A0AAJ0ZD37 · A0AAJ0ZD37_9ENTR
- ProteinBifunctional aspartokinase/homoserine dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids810 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Bifunctional aspartate kinase and homoserine dehydrogenase that catalyzes the first and the third steps toward the synthesis of lysine, methionine and threonine from aspartate.
Catalytic activity
- ATP + L-aspartate = 4-phospho-L-aspartate + ADPThis reaction proceeds in the forward direction.
Cofactor
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | kinase activity |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional aspartokinase/homoserine dehydrogenase
Including 2 domains:
- Recommended nameAspartokinase
- EC number
- Recommended nameHomoserine dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter > Enterobacter cloacae complex
Accessions
- Primary accessionA0AAJ0ZD37
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-284 | Aspartate/glutamate/uridylate kinase | ||||
Sequence: RQLHKFGGSSLADVKCYLRVAGIMTEYSQPGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQSELIAGLLPADVADGLIGAFTHDLERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAERAAQPQVDEGLSYPLLQQLLVQHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQ | ||||||
Domain | 465-600 | Aspartate/homoserine dehydrogenase NAD-binding | ||||
Sequence: GKGNIGSRWLELFAREQVTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAVEQDEESLFLWMRAHPYDDLVVLDVTASEQLADQYLDFASHGFHVISANKLAGASSTDKYRQIHDAFEKTGRHWLYN | ||||||
Domain | 608-803 | Homoserine dehydrogenase catalytic | ||||
Sequence: PVNHTVRDLIESGDSILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAGYDIEPDSVRVESLVPAGCEEGSVDHFFENGEELNEQMVQRLEAANEMGLVLRYVARFEANGKARVGVEAVRPEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDI |
Sequence similarities
In the C-terminal section; belongs to the homoserine dehydrogenase family.
In the N-terminal section; belongs to the aspartokinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length810
- Mass (Da)88,587
- Last updated2024-07-24 v1
- Checksum6CD17EC237550184