Q88JH0 · PEDH_PSEPK
- ProteinQuinoprotein alcohol dehydrogenase PedH
- GenepedH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids595 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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:
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.
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 μM | ethanol | |||||
2261 μM | acetaldehyde | |||||
329 μM | 2-phenylethanol | |||||
0.016 mM | ethanol |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
10.6 μmol/min/mg | with ethanol as substrate using artificial electron acceptor | ||||
8.4 μmol/min/mg | with acetaldehyde as substrate using artificial electron acceptor | ||||
11.8 μmol/min/mg | with 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 87 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 137 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 181 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 197 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 198 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 199 | Pr3+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 263 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 281 | Pr3+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 323 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 323 | Pr3+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 325 | Pr3+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 350 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 417 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 493 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 557 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | alcohol dehydrogenase (cytochrome c) activity | |
Molecular Function | calcium ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQuinoprotein alcohol dehydrogenase PedH
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ88JH0
Proteomes
Subcellular Location
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 412 | In 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. | ||||
Sequence: F → I | ||||||
Mutagenesis | 412 | High 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. | ||||
Sequence: F → V | ||||||
Mutagenesis | 561 | High 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. | ||||
Sequence: W → A | ||||||
Mutagenesis | 561 | In 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. | ||||
Sequence: W → S or Q |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MTRSPRRPLFAVSLVLSAMLLAGAAHA | ||||||
Chain | PRO_5004302083 | 28-595 | Quinoprotein alcohol dehydrogenase PedH | |||
Sequence: AVSNEEILQDPKNPQQIVTNGLGVQGQRYSPLDLLNVNNVKELRPVWAFSFGGEKQRGQQAQPLIKDGVMYLTGSYSRVFAVDARTGKKLWQYDARLPDDIRPCCDVINRGVALYGNLVFFGTLDAKLVALNKDTGKVVWSKKVADHKEGYSISAAPMIVNGKLITGVAGGEFGVVGKIQAYNPENGELLWMRPTVEGHMGYVYKDGKAIENGISGGEAGKTWPGDLWKTGGAAPWLGGYYDPETNLILFGTGNPAPWNSHLRPGDNLYSSSRLALNPDDGTIKWHFQSTPHDGWDFDGVNELISFNYKDGGKEVKAAATADRNGFFYVLDRTNGKFIRGFPFVDKITWATGLDKDGRPIYNDASRPGAPGSEAKGSSVFVAPAFLGAKNWMPMAYNKDTGLFYVPSNEWGMDIWNEGIAYKKGAAFLGAGFTIKPLNEDYIGVLRAIDPVSGKEVWRHKNYAPLWGGVLTTKGNLVFTGTPEGFLQAFNAKTGDKVWEFQTGSGVLGSPVTWEMDGEQYVSVVSGWGGAVPLWGGEVAKRVKDFNQGGMLWTFKLPKQLQQTASVKP | ||||||
Disulfide bond | 131↔132 | |||||
Sequence: CC |
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
- PTM
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
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length595
- Mass (Da)64,884
- Last updated2003-06-01 v1
- Checksum42D63FA11A0F9A67
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE015451 EMBL· GenBank· DDBJ | AAN68287.1 EMBL· GenBank· DDBJ | Genomic DNA |