A0A1Y2GE11 · A0A1Y2GE11_9FUNG
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1628 (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 | 87-90 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ENSK | ||||||
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 | 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: EVIK | ||||||
Binding site | 260 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 270 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 281 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 281 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 285 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 297 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 297 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 366 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 838 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 905-912 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1224 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1253 | 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 | |
Biological Process | phosphorylation |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Lobosporangium
Accessions
- Primary accessionA0A1Y2GE11
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-394 | 3-dehydroquinate synthase | ||||
Sequence: MSHPSPHIDKVSILGQETICLGFHIFDYLVRDTLSNFKASTYVIVTDTHLQKLYLDRFQCTFNKIAKELAHDAPLPRLLTYVIPPGENSKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQIPTTLLAMVDSSIGGKTAIDTPQAKNSIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNESDFVLLENGAEAIRDAVLKPVRNVEFQGATLETRTPAQQLLLKVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLSRCIQAYGLPITMEDKFVKNHIGNQYCTVDELMQVLRVDKKNMGSQKRIVMLSGIGKTLEQKPTNISD | ||||||
Domain | 81-368 | 3-dehydroquinate synthase | ||||
Sequence: YVIPPGENSKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQIPTTLLAMVDSSIGGKTAIDTPQAKNSIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNESDFVLLENGAEAIRDAVLKPVRNVEFQGATLETRTPAQQLLLKVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLSRCIQAYGLPITMEDKFVKNHIGNQYCTVDELMQVLRVDKKN | ||||||
Domain | 419-850 | Enolpyruvate transferase | ||||
Sequence: LSPPGSKSISNRALVLAALGKGTCRLTGLLHSDDTQVMLTALTKLGAATFEWENNGDTLVVHGNGGKMHIPDSELYMGNAGTAARFLTTVSVLVPPSTIPGQKTILTGNSRMKQRPIAPLIDALTTNGSELKYLETKGCLPLEVTPFSHGLAGGEIQLAASISSQYVSSILLCAPYATKEPVTLVLTGGQVISQPYIDMTIAMMKSFGITVEALPNNTYRIPQGTYVNPAEYLVEADASSATYPLAIAAITGTTCTVPNIGSTSLQGDAGFAVNVLRPMGCTVVQTETSTTVTGPPIGTLRPLPHIDMETMTDAFLTASVLAAVTQPATSGGNNVTKISGIANQRVKECNRIAAMMHELGKFGVVTSEFDDGIIVHGHDIASLSPPKDGVKCYDDHRVAMSFSVLANVIPGGTIIREKKCVEKTWPTWWDDL | ||||||
Region | 857-891 | Disordered | ||||
Sequence: RTSDIDLGPPSEHHDYEVKSSPSPSPSASSNKKNI | ||||||
Compositional bias | 876-891 | Polar residues | ||||
Sequence: SSPSPSPSASSNKKNI | ||||||
Region | 1336-1628 | Shikimate dehydrogenase | ||||
Sequence: AKQFYLFGTPISQSLSPLMHNTSFQSLGLPYTYGLHETATVDESVVAKMRSADFGGASVTIPHKIEIMSKLDEITDEAKAIGAVNTIVPIVDRQGKTILVGDNTDWLGIYYQIVRNLSSTTTIHPQNMSGLVIGAGGTSRAALYALYRLGVQEISIFNRTMVKAQAVADSFKNLFTVKILSANELLKNDDGAGTGFDLIISTVPGTIDSSAMFDDSIFGSISEKDKKGVAVELAYTPRFTRFLKLAAQAGWATVEGGQVLVEQGGWQALKWVGRKWDLESVLTQMDLVQAGRE | ||||||
Domain | 1341-1422 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPISQSLSPLMHNTSFQSLGLPYTYGLHETATVDESVVAKMRSADFGGASVTIPHKIEIMSKLDEITDEAKAIGAVNTI | ||||||
Domain | 1465-1524 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: GLVIGAGGTSRAALYALYRLGVQEISIFNRTMVKAQAVADSFKNLFTVKILSANELLKND |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,628
- Mass (Da)176,803
- Last updated2017-08-30 v1
- Checksum27C5C426D7350145
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 876-891 | Polar residues | ||||
Sequence: SSPSPSPSASSNKKNI |
Keywords
- Technical term