A0A9P5ZTV6 · A0A9P5ZTV6_PLEER
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1600 (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 | 45-47 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 85-88 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ETSK | ||||||
Binding site | 116-118 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 141-142 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 148 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 154 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 163 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 164 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 181-184 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLET | ||||||
Binding site | 192 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 196 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 196-199 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 256 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 266 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 270-274 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLVN | ||||||
Binding site | 277 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 281 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 293 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 293 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 362 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 832 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 881-888 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGSGKT | ||||||
Active site | 1203 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1231 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Pleurotineae > Pleurotaceae > Pleurotus
Accessions
- Primary accessionA0A9P5ZTV6
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-390 | 3-dehydroquinate synthase | ||||
Sequence: MAATDVFKVSILGKESIHCGFHLFPHIAATVLSTLPSSTYVLVTDTNVANFHLSTFEEEFMASIGRLENVLTRPRFLSHVILPGETSKSREGKANIEDFLLLNKCTRDTVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPQGKNLIGAFWQPEYIFIDAAFLETLPAREFSNGMAEVVKTAAIWDESEFASLESRYGEIFAAIQTPSRDYSGRTKATRSPAQDILLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMVLEAEVSRQLGVLSQVGVGRLSRCLKSYNLPIALSDLRIANLPASKFLTVDKLLDIMRVDKKNSGPEKKVVILSKIGATYEQKATVVRD | ||||||
Domain | 80-364 | 3-dehydroquinate synthase | ||||
Sequence: VILPGETSKSREGKANIEDFLLLNKCTRDTVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPQGKNLIGAFWQPEYIFIDAAFLETLPAREFSNGMAEVVKTAAIWDESEFASLESRYGEIFAAIQTPSRDYSGRTKATRSPAQDILLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMVLEAEVSRQLGVLSQVGVGRLSRCLKSYNLPIALSDLRIANLPASKFLTVDKLLDIMRVDKKN | ||||||
Domain | 416-844 | Enolpyruvate transferase | ||||
Sequence: ATPGSKSISNRALVLAALGQGTCRLKNLLHSDDTAVMMAALMELKGASFSWEDGGETLVVQGGDGSLSVPTKGKELYLGNAGTAARFLTTVCTLVQSTSSSDGTATVITGNARMKQRPIGPLVNALKANGAQIEYLESQGCLPLSIAPNGLKGSRIQLAASVSSQYVSSILLCAPYAAEAVTLELTGGQVISQPYIDMTVAMMKTFGVDVVRRRDPETNALLDIYDIPKATYISPPVYAIESDASSATYPLAIAAITGTTCTIENIGSASLQGDARFAKEVLERMGCSVTQTETETTVTGPPIGSLQAIEEVDMEVMTDAFLTATALAAVAKGKTRILGIANQRVKECNRIRAMIDQLAKFGVETNELDDGLEIIGRPIAELKEGVSVHCYDDHRVAMAFSVLGSVIKGTILEEKRCVEKTWPNWWDDL | ||||||
Region | 1314-1600 | Shikimate dehydrogenase | ||||
Sequence: SRRFFLFGTPIAHSMSPTLHNTAFSLLGLPYIYELLETKAVGEEIKAALASHDFGGASVTIPFKLDIVPLLDELSPAAQAIGAVNTVIAKPTESSKILYGDNTDWIGIRTSVVNIVGEGNIYSALVIGAGGTARAALYALTSLGAKKIYLFNRTQSKAQELEAAFSNSAIEVIGELGSWSSDPPNVIVSTVPASATTIEALNNSLQIPVSIFNYRSGPAVVVDMAYKPAETPLLQLAKRLAGDNWTTVPGVEVLLEQGYQQFKLWTGRACPRKAVSSKVWEKYNTSV | ||||||
Domain | 1319-1400 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIAHSMSPTLHNTAFSLLGLPYIYELLETKAVGEEIKAALASHDFGGASVTIPFKLDIVPLLDELSPAAQAIGAVNTV | ||||||
Domain | 1435-1485 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: YSALVIGAGGTARAALYALTSLGAKKIYLFNRTQSKAQELEAAFSNSAIEV | ||||||
Domain | 1563-1588 | SDH C-terminal | ||||
Sequence: GVEVLLEQGYQQFKLWTGRACPRKAV |
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
- Length1,600
- Mass (Da)172,705
- Last updated2023-09-13 v1
- Checksum773F8F6707A8303F
Keywords
- Technical term