A0A8H7SY11 · A0A8H7SY11_9FUNG
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2149 (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 | 46-48 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSN | ||||||
Binding site | 88-91 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ETSK | ||||||
Binding site | 119-121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 124 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 135 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 144-145 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 151 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 157 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 167 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 184-187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLKT | ||||||
Binding site | 195 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 199 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 199-202 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: ELIK | ||||||
Binding site | 261 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 271 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 282 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 282 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 286 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 298 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 298 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 367 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 842 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Active site | 1223 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1251 | 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 > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Mucoraceae > Thamnidium
Accessions
- Primary accessionA0A8H7SY11
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-395 | 3-dehydroquinate synthase | ||||
Sequence: MTNKRDVAKISILGSESIIAGFHLSEYLIRDVLNNIPASNYVLVTDSNLAPIYLDTYTETFKKVSSEISTAKGEKEPRFFTRVLPPGETSKSRKVKADIEDWLLSNAVTRDTCFLAMGGGVIGDLIGYVAATFMRGAPFVQIPTTLLAMVDSSIGGKTAIDVPAGKNLIGAFWQPKRIFIDINFLKTLPEREFSNGMAELIKTAAISDENDFCKLENGVEAIRHAVLGNDSKVPDQGATLETRTDSQAMLMDVVLASARFKAFVVTNDEREGGLRGLLNFGHSIGHGIEAIVSPLMLHGECVSIGCMKEAELARNLGHLNQVAVGRLARCFQSYGLPICMEEKKVKDRIGSLYCHVDDIMEIMKVDKKNQGDKKRIVMLSAIGKTLEPRASVIAD | ||||||
Domain | 83-369 | 3-dehydroquinate synthase | ||||
Sequence: VLPPGETSKSRKVKADIEDWLLSNAVTRDTCFLAMGGGVIGDLIGYVAATFMRGAPFVQIPTTLLAMVDSSIGGKTAIDVPAGKNLIGAFWQPKRIFIDINFLKTLPEREFSNGMAELIKTAAISDENDFCKLENGVEAIRHAVLGNDSKVPDQGATLETRTDSQAMLMDVVLASARFKAFVVTNDEREGGLRGLLNFGHSIGHGIEAIVSPLMLHGECVSIGCMKEAELARNLGHLNQVAVGRLARCFQSYGLPICMEEKKVKDRIGSLYCHVDDIMEIMKVDKKN | ||||||
Domain | 423-854 | Enolpyruvate transferase | ||||
