Evidence map›Paper›PMID 40854634›Full record

ArticleJournal, genetic engineering & biotechnology2025

In silico analysis of hypothetical proteins in Pseudomonas aeruginosa PAC1: Structural and functional insights.

Mutaz Mohammed Abdallah, Ruaa Abdalla Ibrahim Suliman, Yousra Tagelsir Ahmed, Mawada Yahia

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Article in Journal, genetic engineering & biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

What it found

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3 · Its place in the literature

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2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Mutaz Mohammed AbdallahCollege of Life Sciences, Northeast Forestry University, Harbin, Heilongjiang 150040, China. Electronic address: mutazm920@nefu.edu.cn.
Ruaa Abdalla Ibrahim SulimanSchool of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Yousra Tagelsir AhmedMicrobiology Department, University of Alzaeim Alazhari, Faculty of Medical Laboratory Science, Khartoum, Sudan.
Mawada YahiaDepartment of Basic Sciences, Faculty of Dental Medicine and Surgery, National University, Sudan. Electronic address: mawadat.mohamed.de@nu.edu.sd.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBacterial genomes contain numerous hypothetical proteins (HPs) with uncharacterized roles. This study used computational methods to identify and predict the functions of such proteins in the Pseudomonas aeruginosa PAC1 strain.

methodsThe PAC1 genome (GenBank: CP053706.1) was analyzed, starting with 828 HPs. Proteins shorter than 50 amino acids (unlikely to form stable structures) were excluded, leaving 807 HPs. Physicochemical properties were assessed to filter unstable proteins, resulting in 272 candidates. Subcellular localization tools predicted cytoplasmic localization for 58 proteins. Functional annotation identified conserved domains, and homology modeling generated 3D structures for proteins with >80 % similarity to known templates. Structural validation and active site prediction were performed to assess biological relevance.

resultsTwo HPs, WP_003099663.1 (186 residues) and WP_010793930.1 (455 residues), exhibited structural stability and functional potential. WP_003099663.1 was annotated as a zinc-dependent enzyme involved in carbon dioxide regulation, while WP_010793930.1 was linked to amino acid biosynthesis. Structural models confirmed stable folds, and ligand-binding site predictions highlighted conserved regions, suggesting roles in metabolic pathways.

conclusionThis study demonstrates a systematic computational approach for characterizing hypothetical proteins in bacterial genomes. WP_003099663.1 and WP_010793930.1 exhibit promising structural and functional features and warrant further experimental investigation.

Indexed as

Bioinformatics analysisCytoplasmicHomology modelingHypothetical proteinsPseudomonas aeruginosa

Identifiers

PMID40854634
PMCPMC12221643

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