P37142 · AKH_DAUCA

  • Protein
    Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Cofactor

a metal cation (UniProtKB | Rhea| CHEBI:25213 )

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.

TypeIDPosition(s)Description
Binding site573NAD+ (UniProtKB | ChEBI)
Binding site573NADP+ (UniProtKB | ChEBI)
Binding site573NADPH (UniProtKB | ChEBI)
Binding site605NADP+ (UniProtKB | ChEBI)
Binding site654NAD+ (UniProtKB | ChEBI)
Binding site654NADP+ (UniProtKB | ChEBI)
Binding site654NADPH (UniProtKB | ChEBI)
Binding site678NADP+ (UniProtKB | ChEBI)
Binding site678NADPH (UniProtKB | ChEBI)
Binding site705Na+ (UniProtKB | ChEBI)
Binding site708Na+ (UniProtKB | ChEBI)
Binding site710Na+ (UniProtKB | ChEBI)
Binding site712Na+ (UniProtKB | ChEBI)
Binding site763NADP+ (UniProtKB | ChEBI)
Binding site766L-homoserine (UniProtKB | ChEBI)
Binding site766NADP+ (UniProtKB | ChEBI)
Binding site777L-homoserine (UniProtKB | ChEBI)
Active site781Proton donor
Binding site898NAD+ (UniProtKB | ChEBI)
Binding site898NADP+ (UniProtKB | ChEBI)
Binding site898NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functionaspartate kinase activity
Molecular FunctionATP binding
Molecular Functionhomoserine dehydrogenase activity
Molecular Functionmetal ion binding
Molecular FunctionNAD+ binding
Molecular FunctionNADP binding
Biological Processhomoserine biosynthetic process
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processmethionine biosynthetic process
Biological Processphosphorylation
Biological Processthreonine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic
  • Short names
    AK-HD; AK-HSDH

Including 2 domains:

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Apiales > Apiaceae > Apioideae > Scandiceae > Daucinae > Daucus > Daucus sect. Daucus

Accessions

  • Primary accession
    P37142

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-87Chloroplast
ChainPRO_000000239188-921Bifunctional aspartokinase/homoserine dehydrogenase, chloroplastic

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region88-339Aspartokinase
Region340-567Interface
Domain417-489ACT 1
Domain498-575ACT 2
Region568-921Homoserine dehydrogenase

Sequence similarities

In the N-terminal section; belongs to the aspartokinase family.
In the C-terminal section; belongs to the homoserine dehydrogenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    921
  • Mass (Da)
    100,226
  • Last updated
    1994-10-01 v1
  • Checksum
    9C89C392DA76A996
SLSSAISPSSYAAIAAAYSARTPIFNKKKTAAVLSPLSLFHQSPSLSKTGIFLHRGRKESSSKFYIAASVTTAVPSLDDSVEKVHLPRGAMWSIHKFGGTCVGSSERIRNVAEIVVEDDSERKLVVVSAMSKVTDMMYDLIYKAQSRDDSYESALDAVMEKHKLTAFDLLDEDDLARFLTRLQHDVITLKAMLRAIYIAGHATESFSDFVVGHGELWSAQLLSFVIRKNGGDCNWMDTRDVLVVNPAGSNQVDPDYLESEKRLEKWFSSNQCQTIVATGFIASTPQNIPTTLKRDGSDFSAAIMGALLRAGQVTIWTDVNGVYSADPRKVSEAVVLKTLSYQEAWEMSYFGANVLHPRTINPVMRYDIPIVIRNIFNLSAPGTMICRESVGETEDGLKLESHVKGFATIDNLALINVEGTGMAGVPGTATAIFGAVKDVGANVIMISQASSEHSICFAVPESEVKAVAKALEARFRQALDAGRLSQVANNPNCSILATVGQKMASTPGVSATLFNALAKANINVRAIAQGCTEYNITVVLSREDCVRALKAVHSRFYLSRTTIAVGIVGPGLIGATLLDQLRDQAAILKENSKIDLRVMGITGSRTMLLSETGIDLSRWREVQKEKGQTAGLEKFVQHVRGNHFIPSTVIVDCTADSEVASHYHDWLCRGIHVITPNKKANSGPLDQYLKLRALQRRSYTHYFYEATVVAGLPIITTLQGLLETGDKILRIEGIFSGTLSYIFNNFKSTTPFSEVVSEAKAAGYTEPDPRDDLAGTDVARKVIILARGSGLKLELSDIPVQSLVPEPLRGIASAEEFLLQLPQFDSDMTRKREDAENAGEVLRYVGVVDAVNQKGVVELKRYKKEHPFAQLSGSDNINAFTTERYNKQPPIIRGPGAGAEVTAGGVFSDILRLASYLGAPS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L11529
EMBL· GenBank· DDBJ
AAA16972.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp