyrophosphatases. The nonapeptide patterns have charged amino acid residues at positions 1, 5 and 9, are apparent binding sites for the substrate and parts of the active site, and were shown to be so specific for these enzymes that they can be used for functional assignments of unannotated genomes.

Idioma originalAnglès
Pàgines (de-a)5183-5193
Nombre de pàgines11
RevistaFEBS Journal
Volum273
Número22
DOIs
Estat de la publicacióPublicada - de nov. 2006
Publicat externament

Fingerprint

Navegar pels temes de recerca de 'Analysis of ancient sequence motifs in the H+-PPase family'. Junts formen un fingerprint únic.

Com citar-ho