A0A066X883 · A0A066X883_COLSU
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1579 (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 | 53-55 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 87-90 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EVSK | ||||||
Binding site | 118-120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 123 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 134 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 143-144 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 150 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 156 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 183-186 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLET | ||||||
Binding site | 194 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 198 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 198-201 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 251 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 261 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 265-269 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 272 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 272 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 276 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 288 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 288 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 357 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 820 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 868-875 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1172 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1200 | 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 | |
Biological Process | chorismate biosynthetic process |
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum graminicola species complex
Accessions
- Primary accessionA0A066X883
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-385 | 3-dehydroquinate synthase | ||||
Sequence: MGLANGSSSGTGPARITILGKDNIVVDHGLWLNFVTHDLLENLKTSTYVVITDTNLYDTYIPPFQEVFNVAAPASTRLLTYAIPPGEVSKSRQTKASIEDWMLSQKCTRDTVIIALGGGVIGDMIGYVAATFMRGVRLVQVPTTLLSMVDSSIGGKTAIDTPAGKNLVGAFWQPLRIYIDLAFLETLPTREFINGMAEVVKTAAIWDEEEFTMLESNAPTILAAVKSQGSQRLSPIRDILKRIVLGSARVKAQVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIASYELPTSVHDKKVIKLTAGKACPVDVLLEKMAVDKKNDGAKKKIVLLSAIGRTHEQKASVVED | ||||||
Domain | 81-359 | 3-dehydroquinate synthase | ||||
Sequence: YAIPPGEVSKSRQTKASIEDWMLSQKCTRDTVIIALGGGVIGDMIGYVAATFMRGVRLVQVPTTLLSMVDSSIGGKTAIDTPAGKNLVGAFWQPLRIYIDLAFLETLPTREFINGMAEVVKTAAIWDEEEFTMLESNAPTILAAVKSQGSQRLSPIRDILKRIVLGSARVKAQVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIASYELPTSVHDKKVIKLTAGKACPVDVLLEKMAVDKKN | ||||||
Domain | 407-832 | Enolpyruvate transferase | ||||
Sequence: DTTVTPPGSKSISNRALVLAALGQGTCRITNLLHSDDTEYMLSAIAQLGGATYAWEDAGEVLAVQGKGGRLSASKEPLYLGNAGTASRFLTTVVALCAPSDVSSTVLTGNARMKVRPIGPLVDALRANGLGIKYLGQDKSLPLQVDAANGFEGGVIELAATISSQYVSSILMAAPYAKNPVTLRLIGGKPISQFYIDMTIAMMRTFGVNVTKSAEEPNTYHIPKAVYQNPPEYVVESDASSATYPLAIAAITGTTCTVPNIGSESLQGDSRFAVDVLRPMGCTVEQTGTSTTVTGPPIGSLKAIEHVDMEPMTDAFLTASVLAAVASGTTKISGIANQRVKECNRIGAMREQLAKFGVDTDEFDDGIIVTGRSVQSLQGPTEDIFCYDDHRVAMSFSVLSVVAPKPVTILERECTGKTWPGWWDTL | ||||||
Region | 1282-1579 | Shikimate dehydrogenase | ||||
Sequence: PQSFYLFGKPISASRSPALHNTLFALTGLPHRYLLKETDHAADVREVIRAPDFGGASVTIPLKLDIMKEIDEVSEAARIIGAVNTIIPVRDRGDSTAKLVGDNTDWSGMVHSLQSAGVAARSASGVECSAMVIGSGGTTRAAIFALHALGFGPIYALARNSSNLETLKASFPPEYRIEPLKSASDASTLPSSPTVIVSTIPADKPVDPSLRETLVTVLRHEPATEEKRVLLEMAYQPRHTPLMQLAEEAGWATIPGLEVLSAQGWYQFRKWTDITPLYQTARAAVLGEEATETVGRKV | ||||||
Domain | 1287-1367 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGKPISASRSPALHNTLFALTGLPHRYLLKETDHAADVREVIRAPDFGGASVTIPLKLDIMKEIDEVSEAARIIGAVNTI |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,579
- Mass (Da)170,469
- Last updated2014-09-03 v1
- Checksum5DE9D2AE01281746
Keywords
- Technical term