Q88JH0 · PEDH_PSEPK

Function

function

Alcohol dehydrogenase that catalyzes the oxidation of a range of substrates, including linear and aromatic primary and secondary alcohols, as well as aldehydes, but only in the presence of lanthanides, allowing bacterial growth with a variety of volatile organic compounds (VOCs) as carbon and energy sources. Is also involved in the transcriptional regulation of pedE and pedH, most likely acting as a lanthanide sensory module (PubMed:28655819).
Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor (By similarity).

Miscellaneous

The soil-dwelling organism P.putida KT2440 produces 2 PQQ-ADHs, namely, PedE, which is Ca2+-dependent, and PedH, which is lanthanide-dependent. These enzymes are crucial for efficient bacterial growth with a variety of volatile alcohols. The functional redundancy of the PQQ-ADHs and inverse transcriptional regulation of PedE and PedH represent an adaptive strategy of P.putida KT2440 to optimize growth with volatile alcohols and aldehyde substrates in response to the availability of different lanthanides in the natural environment of the bacterium.

Catalytic activity

  • a primary alcohol + 2 Fe(III)-[cytochrome c] = an aldehyde + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • ethanol + 2 Fe(III)-[cytochrome c] = acetaldehyde + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • butan-2-ol + 2 Fe(III)-[cytochrome c] = butan-2-one + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • 2-phenylethanol + 2 Fe(III)-[cytochrome c] = 2-phenylacetaldehyde + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • octan-1-ol + 2 Fe(III)-[cytochrome c] = octanal + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • hexan-1-ol + 2 Fe(III)-[cytochrome c] = hexanal + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • cinnamyl alcohol + 2 Fe(III)-[cytochrome c] = cinnamaldehyde + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • farnesol + 2 Fe(III)-[cytochrome c] = farnesal + 2 Fe(II)-[cytochrome c] + 2 H+
    This reaction proceeds in the forward direction.
  • an aldehyde + 2 Fe(III)-[cytochrome c] + H2O = a carboxylate + 2 Fe(II)-[cytochrome c] + 3 H+
    This reaction proceeds in the forward direction.
  • acetaldehyde + 2 Fe(III)-[cytochrome c] + H2O = 2 Fe(II)-[cytochrome c] + acetate + 3 H+
    This reaction proceeds in the forward direction.
  • butanal + 2 Fe(III)-[cytochrome c] + H2O = butanoate + 2 Fe(II)-[cytochrome c] + 3 H+
    This reaction proceeds in the forward direction.
  • hexanal + 2 Fe(III)-[cytochrome c] + H2O = hexanoate + 2 Fe(II)-[cytochrome c] + 3 H+
    This reaction proceeds in the forward direction.
  • octanal + 2 Fe(III)-[cytochrome c] + H2O = octanoate + 2 Fe(II)-[cytochrome c] + 3 H+
    This reaction proceeds in the forward direction.

Cofactor

Protein has several cofactor binding sites:
Pr3+ (UniProtKB | Rhea| CHEBI:229784 )

Nd3+ (UniProtKB | Rhea| CHEBI:229785 )

La3+ (UniProtKB | Rhea| CHEBI:49701 )

Ce3+ (UniProtKB | Rhea| CHEBI:48782 )

Sm3+ (UniProtKB | Rhea| CHEBI:49890 )

Note: Exhibits enzymatic activity only in the presence of lanthanide ions; maximal activity is observed with Pr3+ and Nd3+, and the activity decreases gradually with lanthanides with atomic masses higher than that of Nd3+. PedH activity is found with lanthanide concentrations as low as 10 nM and up to 100 uM, with a peak in activity at 1 uM.
pyrroloquinoline quinone (UniProtKB | Rhea| CHEBI:58442 )

Note: Binds 1 PQQ group per subunit.

