U7R3E0 · U7R3E0_PHOTE
- ProteinBifunctional aspartokinase/homoserine dehydrogenase
- GenemetL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids811 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- L-aspartate + ATP = 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 | aspartate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | homoserine dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NADP binding | |
Biological Process | homoserine biosynthetic process | |
Biological Process | lysine biosynthetic process via diaminopimelate | |
Biological Process | methionine biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | threonine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
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 > Morganellaceae > Photorhabdus
Accessions
- Primary accessionU7R3E0
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-284 | Aspartate/glutamate/uridylate kinase | ||||
Sequence: RQLHKFGGSSLADVKCYQRVAKIMANYSQPGDLMVVSAAGSTTNQLINWLKLSQNDRISAHQVQQVLRRYQQDLIRGLLPETVAEELVKRFITDLERLSALLDKPVSDVTYAEVVGHGEIWSARLMSAVLEAQGIASDWVDARQFLRAERAAQPQVDVDLSQPLLNQLLTQNLNKRLVVTGFISSNHDGETVLLGRNGSDYSATQVGALAGAKRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHTRTLQPVSVSDIDL | ||||||
Domain | 466-601 | Aspartate/homoserine dehydrogenase NAD-binding | ||||
Sequence: GKGNIGSRWLELFAREQKNISARSDFEFILAGVADSRRSLLDYQGIDASRALAFFDAEATEHDVDELFLWMRAHPYDDLVILDVTASEELARCYSDFASYGFHVISANKIAGASSSNDYRLIRDAFAKTGRHWFYN | ||||||
Domain | 609-804 | Homoserine dehydrogenase catalytic | ||||
Sequence: PINHTVRDLRESGDTILSISGIFSGTLSWLFLQFDGSVPFSDLVEQAWQQGLTEPDPRIDLSGQDVMRKLIILAREAGYEIEPEQVRVESLVPKEAKSGSIEQFFDNSGAINEQMVQRLAAAQEMGMVLRYVARFDANGKAKVGVEAVRPDHPLASLLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDL |
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
- Length811
- Mass (Da)89,463
- Last updated2014-01-22 v1
- Checksum0D8BE82E8080652E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AXDT01000086 EMBL· GenBank· DDBJ | ERT13211.1 EMBL· GenBank· DDBJ | Genomic DNA |