P27725 · AK1H_SERMA
- ProteinBifunctional aspartokinase/homoserine dehydrogenase 1
- GenethrA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids819 (go to sequence)
- Protein existenceInferred from homology
- 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+ = H+ + L-aspartate 4-semialdehyde + NADPHThis 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.
Activity regulation
The enzyme activities are regulated allosterically by L-threonine.
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 | 473 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 475 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 476 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 476 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 476 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 504 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 507 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 555 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 555 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 555 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 556 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 579 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 579 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 606 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 609 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 611 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 613 | Na+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 664 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 667 | L-homoserine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 667 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 678 | L-homoserine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 682 | Proton donor | ||||
Sequence: K | ||||||
Binding site | 797 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 797 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 797 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G |
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 | 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 | threonine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional aspartokinase/homoserine dehydrogenase 1
- Alternative names
Including 2 domains:
- Recommended nameAspartokinase
- EC number
- Recommended nameHomoserine dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionP27725
- Secondary accessions
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 330 | in strain: Sr41 / 8000, Sr41 / HNr21; loss of feedback inhibition | ||||
Sequence: G → D | ||||||
Natural variant | 352 | in strain: Sr41 / TLr156; loss of feedback inhibition | ||||
Sequence: S → F | ||||||
Natural variant | 479 | in strain: Sr41 / HNr59; Thr-resistant HDI | ||||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000066682 | 1-819 | Bifunctional aspartokinase/homoserine dehydrogenase 1 | |||
Sequence: MRVLKFGGTSVANAERFLRVADIMESNARQGQVATVLSAPAKITNHLVAMIDKTVAGQDILPNMSDAERIFADLLSGLAQALPGFEYDRLKGVVDQEFAQLKQVLHGVSLLGQCPDSVNAAIICRGEKLSIAIMEGVFRAKGYPVTVINPVEKLLAQGHYLESTVDIAESTLRIAAAAIPADHIVLMAGFTAGNDKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRTVPDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTSNPQAPGTLIGKDSTDADMPVKGITNLNNMAMINVSGPGMKGMVGMAARVFAVMSRAGISVVLITQSSSEYSISFCVPQGELQRARRALEEEFYLELKDGVLDPLDVMERLAIISVVGDGMRTLRGISARFFSALARANINIVAIAQGSSERSISVVVSNDSATTGVRVSHQMLFNTDQVIEVFVIGVGGVGGALIEQIYRQQPWLKQKHIDLRVCGIANSRVMLTNVHGIALDSWRDALAGAQEPFNLGRLIRLVKEYHLLNPVIVDCTSSQAVADQYVDFLADGFHVVTPNKKANTSSMNYYQQLRAAAAGSHRKFLYDTNVGAGLPVIENLQNLLNAGDELVRFSGILSGSLSFIFGKLDEGLSLSAATLQARANGYTEPDPRDDLSGMDVARKLLILAREAGYKLELSDIEVEPVLPPSFDASGDVDTFLARLPELDKEFARNVANAAEQGKVLRYVGLIDEGRCKVRIEAVDGNDPLYKVKNGENALAFYSRYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV |
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-249 | Aspartokinase | ||||
Sequence: MRVLKFGGTSVANAERFLRVADIMESNARQGQVATVLSAPAKITNHLVAMIDKTVAGQDILPNMSDAERIFADLLSGLAQALPGFEYDRLKGVVDQEFAQLKQVLHGVSLLGQCPDSVNAAIICRGEKLSIAIMEGVFRAKGYPVTVINPVEKLLAQGHYLESTVDIAESTLRIAAAAIPADHIVLMAGFTAGNDKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRTVPDARLLKSM | ||||||
Region | 250-470 | Interface | ||||
Sequence: SYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTSNPQAPGTLIGKDSTDADMPVKGITNLNNMAMINVSGPGMKGMVGMAARVFAVMSRAGISVVLITQSSSEYSISFCVPQGELQRARRALEEEFYLELKDGVLDPLDVMERLAIISVVGDGMRTLRGISARFFSALARANINIVAIAQGSSERSISVVVSNDSATTGVRVSHQMLFNTDQVIEVFV | ||||||
Domain | 320-394 | ACT 1 | ||||
Sequence: VSGPGMKGMVGMAARVFAVMSRAGISVVLITQSSSEYSISFCVPQGELQRARRALEEEFYLELKDGVLDPLDVME | ||||||
Domain | 401-478 | ACT 2 | ||||
Sequence: VVGDGMRTLRGISARFFSALARANINIVAIAQGSSERSISVVVSNDSATTGVRVSHQMLFNTDQVIEVFVIGVGGVGG | ||||||
Region | 471-819 | Homoserine dehydrogenase | ||||
Sequence: IGVGGVGGALIEQIYRQQPWLKQKHIDLRVCGIANSRVMLTNVHGIALDSWRDALAGAQEPFNLGRLIRLVKEYHLLNPVIVDCTSSQAVADQYVDFLADGFHVVTPNKKANTSSMNYYQQLRAAAAGSHRKFLYDTNVGAGLPVIENLQNLLNAGDELVRFSGILSGSLSFIFGKLDEGLSLSAATLQARANGYTEPDPRDDLSGMDVARKLLILAREAGYKLELSDIEVEPVLPPSFDASGDVDTFLARLPELDKEFARNVANAAEQGKVLRYVGLIDEGRCKVRIEAVDGNDPLYKVKNGENALAFYSRYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV |
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 statusComplete
- Length819
- Mass (Da)88,495
- Last updated1992-08-01 v1
- Checksum1F18552B036A8E39
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D10385 EMBL· GenBank· DDBJ | BAA38474.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D10386 EMBL· GenBank· DDBJ | BAA38477.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D10387 EMBL· GenBank· DDBJ | BAA38480.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X60821 EMBL· GenBank· DDBJ | CAA43212.1 EMBL· GenBank· DDBJ | Genomic DNA |