Q79FW0 · BALDT_MYCTU
- ProteinBifunctional aminodeoxychorismate lyase / D-amino acid transaminase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids289 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4-deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis (PubMed:33950161).
DAAT activity is strictly restricted to D-alanine and D-glutamate (PubMed:33950161).
May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation (PubMed:33950161).
Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis (PubMed:33950161).
DAAT activity is strictly restricted to D-alanine and D-glutamate (PubMed:33950161).
May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation (PubMed:33950161).
Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis (PubMed:33950161).
Catalytic activity
- 4-amino-4-deoxychorismate = 4-aminobenzoate + H+ + pyruvate
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.4 mM | aminodeoxychorismate | |||||
7.3 mM | D-alanine | |||||
0.24 mM | D-glutamate |
kcat is 1.9 sec-1 with aminodeoxychorismate as substrate. kcat is 1.46 sec-1 with D-alanine as substrate. kcat is 0.25 sec-1 with D-glutamate as substrate.
Pathway
Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 2/2.
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 26 | Important for dual ACDL/DAAT activities | ||||
Sequence: R | ||||||
Binding site | 50 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 153 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 216 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 217 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 252 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 253 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 254 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 255 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | 4-amino-4-deoxychorismate lyase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | transaminase activity | |
Biological Process | carboxylic acid metabolic process | |
Biological Process | folic acid biosynthetic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape | |
Biological Process | tetrahydrofolate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional aminodeoxychorismate lyase / D-amino acid transaminase
- EC number
- Short namesBifunctional ADCL/DAAT
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionQ79FW0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Deletion mutant exhibits a growth defect in liquid culture (PubMed:33950161).
Mutant is significantly impaired for folate biosynthesis and exhibits minor defects in D-amino acid metabolism (PubMed:33950161).
It shows a marked and selective accumulation of ADC, while the levels of PABA and downstream intermediates of folate biosynthesis are markedly depleted (PubMed:33950161).
It also exhibits a selective and genetically complementable defect in D-glutamate pools, but not D-alanine pools (PubMed:33950161).
Mutant is significantly impaired for folate biosynthesis and exhibits minor defects in D-amino acid metabolism (PubMed:33950161).
It shows a marked and selective accumulation of ADC, while the levels of PABA and downstream intermediates of folate biosynthesis are markedly depleted (PubMed:33950161).
It also exhibits a selective and genetically complementable defect in D-glutamate pools, but not D-alanine pools (PubMed:33950161).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 26 | Decreases kcat of both reactions. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458669 | 1-289 | Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase | |||
Sequence: MVVTLDGEILQPGMPLLHADDLAAVRGDGVFETLLVRDGRACLVEAHLQRLTQSARLMDLPEPDLPRWRRAVEVATQRWVASTADEGALRLIYSRGREGGSAPTAYVMVSPVPARVIGARRDGVSAITLDRGLPADGGDAMPWLIASAKTLSYAVNMAVLRHAARQGAGDVIFVSTDGYVLEGPRSTVVIATDGDQGGGNPCLLTPPPWYPILRGTTQQALFEVARAKGYDCDYRALRVADLFDSQGIWLVSSMTLAARVHTLDGRRLPRTPIAEVFAELVDAAIVSDR | ||||||
Modified residue | 149 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)31,123
- Last updated2004-07-05 v1
- ChecksumA384C2289727FC80
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP43560.1 EMBL· GenBank· DDBJ | Genomic DNA |