A0A9W8DSZ4 · A0A9W8DSZ4_9FUNG
- ProteinPentafunctional AROM polypeptide
- GeneARO1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2431 (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 | 58-60 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 105-108 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ETTK | ||||||
Binding site | 136-138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 141 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 161-162 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 168 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 174 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 183 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 184 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 201-204 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLRT | ||||||
Binding site | 212 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 216 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 216-219 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 279 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 289 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 300 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 300 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 304 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 316 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 316 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 387 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 859 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Active site | 1238 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1268 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K | ||||||
Binding site | 1763 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1767 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1846 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
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 > Zoopagomycota > Kickxellomycotina > Kickxellomycetes > Kickxellales > Kickxellaceae > Mycoemilia
Accessions
- Primary accessionA0A9W8DSZ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 2175-2197 | Helical | ||||
Sequence: VIAGIVIGAIAGLLVCIGLLVWL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 1763↔1767 | Redox-active | ||||
Sequence: CPDIC |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-415 | 3-dehydroquinate synthase | ||||
Sequence: MASIRHPYGTDLAIKPDVERLSILGNDTLILGYNLIDFMWHDIFTTLKKSSTYVLITDTNLAKLYIYLFKERFEAVKKHVENSQEHASKIAKGCRLLTYILPPGETTKSRATKSLIEDWLFSETCTRDTMFLALGGGVIGDLVGYVAATFMRGVPYVQIPTSLLAMVDSSIGGKTAVDTPAGKNLIGAFWQPEKNYMDISFLRTLPAREFSNGMAEVIKTAAIMDDKDFDILESKVDLIREAVLGVPSDADPMQGYTLDTRTEQQKLLLRVITGSARVKAYVVTVDVRETGLRGLLNFGHSIGHAIEGIMSPQLLHGECVSIGCVLESELSRRLGHLRQVSVARLTRCLKSYGLPVSIDDPIVLNLIGSKRKEYTVENLMRVLRVDKKNVGSQKRIVLLKRLGETVEPKPSNVDD | ||||||
Domain | 99-389 | 3-dehydroquinate synthase | ||||
Sequence: YILPPGETTKSRATKSLIEDWLFSETCTRDTMFLALGGGVIGDLVGYVAATFMRGVPYVQIPTSLLAMVDSSIGGKTAVDTPAGKNLIGAFWQPEKNYMDISFLRTLPAREFSNGMAEVIKTAAIMDDKDFDILESKVDLIREAVLGVPSDADPMQGYTLDTRTEQQKLLLRVITGSARVKAYVVTVDVRETGLRGLLNFGHSIGHAIEGIMSPQLLHGECVSIGCVLESELSRRLGHLRQVSVARLTRCLKSYGLPVSIDDPIVLNLIGSKRKEYTVENLMRVLRVDKKN | ||||||
Domain | 442-871 | Enolpyruvate transferase | ||||