Sequence: KLTTPGSKSISNRALLIAALGKGTVRVKNLLHSDDTQFMLAALKSLDAADFEWEDNGETLVVHGGGGRLSVPDKEIYVGNAGTASRFLTSVLTMIPTAENSKNATAVLTGNARMKMRPIAPLLDALKSNGAEIVSLEKEGFLPVAVTPNGGLKGGRIELSASISSQYVSSILLCAPYAINEVELALVGGQVISQPYIDMTIAMMESFGAAVERLPENTYRIKQTTYKNPDHYVVESDASSATYPLAIAAITGTTCTVTSIGSSSLQGDATFAINVLRPMGCTVIQTETSTTVTGPPIGQLRPLPSIDMETMTDAFMTATVLAAVTSSADPKGENITRITGIANQRVKECDRIAAMVHELTKFGVQASELPDGIQIHGKPIKDLKAPKEGVHTYDDHRIAMSFSVFATVVPHGTIIMEKKCVEKTWPTWWDDL | ||||||
Region | 1331-2149 | Shikimate dehydrogenase | ||||
Sequence: AQSFWLIGTPIQHSMSPTLHNTGFQVLGLPHQYSLLECHMVEYAEDAIFKDSSFGGASVTIPHKVAIMKYLDEVTENAKAIGAVNTIFVRDTVVNGDKKRQFIGENTDYIGMKRRIQSLMLDPTNPPEQGLVIGAGGTARAALYTLQKIGIQKIYLWNRTISKARDLQKAFEGIIDVEVIDSLDAKIEPGVIISTVPADSGIELPEALYGGIKGIICDMAYKPRRTKLLLQAERKGWSCVEGIEILISQGIAQFELWTGKRAPVTKIEEEVLKKDHEDTYLDTKVLADLANQFNSPLLAELSKLKPNDYSIGLADPILRTFAQFKRAPKEEYIWESVQLPLENMEHVIDREGERQIKTEPTSPPSLHQMLPESRNAMALDKVLLNSNELRRQSILESPNKRQRIGTTSSPSHVSEIDRERRPHSLSAVTTASNQPISRQIRKIQSYPAAETEEQQPASPNKRLSTKHKNSLNLTIFAPSYHEQLAGVRSAPINSNFNRPIPNQPTQQHSRSNYANHGPMTASHNIAPASATIARPPFAHQPSPRRHEFAIPPIVPSQQQPPHSAHPTSRENVMYQQQYVPSPSLYGSHHHTKPQPSSYQRNHESQQKQPQQLAVNAASIPLPPKTPTTNSFAALQRQQYLQPFEHLFDTIETTRTLKSTLDDQIRRSSSLMQTLQASATTIEGLVRNQVKEAQWETMSQMEQTVDALVRRIEIVENRFDRNDSNGSNSAIRRQVQKQPDLRTDIGSLPSPLPSATREERAVAEDLVAFSERKRDGNELEELQTPPTIVRSQNDIGPQEYHNMLDTLRERLDRLERQIES | ||||||
Domain | 1336-1417 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LIGTPIQHSMSPTLHNTGFQVLGLPHQYSLLECHMVEYAEDAIFKDSSFGGASVTIPHKVAIMKYLDEVTENAKAIGAVNTI | ||||||
Domain | 1460-1525 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: GLVIGAGGTARAALYTLQKIGIQKIYLWNRTISKARDLQKAFEGIIDVEVIDSLDAKIEPGVIIST | ||||||
Domain | 1572-1602 | SDH C-terminal | ||||
Sequence: GIEILISQGIAQFELWTGKRAPVTKIEEEVL | ||||||
Compositional bias | 1721-1742 | Polar residues | ||||
Sequence: RQSILESPNKRQRIGTTSSPSH | ||||||
Region | 1721-1769 | Disordered | ||||
Sequence: RQSILESPNKRQRIGTTSSPSHVSEIDRERRPHSLSAVTTASNQPISRQ | ||||||
Compositional bias | 1755-1769 | Polar residues | ||||
Sequence: LSAVTTASNQPISRQ | ||||||
Region | 1824-1853 | Disordered | ||||
Sequence: SNFNRPIPNQPTQQHSRSNYANHGPMTASH | ||||||
Region | 1911-1942 | Disordered | ||||
Sequence: SPSLYGSHHHTKPQPSSYQRNHESQQKQPQQL | ||||||
Region | 2049-2088 | Disordered | ||||
Sequence: DRNDSNGSNSAIRRQVQKQPDLRTDIGSLPSPLPSATREE | ||||||
Compositional bias | 2050-2072 | Polar residues | ||||
Sequence: RNDSNGSNSAIRRQVQKQPDLRT | ||||||
Region | 2101-2123 | Disordered | ||||
Sequence: RKRDGNELEELQTPPTIVRSQND |
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 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
- Length2,149
- Mass (Da)238,006
- Last updated2022-01-19 v1
- ChecksumFE4ACC5331CA3955
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1721-1742 | Polar residues | ||||
Sequence: RQSILESPNKRQRIGTTSSPSH | ||||||
Compositional bias | 1755-1769 | Polar residues | ||||
Sequence: LSAVTTASNQPISRQ | ||||||
Compositional bias | 2050-2072 | Polar residues | ||||
Sequence: RNDSNGSNSAIRRQVQKQPDLRT |
Keywords
- Technical term