A8P0V4 · AA12_COPC7
- ProteinPyrroloquinoline quinone-dependent pyranose dehydrogenase
- GenePDH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids726 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars including L-galactose, L-gulose, D-talose, D-arabinose, D-lyxose, L-fucose and D-glucosone (PubMed:25121592, PubMed:25679509, PubMed:27338639).
Shows significant activity toward the reverse-chair conformation of pyranoses (PubMed:25679509).
Shows little or no activity toward abundant sugars such as D-glucose, D-fructose, cellobiose, as well L-xylose and L-glucose (PubMed:25121592, PubMed:25679509).
This enzyme is able to direct electrical communication with electrodes, without artificial electron mediators, thus allowing direct electron transfer (DET)-type bioelectrocatalysis (PubMed:27338639).
Exhibits binding affinity for insoluble cellulose (PubMed:25679509).
PDH does not oxidize cello-oligosaccharides but is able to activate the C-1-oxidizing Neurospora crassa LPMO9F and the C-4-oxidizing Neurospora crassa LPMO9C thanks to the electron-tranfer activity of the cytochrome domain and the localization of PDH in the vicinity of the LPMO substrates by the CBM1 domain (PubMed:29602785).
Shows significant activity toward the reverse-chair conformation of pyranoses (PubMed:25679509).
Shows little or no activity toward abundant sugars such as D-glucose, D-fructose, cellobiose, as well L-xylose and L-glucose (PubMed:25121592, PubMed:25679509).
This enzyme is able to direct electrical communication with electrodes, without artificial electron mediators, thus allowing direct electron transfer (DET)-type bioelectrocatalysis (PubMed:27338639).
Exhibits binding affinity for insoluble cellulose (PubMed:25679509).
PDH does not oxidize cello-oligosaccharides but is able to activate the C-1-oxidizing Neurospora crassa LPMO9F and the C-4-oxidizing Neurospora crassa LPMO9C thanks to the electron-tranfer activity of the cytochrome domain and the localization of PDH in the vicinity of the LPMO substrates by the CBM1 domain (PubMed:29602785).
Cofactor
Protein has several cofactor binding sites:
Biotechnology
AA12 family proteins are an attractive component of cellulolytic enzymes for use in biodegradation and biomass conversion or as an anode catalyst for bioelectrochemical applications (PubMed:25679509).
Moreover, direct electron transfer (DET)-type bioelectrocatalysis of the PQQ domain from PDH has been used to create an amperometric L-fucose biosensor for the screening test of cancer using urine (PubMed:33288426).
Moreover, direct electron transfer (DET)-type bioelectrocatalysis of the PQQ domain from PDH has been used to create an amperometric L-fucose biosensor for the screening test of cancer using urine (PubMed:33288426).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
7.9 mM | D-glucosone | |||||
24.8 mM | L-fucose | |||||
30.3 mM | D-arabinose | |||||
84.7 mM | L-gulose | |||||
66.8 mM | D-lyxose | |||||
49.7 mM | L-galactose | |||||
23.1 mM | D-talose | |||||
236 mM | L-xylose | |||||
363 mM | L-glucose | |||||
3.3 mM | cytochrome c reduction at pH 6.0 | 6.0 | ||||
6.1 mM | cytochrome c reduction at pH 8.5 | 8.5 |
pH Dependence
Optimum pH is 6.5 for phenazine methosulfate reduction and 8.5 for cytochrome c reduction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 83 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: M | ||||||