Sequence: TLTPPGSKSISNRALLLAALGKGVCRIKNLLHSDDTQVMLTALQALGACSVAWEDDGDTLVLSGNGGKIVAPGSELYMGNAGTAARFLTTLVNLAAPHPEFGDKLVVTGNHRMKVRPIGALVDALRANGCSIEYKEKEGCLPLVVLAGGFKGRKIELAATISSQYVSSILLCAPCSPNPVILELVGGQVISQLYIDMTVEMMRTFGCNVERVNETTYYIPNTGYTNPAEYVVESDASSATYPLAVAAITGTTCIIPSLGSASLQGDARFAVDVLRPMGCTVEQTATSTKVTGPPIGQLRPLPQIDMEPMTDAFLTATALAAVAQDPSGKDSWTRIVGIANQHVKECDRILAMVTELEKFGVKAENLPDGINILGVNPKDLKTPDLGGIHCYDDHRVAMSFSVLSTVTPGSVVIQDRHCTAKTWPQWWDAL | ||||||
Region | 1349-2431 | Shikimate dehydrogenase | ||||
Sequence: PRQFYLFGTPIQASPSPVMHNAAFKATGLPHIYSLLESQTVEPLKDVITDPNFGGASVTIPHKQEIIPLLDELTPAGQRIGAINTIIPVRGSESDENSKFKLLGDNTDYLGIVNSIKRVLEANPTNEQPQLRRQLDVGLVIGAGGTTRAALYALHTLRVPTVYIFNRTFSKAQDLAKEFGDLFENLTAISSLDDLSQQSLWTSSKANVVIGTVPASAIEFSFPEFIFKSSSSEGASNSISIALDMAYKPRWTPLLETADRNGWATIPGVQVLIDQGVEQFKRWTKLNHPPYQIIHNAVMEKQYSTKSKKEETTSDRPKSDANSDKEKKGLFPKSGPLSLPGILLFLTTCMGMVYFYNSEKKRVNEERNKKLSESTAVGKPKLGGPFELIDHNGKEITDKDFLGKYLLVYFGFCHCPDICPDELDKIGEAIEILDKDPKTKDTITPVFITCDPQRDDPATIKQYLEGSIDQVRKACKAYRVYFSKPPNIKENQDYLVDHSIFSYLMDHNGGFVDIYGKDRTSTEMAETTYLWLVSGAQGVENAPTATATNTTSTATPTTKPKQKGREKSKGAKPPRIKYYGKLKPNDIKIPHIKTYTNNTNILPVIHLEAKLKRLGGTGVGEANQFSVFQPKASAYNNLKYNPVHRRQTVYGNTLVKEAPAVFYTGPKASNKNYQPWVTSDYYKIYPYPYWAYGKGAQKGPVYYVDEYKSGIHKCKDQLRNITLAGLTVQPIYDGLDLFGTGVNVPYEQFNNGTVSLYPCGKSSNITSNGCSHVLLDLVNGQIISGNAKIVKQNETGTFFKIYRDGKHTAVLRTQTLIRTGCKAHRPVIAGIVIGAIAGLLVCIGLLVWLPCRIAERKKRKKLMATATQSATPLYDTYRQPGAPGPANMAFSGSCASLSNNNNSEGRLNYSQQLPPQQSLTSLMPASVAGAVVPQPRSLTPNAQNRAQILSDTPTFTNPITGPGAVAAAPKLSGDSPSGSRFMLPSPIPPPVPEKDVAIPIYAQFSRQKQSANSSEESTRPKSKKKSWGFLDFSSSFANPDHQNKKTSGRESDTTTDESPPQKKENAIKKLSKLFTIAKNSHQL | ||||||
Domain | 1354-1434 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIQASPSPVMHNAAFKATGLPHIYSLLESQTVEPLKDVITDPNFGGASVTIPHKQEIIPLLDELTPAGQRIGAINTI | ||||||
Domain | 1487-1540 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: LVIGAGGTTRAALYALHTLRVPTVYIFNRTFSKAQDLAKEFGDLFENLTAISSL | ||||||
Compositional bias | 1650-1679 | Basic and acidic residues | ||||
Sequence: QYSTKSKKEETTSDRPKSDANSDKEKKGLF | ||||||
Region | 1650-1680 | Disordered | ||||
Sequence: QYSTKSKKEETTSDRPKSDANSDKEKKGLFP | ||||||
Compositional bias | 1890-1907 | Polar residues | ||||
Sequence: APTATATNTTSTATPTTK | ||||||
Region | 1890-1924 | Disordered | ||||
Sequence: APTATATNTTSTATPTTKPKQKGREKSKGAKPPRI | ||||||
Compositional bias | 1908-1924 | Basic and acidic residues | ||||
Sequence: PKQKGREKSKGAKPPRI | ||||||
Region | 2300-2418 | Disordered | ||||
Sequence: TPTFTNPITGPGAVAAAPKLSGDSPSGSRFMLPSPIPPPVPEKDVAIPIYAQFSRQKQSANSSEESTRPKSKKKSWGFLDFSSSFANPDHQNKKTSGRESDTTTDESPPQKKENAIKKL | ||||||
Compositional bias | 2376-2390 | Polar residues | ||||
Sequence: GFLDFSSSFANPDHQ | ||||||
Compositional bias | 2391-2417 | Basic and acidic residues | ||||
Sequence: NKKTSGRESDTTTDESPPQKKENAIKK |
Sequence similarities
Belongs to the EPSP synthase family.
Belongs to the SCO1/2 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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,431
- Mass (Da)266,124
- Last updated2023-11-08 v1
- ChecksumBFF5583DAF6962E2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1650-1679 | Basic and acidic residues | ||||
Sequence: QYSTKSKKEETTSDRPKSDANSDKEKKGLF | ||||||
Compositional bias | 1890-1907 | Polar residues | ||||
Sequence: APTATATNTTSTATPTTK | ||||||
Compositional bias | 1908-1924 | Basic and acidic residues | ||||
Sequence: PKQKGREKSKGAKPPRI | ||||||
Compositional bias | 2376-2390 | Polar residues | ||||
Sequence: GFLDFSSSFANPDHQ | ||||||
Compositional bias | 2391-2417 | Basic and acidic residues | ||||
Sequence: NKKTSGRESDTTTDESPPQKKENAIKK |
Keywords
- Technical term