Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases

A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using curre...

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Detalles Bibliográficos
Autores principales: Geremia, R.A., Petroni, E.A., Ielpi, L., Henrissat, B.
Formato: JOUR
Materias:
glycosyltransferase
mannosyltransferase
algorithm
amino acid sequence
article
cluster analysis
data base
gene sequence
nonhuman
priority journal
protein family
Bacteria (microorganisms)
Prokaryota
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_02646021_v318_n1_p133_Geremia
record_format dspace
spelling todo:paper_02646021_v318_n1_p133_Geremia2023-10-03T15:12:57Z Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases Geremia, R.A. Petroni, E.A. Ielpi, L. Henrissat, B. glycosyltransferase mannosyltransferase algorithm amino acid sequence article cluster analysis data base gene sequence nonhuman priority journal protein family Bacteria (microorganisms) Prokaryota A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using current alignment algorithms as well as hydrophobic cluster analysis (HCA). These sequences show a similarity which is significant but too low to be reliably aligned using automatic alignment methods. However, a region spanning approx. 270 residues in these proteins could be aligned by HCA, and several invariant amino acid residues were identified. These features were also found in several other glycosyltransferases, as well as in proteins of unknown function present in sequence databases. This similarity most probably reflects the existence of a family of proteins with conserved structural and mechanistic features. It is argued that the present IUBMB classification of glycosyltransferases could be complemented by a classification of these enzymes based on sequence similarities analogous to that which we proposed for glycosyl hydrolases. Fil:Geremia, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Petroni, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ielpi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic glycosyltransferase
mannosyltransferase
algorithm
amino acid sequence
article
cluster analysis
data base
gene sequence
nonhuman
priority journal
protein family
Bacteria (microorganisms)
Prokaryota
spellingShingle glycosyltransferase
mannosyltransferase
algorithm
amino acid sequence
article
cluster analysis
data base
gene sequence
nonhuman
priority journal
protein family
Bacteria (microorganisms)
Prokaryota
Geremia, R.A.
Petroni, E.A.
Ielpi, L.
Henrissat, B.
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
topic_facet glycosyltransferase
mannosyltransferase
algorithm
amino acid sequence
article
cluster analysis
data base
gene sequence
nonhuman
priority journal
protein family
Bacteria (microorganisms)
Prokaryota
description A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using current alignment algorithms as well as hydrophobic cluster analysis (HCA). These sequences show a similarity which is significant but too low to be reliably aligned using automatic alignment methods. However, a region spanning approx. 270 residues in these proteins could be aligned by HCA, and several invariant amino acid residues were identified. These features were also found in several other glycosyltransferases, as well as in proteins of unknown function present in sequence databases. This similarity most probably reflects the existence of a family of proteins with conserved structural and mechanistic features. It is argued that the present IUBMB classification of glycosyltransferases could be complemented by a classification of these enzymes based on sequence similarities analogous to that which we proposed for glycosyl hydrolases.
format JOUR
author Geremia, R.A.
Petroni, E.A.
Ielpi, L.
Henrissat, B.
author_facet Geremia, R.A.
Petroni, E.A.
Ielpi, L.
Henrissat, B.
author_sort Geremia, R.A.
title Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
title_short Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
title_full Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
title_fullStr Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
title_full_unstemmed Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
title_sort towards a classification of glycosyltransferases based on amino acid sequence similarities: prokaryotic α-mannosyltransferases
url http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia
work_keys_str_mv AT geremiara towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases
AT petroniea towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases
AT ielpil towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases
AT henrissatb towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases
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