P66899 · DPAL_ECOLI
- ProteinDiaminopropionate ammonia-lyase
- GeneygeX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids398 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them.
Catalytic activity
- (S)-2,3-diaminopropanoate + H+ + H2O = 2 NH4+ + pyruvate
Cofactor
Note: Binds 1 pyridoxal phosphate per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.1 mM | D-DAP | |||||
0.048 mM | L-DAP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
48 μmol/min/mg | for D-DAP | ||||
25 μmol/min/mg | for L-DAP |
pH Dependence
Optimum pH is 8.0.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 77 | Proton acceptor; for D-DAP ammonia-lyase activity | ||||
Sequence: K | ||||||
Active site | 120 | Proton acceptor; for L-DAP ammonia-lyase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | diaminopropionate ammonia-lyase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | pyridoxal phosphate binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiaminopropionate ammonia-lyase
- EC number
- Short namesDAPAL
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP66899
- Secondary accessions
Proteomes
Phenotypes & Variants
Disruption phenotype
No growth on minimal medium plus DL-DAP; growth can be restored by a mix of 8 amino acids (Arg, Asn, Cys, Glu, Ile, Leu, Met and Thr).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 77 | No longer binds cofactor, loss of enzymatic activity. | ||||
Sequence: K → H or R | ||||||
Mutagenesis | 120 | No activity on D-DAP, 150-fold reduced catalytic efficiency for L-DAP; alters substrate stereospecificity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 189 | 10000-fold reduced catalytic efficiency for both D- and L-DAP. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000185590 | 1-398 | Diaminopropionate ammonia-lyase | |||
Sequence: MSVFSLKIDIADNKFFNGETSPLFSQSQAKLARQFHQKIAGYRPTPLCALDDLANLFGVKKILVKDESKRFGLNAFKMLGGAYAIAQLLCEKYHLDIETLSFEHLKNAIGEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILNLGAECIVTDMNYDDTVRLTMQHAQQHGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMREMGVTPTHVLLQAGVGAMAGGVLGYLVDVYSPQNLHSIIVEPDKADCIYRSGVKGDIVNVGGDMATIMAGLACGEPNPLGWEILRNCATQFISCQDSVAALGMRVLGNPYGNDPRIISGESGAVGLGVLAAVHYHPQRQSLMEKLALNKDAVVLVISTEGDTDVKHYREVVWEGKHAVAP | ||||||
Modified residue | 77 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K | ||||||
Disulfide bond | 265↔291 | |||||
Sequence: CIYRSGVKGDIVNVGGDMATIMAGLAC |
Keywords
- PTM
Proteomic databases
Expression
Induction
Slightly induced by DL-DAP.
Structure
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)43,328
- Last updated2004-10-11 v1
- ChecksumFAF1277E86D60232
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U28375 EMBL· GenBank· DDBJ | AAA83052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75909.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76937.1 EMBL· GenBank· DDBJ | Genomic DNA |