Gene Ontology annotation through association of InterPro records with GO terms.
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Functional Role of Lanthanides in Enzymatic Activity and Transcriptional Regulation of Pyrroloquinoline Quinone-Dependent Alcohol Dehydrogenases in Pseudomonas putida KT2440.
-
Purified target proteins oxidize both primary and secondary alcohols; artificial acceptor assays do not establish their native cytochrome partner.
"Similarly, 2-phenylethanol, the secondary alcohol 2-butanol, cinnamyl alcohol, and the acyclic sesquiterpene farnesol were efficiently converted, with specific activities ranging from 6.7 ± 1.1 to 2.0 ± 0.3 U mg−1."
-
Target proteins were purified recombinantly from E. coli; that host is not the native organism.
"A one-step affinity chromatography method produced soluble C-terminally His-tagged PedE and PedH to visible purity (see Fig. S1 in the supplemental material) from cell lysates of Escherichia coli BL21(DE3)."
-
Calcium-dependent PedE contrasts with lanthanide-dependent PedH.
"However, in the presence of the lanthanide La3+, Ce3+, Pr3+, Nd3+, Sm3+, Gd3+, or Tb3+ at 1 µM, enzymatic activity was detected, with maximal specific activity observed with Pr3+ and Nd3+ and only very low activity observed with Gd3+ and Tb3+."
-
Native promoter reporters demonstrate a positive feedback phenotype, without identifying the sensing mechanism.
"Notably, the expression from the pedH promoter was dramatically reduced (2-fold versus 37-fold) in the ΔpedH strain in comparison with that in the strains capable of producing a functional PedH protein."
The PedS2/PedR2 Two-Component System Is Crucial for the Rare Earth Element Switch in Pseudomonas putida KT2440.
-
Both proteins are type I quinoproteins in a native periplasmic oxidation system.
"For efficient capture and metabolism of such VOCs, P. putida makes use of two pyrroloquinoline quinone (PQQ)-dependent ethanol dehydrogenases (PQQ-EDHs)—namely, PedE and PedH—to carry out the initial oxidation steps in the periplasm of the cell (7, 8)."
-
PedS2/PedR2 controls expression; PedH-dependent feedback has an unresolved mechanism.
"In addition, the transcription of pedH is activated via a yet unknown pathway, in which a functional PedH protein is an essential component, most likely by acting as a lanthanide sensor (8)."
Dehydrogenation Mechanism of Three Stereoisomers of Butane-2,3-Diol in Pseudomonas putida KT2440.
-
Native deletion and lanthanum rescue distinguish condition-dependent (2S,3S)-butanediol entry; this is not a purified stereospecificity assay.
"Double-knockout strain P. putida KT2440 (ΔpedEΔpedH) was completely unable to utilize (2S,3S)-2,3-BDO both in the presence and absence of La3+ (Figures 5C,D)"
Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U.
Ethylene glycol metabolism by Pseudomonas putida.
pedH curated UniProt record
-
The cytochrome c550 acceptor assignment is explicitly by similarity, not native partner identification.
"Uses a specific
CC inducible cytochrome c550, encoded by the adjacent gene in the locus,
CC as electron acceptor (By similarity)."
RCSB PDB - 6ZCW: Crystal structure of lanthanide-dependent alcohol dehydrogenase PedH from Pseudomonas putida KT2440
-
Wild-type PedH structure maps to Q88JH0 and deposits PQQ; the construct is mature recombinant protein, not a native electron-transfer assay.
"PYRROLOQUINOLINE QUINONE C14 H6 N2 O8"
-
The same structure directly deposits a praseodymium ligand, supporting the lanthanide cofactor site.
"PRASEODYMIUM ION Pr WCWKKSOQLQEJTE-UHFFFAOYSA-N"