A0A9R1CZE7 · A0A9R1CZE7_9TREE
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1610 (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 | 47-49 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 84-87 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EGAK | ||||||
Binding site | 115-117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 131 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 140-141 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 147 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 153 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 162 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 163 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 180-183 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLTT | ||||||
Binding site | 191 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 195 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 195-198 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 257 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 267 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 271-275 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLVN | ||||||
Binding site | 278 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 278 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 282 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 294 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 294 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 363 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 845 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 899-906 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1220 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1248 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 |
Keywords
- Molecular function
- Biological process
- Ligand
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 > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus gattii species complex
Accessions
- Primary accessionA0A9R1CZE7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-391 | 3-dehydroquinate synthase | ||||
Sequence: MSSSSADVLKISILGNESIHVGFHLLPYIFETVVTTLPSSTYVLITDTNLSAIYLNDLKASFEEAEAQAGNKARFLVYEVAPGEGAKSRKVKGEIEDWMLDNKCTRDTVILAFGGGVIGDLAGFVAATFMRGVKFIQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPSYIFVDLAFLTTLPTREVSNGMAEVVKTAAIWKDDDFALLESRSAEISLAASTRPIGSPTAGRFASDRSHAQSLLLTVVSGSIYVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPAMLHGECVSVGIILEAEVARQLGVLSQVAVGRLTRCLQAYGLPVSLSDRRIIALPASSQLSVDRLLDIMKIDKKNSGPAKKIVLLSRIGKTYEEKASVVAD | ||||||
Domain | 79-365 | 3-dehydroquinate synthase | ||||
Sequence: EVAPGEGAKSRKVKGEIEDWMLDNKCTRDTVILAFGGGVIGDLAGFVAATFMRGVKFIQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPSYIFVDLAFLTTLPTREVSNGMAEVVKTAAIWKDDDFALLESRSAEISLAASTRPIGSPTAGRFASDRSHAQSLLLTVVSGSIYVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPAMLHGECVSVGIILEAEVARQLGVLSQVAVGRLTRCLQAYGLPVSLSDRRIIALPASSQLSVDRLLDIMKIDKKN | ||||||
Domain | 417-857 | Enolpyruvate transferase | ||||
Sequence: ATPGSKSISNRALVLAALGKGTCRVRNLLHSDDTAVMMNALVELKGAVFSWEDGGDTIVVKGGGGILSTPAKGKELYLGNAGTASRFLTTVCAMVSGSASSERSTIITGNARMKQRPIGPLVDALTANGAKVKYLESTGCLPLDIETNGFRGGHIQLAASVSSQYVSSILLCAPYAAEQVTLELTGGQVISQPYIDMTIAMMEQFGAIVERQKDEQGNLLDVYVIPKCTYVNPPEYSVESDASSATYPLAIAAITGTTCTISNIGSSSLQGDARFAKEVLEPMGCTVEQTLTSTKVTGPPVGTLRALGNVDMEPMTDAFLTASVLAAVAVKPCLPERKVEGLPETASRIYGIANQRVKECNRIQAMRDQLAKFNVETDEFDDGIIIFGKPEASLFRGASIHCYDDHRVAMAFAVLSCIIDKTIIEEKRCVEKTWPNFWDDL | ||||||
Region | 1331-1610 | Shikimate dehydrogenase | ||||
Sequence: AKKFVLFGSPIAHSVSPLLHNTGFATLGLPHNYGLHESEKVDQDVLEVIRSPDFGGASVTIPLKLDIIPHLDSVSEDAKIIGAVNTVIPRGGKLHGENTDWQAIRQAAAQNLNAGVLSDGSSTALVIGAGGTCRAAIYAMHKLRFKTIYLFNRTPENAAKVKASFPESYNIIVVTSLPLPEAPAVVVSTVPGNSLTLDTSSEGIYFPSEVLSRPNGVAIDLAYKPHMTALLQAAEKKEGWKVVPGVEILCLQGFRQFEEWTGKRAPEKKMRNAVLEKYFA | ||||||
Domain | 1336-1417 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGSPIAHSVSPLLHNTGFATLGLPHNYGLHESEKVDQDVLEVIRSPDFGGASVTIPLKLDIIPHLDSVSEDAKIIGAVNTV | ||||||
Domain | 1451-1524 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: SSTALVIGAGGTCRAAIYAMHKLRFKTIYLFNRTPENAAKVKASFPESYNIIVVTSLPLPEAPAVVVSTVPGNS | ||||||
Domain | 1575-1605 | SDH C-terminal | ||||
Sequence: GVEILCLQGFRQFEEWTGKRAPEKKMRNAVL |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,610
- Mass (Da)173,306
- Last updated2023-09-13 v1
- Checksum594B02D6565D8D04