A0A9P5SQV5 · A0A9P5SQV5_9FUNG
- ProteinPentafunctional AROM polypeptide
- GeneARO1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1610 (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 | 86-89 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EESK | ||||||
Binding site | 117-119 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 122 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 133 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 142-143 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 149 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 155 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 164 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 193 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 197 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 197-200 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 259 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 269 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
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 | ||||||
Active site | 284 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 296 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 296 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 365 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 837 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 894-901 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1213 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1242 | 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 > Podila
Accessions
- Primary accessionA0A9P5SQV5
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-393 | 3-dehydroquinate synthase | ||||
Sequence: MSHPNPHIQKVSILGSETIILGFHIFDYLLRDTLSNFKASTYVVVTDTNLQKLYLDRFLASFHRISQELSSGTLPRLLTYVIPPGEESKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQVPTTLLAMVDSSIGGKTAIDTPMAKNPIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNHDDFVLLENGAEAIRDAVLKPVRNVEFQGAILESRTAAQQLLLQVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLTRCIQAYGLPVTMEDKFVKNHIGNQYCSVDELMQVLRVDKKNMGSQKRIVMLSGIGQTLEQKPSNISD | ||||||
Domain | 80-367 | 3-dehydroquinate synthase | ||||
Sequence: YVIPPGEESKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQVPTTLLAMVDSSIGGKTAIDTPMAKNPIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNHDDFVLLENGAEAIRDAVLKPVRNVEFQGAILESRTAAQQLLLQVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLTRCIQAYGLPVTMEDKFVKNHIGNQYCSVDELMQVLRVDKKN | ||||||
Domain | 417-849 | Enolpyruvate transferase | ||||
Sequence: TLSPPGSKSISNRALVLAALGQGTCRLTGLLHSDDTQVMLTALTKLGAATFEWENNGDTLVVHGNGGKMHIPDSELYLGNAGTAARFLTTVSVLVPPSSISGQKTILTGNARMKQRPIAPLIDALTANGSELKYMEGQGCLPLEVTPFSHGLAGGEIQLAASISSQYVSSILLCAPYATKEPVTLVLTGGQVISQPYIDMTIAMMKSFGVNVEALPNNTYRIPQVHYVNPAAYLVEADASSATYPLAIAAITGTTCTVPNIGSASLQGDAGFAVNVLRPMGCTVVQTETSTTVIGPAIGTLKPLAHIDMETMTDAFLTASVLAAVTQPATPGAENITRISGIANQRVKECNRIAAMMHELGKFGVTTSETPDGIIVHGHDIASLTPPKDGVKCYDDHRVAMSFSVLASVVPGGTIIREKKCVEKTWPTWWDDL | ||||||
Region | 1091-1311 | 3-dehydroquinase | ||||
Sequence: LTFPDISPALPHLSKLTLGSDVIELRVDLLKSSDASGISFRDHVAQQVSLLRRHSDLPILYTVRSVSQGGQWPDKDIDGMVSLLKDGLEWGVEYLDVEIGLPRSRIDEVLPKKGNTLIVASWHDCKGTVRWNSDTMEAQYKLAHSISPDVIKLIGTATSMKDNFDCSEFAARHTKANDLPLIAMNMGAQGQLSRVLNNYLTPVTHKLLPVKAAPGQLTARD | ||||||
Region | 1324-1610 | Shikimate dehydrogenase | ||||
Sequence: AKQFYLFGTPIRQSLSPLMHNTSFQSLGLPYTYDLHETETVDESVVAKMRSKDFGGASVTIPHKIDVMSKLDEITEEAKAIGAVNTVVPVEQEGKPSILVGDNTDWLGIYYQIERNLSSTSVAQPQQMKGLVLGAGGTSRAALYALHRLGVEDISIFNRTMVKAQAVADSFKNLFDVKVLSSNDLLKGSSASGFDLVVSTVPGTIESASMFDDSVFGSAKKGVAVELAYTPRFTRFLKMAQQSGWATVEGGQVLVEQGGWQALKWVGRRWDLESVQQQMDLVQAGRE | ||||||
Domain | 1329-1410 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIRQSLSPLMHNTSFQSLGLPYTYDLHETETVDESVVAKMRSKDFGGASVTIPHKIDVMSKLDEITEEAKAIGAVNTV | ||||||
Domain | 1447-1508 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: QPQQMKGLVLGAGGTSRAALYALHRLGVEDISIFNRTMVKAQAVADSFKNLFDVKVLSSNDL |
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
- Length1,610
- Mass (Da)175,192
- Last updated2023-09-13 v1
- Checksum0C82F6DA224CF172
Keywords
- Technical term