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PMID: 15514110 Published · epublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.

Nucleic acids research ·Vol. 32 ·No. 19 ·2004-00-00 ·Pages 5766-79

Barbe V, Vallenet D, Fonknechten N, Kreimeyer A, Oztas S, Labarre L, Cruveiller S, Robert C, Duprat S, Wincker P, Ornston LN, Weissenbach J, Marlière P, Cohen GN, Médigue C

Abstract

Acinetobacter sp. strain ADP1 is a nutritionally versatile soil bacterium closely related to representatives of the well-characterized Pseudomonas aeruginosa and Pseudomonas putida. Unlike these bacteria, the Acinetobacter ADP1 is highly competent for natural transformation which affords extraordinary convenience for genetic manipulation. The circular chromosome of the Acinetobacter ADP1, presented here, encodes 3325 predicted coding sequences, of which 60% have been classified based on sequence similarity to other documented proteins. The close evolutionary proximity of Acinetobacter and Pseudomonas species, as judged by the sequences of their 16S RNA genes and by the highest level of bidirectional best hits, contrasts with the extensive divergence in the GC content of their DNA (40 versus 62%). The chromosomes also differ significantly in size, with the Acinetobacter ADP1 chromosome <60% of the length of the Pseudomonas counterparts. Genome analysis of the Acinetobacter ADP1 revealed genes for metabolic pathways involved in utilization of a large variety of compounds. Almost all of these genes, with orthologs that are scattered in other species, are located in five major 'islands of catabolic diversity', now an apparent 'archipelago of catabolic diversity', within one-quarter of the overall genome. Acinetobacter ADP1 displays many features of other aerobic soil bacteria with metabolism oriented toward the degradation of organic compounds found in their natural habitat. A distinguishing feature of this genome is the absence of a gene corresponding to pyruvate kinase, the enzyme that generally catalyzes the terminal step in conversion of carbohydrates to pyruvate for respiration by the citric acid cycle. This finding supports the view that the cycle itself is centrally geared to the catabolic capabilities of this exceptionally versatile organism.

MeSH Terms
Acinetobacter/classification,genetics,metabolism Aerobiosis Amino Acids/biosynthesis Base Sequence Biological Transport Coenzymes/biosynthesis Energy Metabolism Evolution, Molecular Genome, Bacterial Molecular Sequence Data Nitrates/metabolism Nitrites/metabolism Nucleic Acids/biosynthesis Polysaccharides/metabolism Sulfates/metabolism Synteny Transformation, Bacterial Vitamins/biosynthesis
Chemicals
Amino Acids Coenzymes Nitrates Nitrites Nucleic Acids Polysaccharides Sulfates Vitamins
Authors & Affiliations
15 authors, click to expand affiliations / ORCID
Barbe Valérie
Genoscope and CNRS-UMR8030, 2 rue Gaston Crémieux, 91057 Evry, Cedex, France. [email protected]
Vallenet David
Fonknechten Nuria
Kreimeyer Annett
Oztas Sophie
Labarre Laurent
Cruveiller Stéphane
Robert Catherine
Duprat Simone
Wincker Patrick
Ornston L Nicholas
Weissenbach Jean
Marlière Philippe
Cohen Georges N
Médigue Claudine
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
Published
2004-00-00
Epub
2004-00-28
Pages
5766-79
Language
English
Region
England
NLM ID
0411011
PMCID
PMC528795
Subset
IM
Databases
GENBANK
CR543861
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