A0A0C3D3G5 · A0A0C3D3G5_9AGAM
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1654 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Catalytic activity
- 3-dehydroquinate = 3-dehydroshikimate + H2O
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 42-44 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 85-88 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 116-118 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 132 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 141-142 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 148 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 154 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 163 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 164 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 181-184 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 192 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 196 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 196-199 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 247 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Active site | 257 | Proton acceptor; for 3-dehydroquinate synthase activity | |||
Binding site | 268 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 268 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 272 | Proton acceptor; for 3-dehydroquinate synthase activity | |||
Binding site | 284 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 284 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 359 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Active site | 899 | For EPSP synthase activity | |||
Binding site | 950-957 | ATP (UniProtKB | ChEBI) | |||
Active site | 1256 | Proton acceptor; for 3-dehydroquinate dehydratase activity | |||
Active site | 1284 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | 3-dehydroquinate dehydratase activity | |
Molecular Function | 3-dehydroquinate synthase activity | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | shikimate 3-dehydrogenase (NADP+) activity | |
Molecular Function | shikimate kinase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePentafunctional AROM polypeptide
Including 5 domains:
- Recommended name3-dehydroquinate synthase
- EC number
- Short namesDHQS
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
- Recommended nameShikimate kinase
- EC number
- Short namesSK
- Recommended name3-dehydroquinate dehydratase
- EC number
- Short names3-dehydroquinase
- Recommended nameShikimate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Sclerodermatineae > Sclerodermataceae > Scleroderma
Accessions
- Primary accessionA0A0C3D3G5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 110-131 | Helical | |||
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-387 | 3-dehydroquinate synthase | |||
Domain | 79-361 | 3-dehydroquinate synthase | |||
Domain | 460-911 | Enolpyruvate transferase | |||
Region | 1365-1654 | Shikimate dehydrogenase | |||
Domain | 1370-1451 | Shikimate dehydrogenase substrate binding N-terminal | |||
Domain | 1491-1570 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | |||
Domain | 1619-1649 | SDH C-terminal | |||
Sequence similarities
Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 2nd section; belongs to the type-I 3-dehydroquinase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the dehydroquinate synthase family.
In the N-terminal section; belongs to the shikimate kinase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,654
- Mass (Da)176,601
- Last updated2015-04-01 v1
- Checksum83A4CC88510FA9AE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KN822136 EMBL· GenBank· DDBJ | KIM55335.1 EMBL· GenBank· DDBJ | Genomic DNA |