A0A9P5UV87 · A0A9P5UV87_9FUNG
- ProteinPentafunctional AROM polypeptide
- GeneARO1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1622 (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 | 89-92 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EESK | ||||||
Binding site | 120-122 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 125 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 136 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 145-146 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 152 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 158 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 167 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 168 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 196 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 200 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 200-203 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 262 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 272 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 283 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 283 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 287 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 299 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 299 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 368 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 840 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 901-908 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1221 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1250 | 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
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 > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Mortierella
Accessions
- Primary accessionA0A9P5UV87
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-396 | 3-dehydroquinate synthase | ||||
Sequence: MSHPNPHIDKVSILGSETIVLGFHIIDYLLRDSLANLKASTYVIITDTNLQKLYLDRFTKAFHKISQELSAASGEPLPRLLTYVIPPGEESKSRAVKGEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQVPTTLLAMVDSSIGGKTAVDTPHAKNPIGAFWQPKRIFIDLSVLETLPEREFVNGMAEVIKTAAIWNHDDFVLLENGAEAIRDAVLKPVRNVEFQGATLETRTAAQQLLLQVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHLGYLSQVAVGRLTRCIQAYGLPVTMEDKFVKNYIGNQYCSVDELMQVLRVDKKNKGNQKRIVMLSAIGKTLEQKASDISD | ||||||
Domain | 83-370 | 3-dehydroquinate synthase | ||||
Sequence: YVIPPGEESKSRAVKGEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQVPTTLLAMVDSSIGGKTAVDTPHAKNPIGAFWQPKRIFIDLSVLETLPEREFVNGMAEVIKTAAIWNHDDFVLLENGAEAIRDAVLKPVRNVEFQGATLETRTAAQQLLLQVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHLGYLSQVAVGRLTRCIQAYGLPVTMEDKFVKNYIGNQYCSVDELMQVLRVDKKN | ||||||
Domain | 421-852 | Enolpyruvate transferase | ||||
Sequence: LSPPGSKSISNRALVLAALGQGTCRLTGLLHSDDTQVMLTALTKLGAATFEWENNGDTLVVHGNGGKMHIPDSELYLGNAGTAARFLTTVSVLVPPSSDPAQKTILTGNARMKQRPIAPLVDALTANGSVLKYVEGKGCLPLEVTPFSHGLAGGEIQLAASISSQYVSSILLCAPYATKEPVTLVLTGGQVISQPYIDMTIAMMKSFGVTVEVLPNNTYRIPQGSYINPEAYLVEADASSATYPLAIAAITGTTCTVPNIGSGSLQGDAGFAVNVLRPMGCTVVQTETSTTVTGPPIGTLKALPHIDMTTMTDAFLTASVLAAVTQPTTPGSENVTKISGIANQRVKECNRIAAMMHELGKFGVKTSEFDDGIIVHGHDIASLTPPKDGVKCYDDHRVAMSFSVLANVVPGGTIILEKKCVEKTWPMWWDDL | ||||||
Region | 1100-1320 | 3-dehydroquinase | ||||
Sequence: LTFPDISPALPHLSKLTLGSDVIELRVDLLKSPSASVSFRDHVAQQVSLLRRHSDLPILYTVRSVSQGGQWPDKDVDGMVSLLNDGLEWGVEYLDVEIGLPRNKIDELLARKGNTLIVASWHDCKGTVAWSSDAMEAQYKLAASISPDVVKLIGTAKSMKDNFECSEFAERHTAKAEDLPLISMNMGAQGQLSRVLNNYLTPVTHKLLPVKAAPGQLDARD | ||||||
Region | 1333-1622 | Shikimate dehydrogenase | ||||
Sequence: AKQFFLFGTPIKQSLSPLMHNTSFQSLGLPYHYGLHETATVDESVVAKMRSADFGGASVTIPHKIDIMSKLDEITDEAKAIGAVNTVVPVQGANQETILVGDNTDWLGIKHQIQRHLSSTSTVQPQQMKGLVIGAGGTSRAALYALHRLGVQEISIYNRTMVKAQSVADSFKDLFAVKVIGSNELLKSSKSSADYDLIVSTVPGTIESEGMFDESIFGAADKKRGVAVELAYTPRFTRFLKLAGQAGWATVEGGEVLVEQGGWQAQKWVGRRWDLESVQVQMDLVQAGRV | ||||||
Domain | 1338-1419 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIKQSLSPLMHNTSFQSLGLPYHYGLHETATVDESVVAKMRSADFGGASVTIPHKIDIMSKLDEITDEAKAIGAVNTV | ||||||
Domain | 1458-1506 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: QQMKGLVIGAGGTSRAALYALHRLGVQEISIYNRTMVKAQSVADSFKDL |
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
- Length1,622
- Mass (Da)176,178
- Last updated2023-09-13 v1
- Checksum3D5A44865A87ACFE
Keywords
- Technical term