Evidence map›Paper›PMID 28403817›Full record

ArticleBMC bioinformatics2017

Homology to peptide pattern for annotation of carbohydrate-active enzymes and prediction of function.

P K Busk, B Pilgaard, M J Lezyk, A S Meyer, L Lange

Abstract read
In one paragraph

Article in BMC bioinformatics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed.

  1. Trial
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  17. iCAZyGFADB: an insect CAZyme and gene function annotation database.Database : the journal of biological databases and curation · 2023
    Article
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16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

P K BuskDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Søltofts Plads, Building 229, 2800, Kgs. Lyngby, Denmark. pbus@kt.dtu.dk.ORCID http://orcid.org/0000-0003-1920-636X
B PilgaardDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Søltofts Plads, Building 229, 2800, Kgs. Lyngby, Denmark.
M J LezykDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Søltofts Plads, Building 229, 2800, Kgs. Lyngby, Denmark.
A S MeyerDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Søltofts Plads, Building 229, 2800, Kgs. Lyngby, Denmark.
L LangeDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, Søltofts Plads, Building 229, 2800, Kgs. Lyngby, Denmark.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCarbohydrate-active enzymes are found in all organisms and participate in key biological processes. These enzymes are classified in 274 families in the CAZy database but the sequence diversity within each family makes it a major task to identify new family members and to provide basis for prediction of enzyme function. A fast and reliable method for de novo annotation of genes encoding carbohydrate-active enzymes is to identify conserved peptides in the curated enzyme families followed by matching of the conserved peptides to the sequence of interest as demonstrated for the glycosyl hydrolase and the lytic polysaccharide monooxygenase families. This approach not only assigns the enzymes to families but also provides functional prediction of the enzymes with high accuracy.

resultsWe identified conserved peptides for all enzyme families in the CAZy database with Peptide Pattern Recognition. The conserved peptides were matched to protein sequence for de novo annotation and functional prediction of carbohydrate-active enzymes with the Hotpep method. Annotation of protein sequences from 12 bacterial and 16 fungal genomes to families with Hotpep had an accuracy of 0.84 (measured as F1-score) compared to semiautomatic annotation by the CAZy database whereas the dbCAN HMM-based method had an accuracy of 0.77 with optimized parameters. Furthermore, Hotpep provided a functional prediction with 86% accuracy for the annotated genes. Hotpep is available as a stand-alone application for MS Windows.

conclusionsHotpep is a state-of-the-art method for automatic annotation and functional prediction of carbohydrate-active enzymes.

Indexed as

Carbohydrate MetabolismBacteriaDatabases, ProteinEnvironmental MicrobiologyFungiGenome, BacterialGenome, FungalGlycoside HydrolasesMixed Function OxygenasesMolecular Sequence AnnotationGlycoside HydrolasesMixed Function OxygenasesAnnotationCarbohydrate-active enzymesGenomicsSoftware

Identifiers

PMID28403817
PMCPMC5389127

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.