(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Pseudomonadales: NE > Pseudomonadaceae: NE > Pseudomonas: NE > Pseudomonas sp. GM101: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Pseudomonas mendocina ymp: N, E.
Pseudomonas stutzeri: N, E.
Pseudomonas stutzeri ATCC 14405 = CCUG 16156: N, E.
Pseudomonas stutzeri CCUG 29243: N, E.
Pseudomonas stutzeri TS44: N, E.
Pseudomonas stutzeri DSM 10701: N, E.
Pseudomonas stutzeri RCH2: N, E.
Pseudomonas stutzeri NF13: N, E.
Pseudomonas stutzeri MF28: N, E.
Pseudomonas stutzeri KOS6: N, E.
Pseudomonas stutzeri A1501: N, E.
Pseudomonas stutzeri ATCC 17588 = LMG 11199: N, E.
Pseudomonas stutzeri B1SMN1: N, E.
Pseudomonas stutzeri DSM 4166: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTKQSLPQGMADQRLCRFFTAALCSLLMILLWPTTVTAGQTFSYTSPQQA YSGSRERSYKVYVPTGLSTPAPMVMALHGCRQTNDDVLNDWGLKAAADRY GFILVAPFITSYDGLRNENCWGFWFEQHIHQGGGEVADLHRIAQQVEANF VIDANRRFITGLSSGGAMALVAAVAYNEYWAAAAPAAGLPYRETASSVSL SGQCPGSATFRSVSQVAADMRSEVNDAYPIPLMILQNRNDCTVLQTAANN MRDAHLQVFGSASRNTPATTKASDTGCSPYHQSDYGCRHIAYTQDGTTAT RSLVETVIYDGPLATPNPQDTNHGHYWIGGAQGNNGKWSLQVGPSYPDII WDFFSRYSRD
References
Title: Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases Kasuya K, Ohura T, Masuda K, Doi Y Ref: Int J Biol Macromol, 24:329, 1999 : PubMed
The substrate specificities of three extracellular polyhydroxybutyrate (PHB) depolymerases from Alcaligenes faecalis (PhaZ Afa), Pseudomonas stutzeri (PhaZ Pst), and Comamonas acidovorans (PhaZ Cac), which are grouped into types A and B based on the position of a lipase box sequence in the catalytic domain, were examined for films of 12 different aliphatic polyesters. Each of these PHB depolymerases used was capable of hydrolyzing poly(3-hydroxybutyrate) (P(3HB)), poly(3-hydroxypropionate) (P(3HP)), poly(4-hydroxybutyrate) (P(4HB)), poly(ethylene succinate) (PESU), and poly(ethylene adipate) (PEA) but could not hydrolyze another seven polyesters. In addition, the binding characteristics of substrate binding domains from PhaZ Afa, PhaZ Cac, and PHB depolymerase from Comamonas testosteroni (PhaZ Cte) were studied by using fusions with glutathione S-transferase (GST). All of fusion proteins adsorbed strongly on the surfaces of polyester granules of P(3HB), P(3HP), and poly(2-hydroxypropionate) (P(2HP)) which was not hydrolyzed by the PHB depolymerases used in this study, while they did not bind on Avicel and chitin granules. The adsorption kinetics of the fusion proteins to the surface of P(3HB) and P(2HP) granules were found to obey the Langmuir isotherm. The cross-area per molecule of fusion protein bound to P(3HB) granules was estimated to be 12+/-4 nm2/molecule. It has been suggested that the active sites in catalytic domains of PHB depolymerases have a similar conformational structure, and that several amino acids in substrate-binding domains of PHB depolymerases interact specifically with the surface of polyesters.
Title: Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains Ohura T, Kasuya KI, Doi Y Ref: Applied Environmental Microbiology, 65:189, 1999 : PubMed
The extracellular polyhydroxybutyrate (PHB) depolymerase gene (phaZPst) of Pseudomonas stutzeri was cloned and sequenced. phaZPst was composed of 1,728 bp encoding a protein of 576 amino acids. Analyses of the N-terminal amino acid sequence and the matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrum of the purified enzyme showed that the mature enzyme consisted of 538 amino acids with a deduced molecular mass of 57,506 Da. Analysis of the deduced amino acid sequence of the protein revealed a domain structure containing a catalytic domain, putative linker region, and two putative substrate-binding domains (SBDI and SBDII). The putative linker region was similar to the repeating units of the cadherin-like domain of chitinase A from Vibrio harveyi and chitinase B from Clostridium paraputrificum. The binding characteristics of SBDs to poly([R]-3-hydroxybutyrate) [P(3HB)] and chitin granules were characterized by using fusion proteins of SBDs with glutathione S-transferase (GST). These GST fusion proteins with SBDII and SBDI showed binding activity toward P(3HB) granules but did not bind on chitin granules. It has been suggested that the SBDs of the depolymerase interact specifically with the surface of P(3HB). In addition, a kinetic analysis for the enzymatic hydrolysis of 3-hydroxybutyrate oligomers of various sizes has suggested that the catalytic domain of the enzyme recognizes at least two monomeric units as substrates.
