A0A6J3MBD0 · A0A6J3MBD0_9PEZI
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1608 (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 | 50-52 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 92-95 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 123-125 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 128 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 139 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 148-149 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 155 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 161 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 170 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 171 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 188-191 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 199 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 203 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 203-206 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 257 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Active site | 267 | Proton acceptor; for 3-dehydroquinate synthase activity | |||
Binding site | 271-275 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 278 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 278 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 282 | Proton acceptor; for 3-dehydroquinate synthase activity | |||
Binding site | 294 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Binding site | 294 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 362 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | |||
Active site | 832 | For EPSP synthase activity | |||
Binding site | 887-894 | ATP (UniProtKB | ChEBI) | |||
Active site | 1199 | Proton acceptor; for 3-dehydroquinate dehydratase activity | |||
Active site | 1229 | 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 > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Mycosphaerellales > Dissoconiaceae > Dissoconium
Accessions
- Primary accessionA0A6J3MBD0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 117-138 | Helical | |||
Keywords
- Cellular component
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-390 | 3-dehydroquinate synthase | |||
Domain | 88-364 | 3-dehydroquinate synthase | |||
Domain | 411-844 | Enolpyruvate transferase | |||
Region | 1312-1608 | Shikimate dehydrogenase | |||
Domain | 1317-1397 | Shikimate dehydrogenase substrate binding N-terminal | |||
Domain | 1574-1604 | SDH C-terminal | |||
Sequence similarities
Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase 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 sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,608
- Mass (Da)173,851
- Last updated2020-10-07 v1
- MD5 Checksum86ED29DB2E30578B181C44F059248AD2
Keywords
- Technical term