P0A182 · QADG_PSEPU
- ProteinQuinohemoprotein amine dehydrogenase subunit gamma
- GeneqhnDH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidative deamination of a wide range of aliphatic monoamines and diamines (PubMed:27315927).
The physiological electron acceptor is an azurin-like blue protein (PubMed:27315927).
The physiological electron acceptor is an azurin-like blue protein (PubMed:27315927).
Catalytic activity
- A + an aliphatic amine + H2O = AH2 + an aldehyde + NH4+This reaction proceeds in the forward direction.
Cofactor
Note: Contains 1 cysteine tryptophylquinone per subunit.
Activity regulation
Inhibited by various carbonyl reagents, such as p-nitrophenylhydrazine (pNPH), 2,4-dinitrophenylhydrazine, semicarbazide and hydroxylamine.
pH Dependence
Optimum pH is around 8.0 for n-butylamine oxidation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 33 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | amine dehydrogenase activity |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQuinohemoprotein amine dehydrogenase subunit gamma
- EC number
- Short namesQH-AmDH
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP0A182
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is probably co-translocated into the periplasm when associated with the alpha and/or beta subunit, which contain both a signal peptide.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 62 | in strain: IFO 15366 | ||||
Sequence: S → T | ||||||
Natural variant | 66 | in strain: IFO 15366 | ||||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000220551 | 2-79 | Quinohemoprotein amine dehydrogenase subunit gamma | |||
Sequence: SAVAGCTATTDPGWEVDAFGGVSSLCQPMEADLYGCSDPCWWPAQVPDMMSTYQDWNAQASNSAEDWRNLGTVFPKDK | ||||||
Cross-link | 7↔16 | 4-cysteinyl-glutamic acid (Cys-Glu) | ||||
Sequence: CTATTDPGWE | ||||||
Cross-link | 27↔33 | 3-cysteinyl-aspartic acid (Cys-Asp) | ||||
Sequence: CQPMEAD | ||||||
Cross-link | 37↔43 | 4'-cysteinyl-tryptophylquinone (Cys-Trp) | ||||
Sequence: CSDPCWW | ||||||
Cross-link | 41↔49 | 3-cysteinyl-aspartic acid (Cys-Asp) | ||||
Sequence: CWWPAQVPD | ||||||
Modified residue | 43 | Tryptophylquinone | ||||
Sequence: W |
Post-translational modification
The cysteine tryptophylquinone (CTQ) is generated by oxidation of the indole ring of a tryptophan residue to form tryptophylquinone, followed by covalent cross-linking with a cysteine residue.
Keywords
- PTM
Interaction
Subunit
Heterotrimer of an alpha, a beta and a gamma subunit.
Structure
Sequence
- Sequence statusComplete
- Length79
- Mass (Da)8,597
- Last updated2007-01-23 v2
- Checksum3B7EA9B9A4AB7298
Mass Spectrometry
Keywords
- Technical term