Barbe_2004_Nucleic.Acids.Res_32_5766

Reference

Title : Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium - Barbe_2004_Nucleic.Acids.Res_32_5766
Author(s) : Barbe V , Vallenet D , Fonknechten N , Kreimeyer A , Oztas S , Labarre L , Cruveiller S , Robert C , Duprat S , Wincker P , Ornston LN , Weissenbach J , Marliere P , Cohen GN , Medigue C
Ref : Nucleic Acids Research , 32 :5766 , 2004
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.

PubMedSearch : Barbe_2004_Nucleic.Acids.Res_32_5766
PubMedID: 15514110
Gene_locus related to this paper: aciad-q6f6s6 , aciad-q6f6x6 , aciad-q6f6x7 , aciad-q6f6z2 , aciad-q6f7m0 , aciad-q6f7y3 , aciad-q6f8t1 , aciad-q6f8v6 , aciad-q6f8x2 , aciad-q6f9b1 , aciad-q6f9f4 , aciad-q6f933 , aciad-q6f951 , aciad-q6fa15 , aciad-q6fa93 , aciad-q6fag8 , aciad-q6fak6 , aciad-q6fal1 , aciad-q6fas4 , aciad-q6faz3 , aciad-q6fbp9 , aciad-q6fbr2 , aciad-q6fbr5 , aciad-q6fc40 , aciad-q6fd43 , aciad-q6fd56 , aciad-q6fdd3 , aciad-q6fdh2 , aciad-q6fe39 , aciad-q6feb1 , aciad-q6fen4 , aciad-q6feq3 , aciad-q6ff86 , aciad-q6ffz9 , aciad-q8rlz8 , acica-elh1 , acica-elh2 , acica-estB , acica-este2 , acica-este3

Related information

Gene_locus aciad-q6f6s6    aciad-q6f6x6    aciad-q6f6x7    aciad-q6f6z2    aciad-q6f7m0    aciad-q6f7y3    aciad-q6f8t1    aciad-q6f8v6    aciad-q6f8x2    aciad-q6f9b1    aciad-q6f9f4    aciad-q6f933    aciad-q6f951    aciad-q6fa15    aciad-q6fa93    aciad-q6fag8    aciad-q6fak6    aciad-q6fal1    aciad-q6fas4    aciad-q6faz3    aciad-q6fbp9    aciad-q6fbr2    aciad-q6fbr5    aciad-q6fc40    aciad-q6fd43    aciad-q6fd56    aciad-q6fdd3    aciad-q6fdh2    aciad-q6fe39    aciad-q6feb1    aciad-q6fen4    aciad-q6feq3    aciad-q6ff86    aciad-q6ffz9    aciad-q8rlz8    acica-elh1    acica-elh2    acica-estB    acica-este2    acica-este3

Citations formats

Barbe V, Vallenet D, Fonknechten N, Kreimeyer A, Oztas S, Labarre L, Cruveiller S, Robert C, Duprat S, Wincker P, Ornston LN, Weissenbach J, Marliere P, Cohen GN, Medigue C (2004)
Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium
Nucleic Acids Research 32 :5766

Barbe V, Vallenet D, Fonknechten N, Kreimeyer A, Oztas S, Labarre L, Cruveiller S, Robert C, Duprat S, Wincker P, Ornston LN, Weissenbach J, Marliere P, Cohen GN, Medigue C (2004)
Nucleic Acids Research 32 :5766