Binding site | 108 | heme b (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 181 | heme b (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 182 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 273 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 363 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 430 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 431 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 449 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 451 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 539 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 560 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 563 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 564 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 621 | pyrroloquinoline quinone (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cellulose binding | |
Molecular Function | metal ion binding | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrroloquinoline quinone-dependent pyranose dehydrogenase
- EC number
- Short namesPDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Psathyrellaceae > Coprinopsis
Accessions
- Primary accessionA8P0V4
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MRSSSLAWALGLVALANA | ||||||
Chain | PRO_5002726695 | 19-726 | Pyrroloquinoline quinone-dependent pyranose dehydrogenase | |||
Sequence: QGSPTQWYDSITGVTFSRFYQQDTDASWGYIFPSASGGQAPDEFIGLFQGPASAGWIGNSLGGSMRNNPLLVGWVDGSTPRISARWATDYAPPSIYSGPRLTILGSSGTNGNIQRIVYRCQNCTRWTGGAGGIPTTGSAVFGWAFHSTTKPLTPSDPSSGLYRHSHAAQYGFDIGNARTTLYDYYLQQLTNAPPLSGGAPTQPPTQQPPTTTAPPPPPPSSTFVSCPGAPQPRYQMNVANGFRVAPVLGGLTMPRGITLDTRGNLLVVERGRGLTGHTLDANGCVTSSKVVIQDTQINHGIDVHPSGRRIIASSGDIAWSWDYDPATMTATNRRTLVTGMNNFYHFTRTVHISRKYPNLFALNVGSDGNIDVPTRQQNSGRAQIRVFDYDQLPQNGVPFVSQYGRVLGYGLRNDVGITEDRAGNIHSIENSLDNAYRMVNGQRRDIHTNNPAEKVYNLGDPSNPRAIFGGYPDCYTVWEPSDFTDSPKQPGDWFTQDNSGQYTDAWCNANAVKPTLLLPPHTAPLDMKFGLGNDTNLYVALHGSWNRQPPQGYKVVVVPGQYSASGEWSPTAPLAQSRTAWSDLLTNRNENQCSGFGNANCFRPVGLVWSADGQNLYVSSDTSGEVFIIKRMSGPIVQPPITQPPITTSPPTPTTPPVVQPPTTVAPPQASQTLWGQCGGQGWTGPTLCPANSVCRESNQWYSQCVPA | ||||||
Disulfide bond | 138↔141 | |||||
Sequence: CQNC | ||||||
Glycosylation | 140 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 244↔302 | |||||
Sequence: CPGAPQPRYQMNVANGFRVAPVLGGLTMPRGITLDTRGNLLVVERGRGLTGHTLDANGC | ||||||
Disulfide bond | 492↔525 | |||||
Sequence: CYTVWEPSDFTDSPKQPGDWFTQDNSGQYTDAWC | ||||||
Glycosylation | 551 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 611↔619 | |||||
Sequence: CSGFGNANC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 688-724 | CBM1 | ||||
Sequence: ASQTLWGQCGGQGWTGPTLCPANSVCRESNQWYSQCV |
Domain
PDH consists of three domains: an N-terminal cytochrome domain (found in AA8 family enzymes), a PQQ-dependent dehydrogenase domain in the middle of the sequence, and a C-terminal cellulose-binding domain classified as a member of the family 1 carbohydrate-binding module (CBM1).
The N-terminal cytochrome domain has an electron transfer function, i.e., intra- and inter-molecular electron transfer between the cytochrome domain and the catalytic domain and also Fe (III)-reducing ability (PubMed:25679509, PubMed:27338639).
This function is essential to activate lytic polysaccharide monooxygenases (LPMOs) at the cell wall (PubMed:29602785).
This function is essential to activate lytic polysaccharide monooxygenases (LPMOs) at the cell wall (PubMed:29602785).
The CBM1 domain binds cellulose and is essential to localize the electron transfer activity in the vicinity of the substrate of lytic polysaccharide monooxygenases (LPMOs) to activate them.
Sequence similarities
Belongs to the sugar dehydrogenase AA12 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length726
- Mass (Da)78,379
- Last updated2008-01-15 v1
- Checksum8AB6ED5467464747
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACS02000006 EMBL· GenBank· DDBJ | EAU83856.1 EMBL· GenBank· DDBJ | Genomic DNA |