(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 putida group: NE > Pseudomonas putida: 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 putida S16: N, E.
Pseudomonas monteilii SB3101: N, E.
Pseudomonas plecoglossicida NB2011: N, E.
Pseudomonas plecoglossicida: N, E.
Pseudomonas putida W619: N, E.
Pseudomonas putida DOT-T1E: N, E.
Pseudomonas putida F1: N, E.
Pseudomonas putida TRO1: N, E.
Pseudomonas putida S11: N, E.
Pseudomonas putida CSV86: N, E.
Pseudomonas putida S610: N, E.
Pseudomonas putida S12: N, E.
Pseudomonas putida S13.1.2: N, E.
Pseudomonas putida KG-4: N, E.
Pseudomonas putida LF54: N, E.
Pseudomonas putida KT2440: N, E.
Pseudomonas putida BIRD-1: N, E.
Pseudomonas putida GB-1: N, E.
Pseudomonas sp. ND6: N, E.
Pseudomonas putida H8234: N, E.
Pseudomonas putida HB3267: N, E.
Pseudomonas putida SJ3: N, E.
Pseudomonas putida LS46: N, E.
Pseudomonas putida NBRC 14164: N, E.
Pseudomonas putida ND6: N, E.
Pseudomonas putida B6-2: N, E.
Pseudomonas putida SJTE-1: N, E.
Pseudomonas sp. ICMP 564: N, E.
Pseudomonas sp. JY-Q: N, E.
compost metagenome: N, E.
Molecular evidence
Database
No mutation 1 structure: 4L0C: Crystal structure of the N-Formylmaleamic acid deformylase Nfo(S94A) from Pseudomonas putida S16 No kinetic
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 MKGYNVYANGIRQHIIHFPGTGSPLLLIPGITSPAVTWGFVAERLAKYFD VHVVDVRGRGLSESGDLDYSLDAMADDLVALAQRMEGVVVLGHSMGARIA IRAARKDSQVFSRLILVDPPVSGPGRRPYPAKWSWYAESIRLAQRGCTAM EMRSYCPTWTDEQIELRAEWLHTCQYTAVKTAFDGFHTDDIHTDLAQLTL PIQLVVAGGAEVIQPDDIAEIISLAPQTTTYVVEEAGHMIPWDNLEGFIT AVSNR
References
Title: Structural insights into the specific recognition of N-heterocycle biodenitrogenation-derived substrates by microbial amide hydrolases Wu G, Chen D, Tang H, Ren Y, Chen Q, Lv Y, Zhang Z, Zhao YL, Yao Y, Xu P Ref: Molecular Microbiology, 91:1009, 2014 : PubMed
N-heterocyclic compounds from industrial wastes, including nicotine, are environmental pollutants or toxicants responsible for a variety of health problems. Microbial biodegradation is an attractive strategy for the removal of N-heterocyclic pollutants, during which carbon-nitrogen bonds in N-heterocycles are converted to amide bonds and subsequently severed by amide hydrolases. Previous studies have failed to clarify the molecular mechanism through which amide hydrolases selectively recognize diverse amide substrates and complete the biodenitrogenation process. In this study, structural, computational and enzymatic analyses showed how the N-formylmaleamate deformylase Nfo and the maleamate amidase Ami, two pivotal amide hydrolases in the nicotine catabolic pathway of Pseudomonas putida S16, specifically recognize their respective substrates. In addition, comparison of the alpha-beta-alpha groups of amidases, which include Ami, pinpointed several subgroup-characteristic residues differentiating the two classes of amide substrates as containing either carboxylate groups or aromatic rings. Furthermore, this study reveals the molecular mechanism through which the specially tailored active sites of deformylases and amidases selectively recognize their unique substrates. Our work thus provides a thorough elucidation of the molecular mechanism through which amide hydrolases accomplish substrate-specific recognition in the microbial N-heterocycles biodenitrogenation pathway.
Title: A novel NADH-dependent and FAD-containing hydroxylase is crucial for nicotine degradation by Pseudomonas putida Tang H, Yao Y, Zhang D, Meng X, Wang L, Yu H, Ma L, Xu P Ref: Journal of Biological Chemistry, 286:39179, 2011 : PubMed
Nicotine, the main alkaloid produced by Nicotiana tabacum and other Solanaceae, is very toxic and may be a leading toxicant causing preventable disease and death, with the rise in global tobacco consumption. Several different microbial pathways of nicotine metabolism have been reported: Arthrobacter uses the pyridine pathway, and Pseudomonas, like mammals, uses the pyrrolidine pathway. We identified and characterized a novel 6-hydroxy-3-succinoyl-pyridine (HSP) hydroxylase (HspB) using enzyme purification, peptide sequencing, and sequencing of the Pseudomonas putida S16 genome. The HSP hydroxylase has no known orthologs and converts HSP to 2,5-dihydroxy-pyridine and succinic semialdehyde, using NADH. (18)O(2) labeling experiments provided direct evidence for the incorporation of oxygen from O(2) into 2,5-dihydroxy-pyridine. The hspB gene deletion showed that this enzyme is essential for nicotine degradation, and site-directed mutagenesis identified an FAD-binding domain. This study demonstrates the importance of the newly discovered enzyme HspB, which is crucial for nicotine degradation by the Pseudomonas strain.
Title: Complete genome sequence of the nicotine-degrading Pseudomonas putida strain S16 Yu H, Tang H, Wang L, Yao Y, Wu G, Xu P Ref: Journal of Bacteriology, 193:5541, 2011 : PubMed
Pseudomonas putida S16 is an efficient degrader of nicotine. The complete genome of strain S16 (5,984,790 bp in length) includes genes related to catabolism of aromatic and heterocyclic compounds. The genes of enzymes in the core genome and a genomic island encode the proteins responsible for nicotine catabolism.
Pseudomonas putida, Pseudomonas monteilii, Pseudomonas plecoglossicida. N-formylmaleamate deformylase
