A0AAI9SXM2 · A0AAI9SXM2_9ASCO
- ProteinPentafunctional AROM polypeptide
- GeneARO1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1553 (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) | ||||
Sequence: DTN | ||||||
Binding site | 80-83 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ENNK | ||||||
Binding site | 111-113 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 116 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 136-137 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 143 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 149 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 158 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 159 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 176-179 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLQT | ||||||
Binding site | 187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 191 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 191-194 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 243 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 253 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 257-261 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 264 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 264 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 268 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 280 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 280 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 351 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 870-877 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRAAGKS | ||||||
Active site | 1170 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1199 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
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 > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionA0AAI9SXM2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-379 | 3-dehydroquinate synthase | ||||
Sequence: MKIEKVPILGKETIHIGYQIQSHIVNEIIKELASSTYVIITDTNMCQTGTYEKLKTSFEETLQKERPQSRLLTYLVPPGENNKNRKTKAQVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQIPTTLLAMVDSSVGGKTAIDTELGKNFIGAFHQPEYVFCDVSFLQTLPTRQLINGMAEVVKTATIWDEEEFTRLEKFSKQFVAEVSSPEKNLENIKTDLIKTVLGSVRVKALVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPAAVARLSKCLTAYNLPVSVDDKNFAKIVGAKKNNLEIDTLIKKMSIDKKNDGSKIKCVLLEKIGKCFDSKAHQISK | ||||||
Domain | 74-353 | 3-dehydroquinate synthase | ||||
Sequence: YLVPPGENNKNRKTKAQVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQIPTTLLAMVDSSVGGKTAIDTELGKNFIGAFHQPEYVFCDVSFLQTLPTRQLINGMAEVVKTATIWDEEEFTRLEKFSKQFVAEVSSPEKNLENIKTDLIKTVLGSVRVKALVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPAAVARLSKCLTAYNLPVSVDDKNFAKIVGAKKNNLEIDTLIKKMSIDKKN | ||||||
Domain | 403-838 | Enolpyruvate transferase | ||||
Sequence: TITPPGSKSISNRALILAALGKGTVRIKNLLHSDDTKYMLDALVLLKGATVSFEDETVVVTGNGGDLFACKEELYLGNAGTASRFLTAVASLVKESSKNDNVVVLTGNSRMQERPIGPLVDSLKANGSEIEYLNKQGSLPLKIVASPSASASAAAGKGFKGGKITLAATTSSQYVSAILMCAPYANEEVTLTLVGGKPISQLYIDMTCAMMKEFGVEVVKSTTEEYTYHIPRTTYKNPSEYIVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCAVVQTEHSTTVTGPPIGELVALSSVDMEPMTDAFLTASVVAAVAQGKTTITGIANQRVKECNRIKAMCDELAKFGVEASEISDGIVISGVDPTDLKTPPLDPGVKTYDDHRVAMSFSLLAGLCKKPVLILERSTTGKTWPGWWDIL | ||||||
Region | 1279-1553 | Shikimate dehydrogenase | ||||
Sequence: EEKFWVVGSPVGHSRSPALHNAAYKALGLPYKFDKFDTDNAEKVYNELMLEPNFGGLAITIPLKIDMMTYCTELSESSKIIGAINTIVPAKNGFLGDNTDWIGIANSFKQNGFIEGKSVSGLVIGGGGTSRAAIYALHKLGCEKIYLLNRTESKLLDLIKNFPSEYNLEIISLNLEEIETRDISLIVSCVPGDKPLDEKLITRLEKILKNNSESILLEAAYKPRFTPIMQLAREKYKCRVIPGVEMLINQGDAQFKIHTGYPAPYSIIREAVLED | ||||||
Domain | 1284-1365 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: VVGSPVGHSRSPALHNAAYKALGLPYKFDKFDTDNAEKVYNELMLEPNFGGLAITIPLKIDMMTYCTELSESSKIIGAINTI | ||||||
Domain | 1399-1477 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: GLVIGGGGTSRAAIYALHKLGCEKIYLLNRTESKLLDLIKNFPSEYNLEIISLNLEEIETRDISLIVSCVPGDKPLDEK | ||||||
Domain | 1521-1551 | SDH C-terminal | ||||
Sequence: GVEMLINQGDAQFKIHTGYPAPYSIIREAVL |
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
- Length1,553
- Mass (Da)170,556
- Last updated2024-07-24 v1
- ChecksumA00BD5EEC87E3C54