Biotechnology

Is an attractive biocatalyst for the oxidation of 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA), a key reaction within the biocatalytic route toward furan-2,5-dicarboxylic acid (FDCA) production. FDCA is a bio-based platform chemical with the potential to replace terephthalic acid in the production of polymers.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
177 μMethanol
2261 μMacetaldehyde
329 μM2-phenylethanol
0.016 mMethanol
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
10.6 μmol/min/mgwith ethanol as substrate using artificial electron acceptor
8.4 μmol/min/mgwith acetaldehyde as substrate using artificial electron acceptor
11.8 μmol/min/mgwith 2-phenylethanol as substrate using artificial electron acceptor
kcat is 5.0 sec-1 with ethanol as substrate using artificial electron acceptor.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site87pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site137pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site181pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site197pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site198pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site199Pr3+ (UniProtKB | ChEBI)
Binding site263pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site281Pr3+ (UniProtKB | ChEBI)
Active site323Proton acceptor
Binding site323Pr3+ (UniProtKB | ChEBI)
Binding site325Pr3+ (UniProtKB | ChEBI)
Binding site350pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site417pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site493pyrroloquinoline quinone (UniProtKB | ChEBI)
Binding site557pyrroloquinoline quinone (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentouter membrane-bounded periplasmic space
Molecular Functionalcohol dehydrogenase (cytochrome c) activity
Molecular Functioncalcium ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Quinoprotein alcohol dehydrogenase PedH
  • EC number
  • Alternative names
    • Lanthanide-dependent pyrroloquinoline quinone-dependent alcohol dehydrogenase
      (Lanthanide-dependent PQQ-ADH
      )

Gene names

    • Name
      pedH
    • Synonyms
      qedH-II
    • Ordered locus names
      PP_2679

Organism names

Accessions

  • Primary accession
    Q88JH0

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene grow efficiently with ethanol, 1-butanol, and 2-phenylethanol in the absence of La3+, like wild-type strain, and the addition of 20 uM La3+ to the agar medium restricts the growth of the mutant strain. Cells lacking both pedE and pedH show no growth under both conditions.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis412In contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA); when associated with Ser-561 or Gln-561.
Mutagenesis412High decrease in affinity for ethanol, and in contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA) and can also oxidize 5-(hydroxymethyl)furfural (HMF) and 5-formylfurfural (FFF); when associated with Ala-561.
Mutagenesis561High decrease in affinity for ethanol, and in contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA) and can also oxidize 5-(hydroxymethyl)furfural (HMF) and 5-formylfurfural (FFF); when associated with Val-412.
Mutagenesis561In contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA); when associated with Ile-412.

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_500430208328-595Quinoprotein alcohol dehydrogenase PedH
Disulfide bond131↔132

Post-translational modification

The disulfide ring formed between the two adjacent cysteine residues Cys-131 and Cys-132 is essential for efficient electron transfer at pH 7 from PedH to its natural electron acceptor cytochrome c550.

Keywords

Proteomic databases

Expression

Induction

Induced in the presence of lanthanides. The underlying regulatory network is responsive to as little as 1 to 10 nM lanthanum, a concentration assumed to be of ecological relevance.

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the bacterial PQQ dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    595
  • Mass (Da)
    64,884
  • Last updated
    2003-06-01 v1
  • Checksum
    42D63FA11A0F9A67
MTRSPRRPLFAVSLVLSAMLLAGAAHAAVSNEEILQDPKNPQQIVTNGLGVQGQRYSPLDLLNVNNVKELRPVWAFSFGGEKQRGQQAQPLIKDGVMYLTGSYSRVFAVDARTGKKLWQYDARLPDDIRPCCDVINRGVALYGNLVFFGTLDAKLVALNKDTGKVVWSKKVADHKEGYSISAAPMIVNGKLITGVAGGEFGVVGKIQAYNPENGELLWMRPTVEGHMGYVYKDGKAIENGISGGEAGKTWPGDLWKTGGAAPWLGGYYDPETNLILFGTGNPAPWNSHLRPGDNLYSSSRLALNPDDGTIKWHFQSTPHDGWDFDGVNELISFNYKDGGKEVKAAATADRNGFFYVLDRTNGKFIRGFPFVDKITWATGLDKDGRPIYNDASRPGAPGSEAKGSSVFVAPAFLGAKNWMPMAYNKDTGLFYVPSNEWGMDIWNEGIAYKKGAAFLGAGFTIKPLNEDYIGVLRAIDPVSGKEVWRHKNYAPLWGGVLTTKGNLVFTGTPEGFLQAFNAKTGDKVWEFQTGSGVLGSPVTWEMDGEQYVSVVSGWGGAVPLWGGEVAKRVKDFNQGGMLWTFKLPKQLQQTASVKP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE015451
EMBL· GenBank· DDBJ
AAN68287.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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