A0A8H7PW36 · A0A8H7PW36_MORIS
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1609 (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 | 51-53 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 93-96 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ELTK | ||||||
Binding site | 124-126 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 129 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 140 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 149-150 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 156 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 162 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 171 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 172 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 189-192 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLQT | ||||||
Binding site | 200 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 204 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 204-207 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 266 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 276 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 287 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 287 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 291 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 303 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 303 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 372 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 846 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Active site | 1226 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1254 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Umbelopsidomycetes > Umbelopsidales > Umbelopsidaceae > Umbelopsis
Accessions
- Primary accessionA0A8H7PW36
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-400 | 3-dehydroquinate synthase | ||||
Sequence: MSPAPSEIEPLVTKVSILGSESIILGFHLTEYILKDILTNIPASNYVIITDTNLAPIYLPNLVERFNHHSAEISAAKGQKASRLFTRALPPGELTKSRSTKAEIEDWLLSNAVTRDTCFIAMGGGVIGDLIGFVAATFMRGVPVVQMPTTLLSMVDSAIGGKTAIDTPQGKNLVGAFWQPKRIYIDLAFLQTLPEREFSNGMAEVIKTAAIWCEEDFVKLENGVEKIREAVLGKSNRVPFQGATLETRTEGQTLLMDVVSASARVKAYVVTEDEREGGLRGLLNFGHSIGHGIEALVSPMMLHGECVSVGMIKEAELSRNLGHLNQVAVGRLTRCLASYGLPVSMDEKRVRDLIGTAYCHVDDIMEVMKVDKKNQGDKKRIVLLAAIGKTLEPRASVVAD | ||||||
Domain | 89-374 | 3-dehydroquinate synthase | ||||
Sequence: LPPGELTKSRSTKAEIEDWLLSNAVTRDTCFIAMGGGVIGDLIGFVAATFMRGVPVVQMPTTLLSMVDSAIGGKTAIDTPQGKNLVGAFWQPKRIYIDLAFLQTLPEREFSNGMAEVIKTAAIWCEEDFVKLENGVEKIREAVLGKSNRVPFQGATLETRTEGQTLLMDVVSASARVKAYVVTEDEREGGLRGLLNFGHSIGHGIEALVSPMMLHGECVSVGMIKEAELSRNLGHLNQVAVGRLTRCLASYGLPVSMDEKRVRDLIGTAYCHVDDIMEVMKVDKKN | ||||||
Domain | 428-858 | Enolpyruvate transferase | ||||
Sequence: TLSTPGSKSISNRVLLIASLGAGTTRIKGLLHSDDTQFMRAALKDLGAADFDWEDNGDTLVVKGGGGKLRVPDKELYVGNAGTASRFLTTVLALIQERTGDQPEAAILTGNARMKQRPIAPLLTALIANGAKIKSTEKEGFLPIAVKPNGGFKGGRIELAASISSQYVSSILLCAPYAQEPVELVLTGGQVISQPYIDMTIAMMESFGVNVDRLPNNTYRIAQAVYQNPDVYMVESDASSATYPLAIAAITGTTCTVSNIGTASLQGDATFAVNILRPMGCTVMQTESSTTVTGPPVGQLRPIPTVDMETMTDAFLTASVLAAATQAPEGTENITRITGIANQRVKECNRIAAMVHELTKFGVTCSELPDGIQIHGKPIKDLKAPAEGVHCYDDHRVAMSFAVLSTVVPNGTIIQEKKCVEKTWPQWWDDL | ||||||
Region | 1334-1609 | Shikimate dehydrogenase | ||||
Sequence: AKKFYLFGTPIAHSMSPTLHNTGFHTIGLPYQYELLECSSVAYAEHVLYEENFGGASVTIPHKISIMKYLDEVTDNVKAIGAVNTVYPVYVKDENGEMKRQLHGENTDYLGIKGCVQKLLLNPDNVAEGLVIGSGGTSRAALYALHTLGVKKIHLWNRTISKAHELRDHFAQYFEVNVIESLEADIHPQVIISTIPADNGVKVPDALFGGIRGICCDMAYKPRRTELLKQAEQHGWSTVEGIEVLIEQGYGQFKIWTNKVAPKQAMATEVNKKYDL | ||||||
Domain | 1339-1419 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIAHSMSPTLHNTGFHTIGLPYQYELLECSSVAYAEHVLYEENFGGASVTIPHKISIMKYLDEVTDNVKAIGAVNTV | ||||||
Domain | 1462-1528 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: GLVIGSGGTSRAALYALHTLGVKKIHLWNRTISKAHELRDHFAQYFEVNVIESLEADIHPQVIISTI | ||||||
Domain | 1574-1600 | SDH C-terminal | ||||
Sequence: GIEVLIEQGYGQFKIWTNKVAPKQAMA |
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
- Length1,609
- Mass (Da)176,542
- Last updated2022-01-19 v1
- ChecksumD9F7766A5C6588F7
Keywords
- Technical term