P37142 · AKH_DAUCA
- ProteinBifunctional aspartokinase/homoserine dehydrogenase, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids921 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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-homoserine + NADP+ = L-aspartate 4-semialdehyde + NADPH + H+This reaction proceeds in the backward direction.
Cofactor
Note: A sodium ion is seen in the structure; a metal ion may subtly affect the relative position of the nucleotide-binding region to influence enzyme activity, and could increase the stability of the enzyme.
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.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 573 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 573 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 573 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 605 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 654 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 654 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 654 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 678 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 678 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 705 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 708 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 710 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 712 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 763 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 766 | L-homoserine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 766 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 777 | L-homoserine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 781 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 898 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 898 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 898 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | aspartate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | homoserine dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD+ 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, chloroplastic
- Short namesAK-HD; AK-HSDH
Including 2 domains:
- Recommended nameAspartokinase
- EC number
- Recommended nameHomoserine dehydrogenase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Apiales > Apiaceae > Apioideae > Scandiceae > Daucinae > Daucus > Daucus sect. Daucus
Accessions
- Primary accessionP37142
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-87 | Chloroplast | ||||
Sequence: SLSSAISPSSYAAIAAAYSARTPIFNKKKTAAVLSPLSLFHQSPSLSKTGIFLHRGRKESSSKFYIAASVTTAVPSLDDSVEKVHLP | ||||||
Chain | PRO_0000002391 | 88-921 | Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic | |||
Sequence: RGAMWSIHKFGGTCVGSSERIRNVAEIVVEDDSERKLVVVSAMSKVTDMMYDLIYKAQSRDDSYESALDAVMEKHKLTAFDLLDEDDLARFLTRLQHDVITLKAMLRAIYIAGHATESFSDFVVGHGELWSAQLLSFVIRKNGGDCNWMDTRDVLVVNPAGSNQVDPDYLESEKRLEKWFSSNQCQTIVATGFIASTPQNIPTTLKRDGSDFSAAIMGALLRAGQVTIWTDVNGVYSADPRKVSEAVVLKTLSYQEAWEMSYFGANVLHPRTINPVMRYDIPIVIRNIFNLSAPGTMICRESVGETEDGLKLESHVKGFATIDNLALINVEGTGMAGVPGTATAIFGAVKDVGANVIMISQASSEHSICFAVPESEVKAVAKALEARFRQALDAGRLSQVANNPNCSILATVGQKMASTPGVSATLFNALAKANINVRAIAQGCTEYNITVVLSREDCVRALKAVHSRFYLSRTTIAVGIVGPGLIGATLLDQLRDQAAILKENSKIDLRVMGITGSRTMLLSETGIDLSRWREVQKEKGQTAGLEKFVQHVRGNHFIPSTVIVDCTADSEVASHYHDWLCRGIHVITPNKKANSGPLDQYLKLRALQRRSYTHYFYEATVVAGLPIITTLQGLLETGDKILRIEGIFSGTLSYIFNNFKSTTPFSEVVSEAKAAGYTEPDPRDDLAGTDVARKVIILARGSGLKLELSDIPVQSLVPEPLRGIASAEEFLLQLPQFDSDMTRKREDAENAGEVLRYVGVVDAVNQKGVVELKRYKKEHPFAQLSGSDNINAFTTERYNKQPPIIRGPGAGAEVTAGGVFSDILRLASYLGAPS |
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 88-339 | Aspartokinase | ||||
Sequence: RGAMWSIHKFGGTCVGSSERIRNVAEIVVEDDSERKLVVVSAMSKVTDMMYDLIYKAQSRDDSYESALDAVMEKHKLTAFDLLDEDDLARFLTRLQHDVITLKAMLRAIYIAGHATESFSDFVVGHGELWSAQLLSFVIRKNGGDCNWMDTRDVLVVNPAGSNQVDPDYLESEKRLEKWFSSNQCQTIVATGFIASTPQNIPTTLKRDGSDFSAAIMGALLRAGQVTIWTDVNGVYSADPRKVSEAVVLKTL | ||||||
Region | 340-567 | Interface | ||||
Sequence: SYQEAWEMSYFGANVLHPRTINPVMRYDIPIVIRNIFNLSAPGTMICRESVGETEDGLKLESHVKGFATIDNLALINVEGTGMAGVPGTATAIFGAVKDVGANVIMISQASSEHSICFAVPESEVKAVAKALEARFRQALDAGRLSQVANNPNCSILATVGQKMASTPGVSATLFNALAKANINVRAIAQGCTEYNITVVLSREDCVRALKAVHSRFYLSRTTIAVGI | ||||||
Domain | 417-489 | ACT 1 | ||||
Sequence: VEGTGMAGVPGTATAIFGAVKDVGANVIMISQASSEHSICFAVPESEVKAVAKALEARFRQALDAGRLSQVAN | ||||||
Domain | 498-575 | ACT 2 | ||||
Sequence: TVGQKMASTPGVSATLFNALAKANINVRAIAQGCTEYNITVVLSREDCVRALKAVHSRFYLSRTTIAVGIVGPGLIGA | ||||||
Region | 568-921 | Homoserine dehydrogenase | ||||
Sequence: VGPGLIGATLLDQLRDQAAILKENSKIDLRVMGITGSRTMLLSETGIDLSRWREVQKEKGQTAGLEKFVQHVRGNHFIPSTVIVDCTADSEVASHYHDWLCRGIHVITPNKKANSGPLDQYLKLRALQRRSYTHYFYEATVVAGLPIITTLQGLLETGDKILRIEGIFSGTLSYIFNNFKSTTPFSEVVSEAKAAGYTEPDPRDDLAGTDVARKVIILARGSGLKLELSDIPVQSLVPEPLRGIASAEEFLLQLPQFDSDMTRKREDAENAGEVLRYVGVVDAVNQKGVVELKRYKKEHPFAQLSGSDNINAFTTERYNKQPPIIRGPGAGAEVTAGGVFSDILRLASYLGAPS |
Sequence similarities
In the N-terminal section; belongs to the aspartokinase family.
In the C-terminal section; belongs to the homoserine dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length921
- Mass (Da)100,226
- Last updated1994-10-01 v1
- Checksum9C89C392DA76A996
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: S |
Keywords
- Technical term