A0A0C3HLM9 · A0A0C3HLM9_OIDMZ
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1580 (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 | 44-46 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 81-84 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ENSK | ||||||
Binding site | 112-114 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 128 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137-138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 144 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 150 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 159 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 160 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 177-180 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLNT | ||||||
Binding site | 188 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 192 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 192-195 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 246 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 256 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 260-264 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 267 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 267 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 271 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 283 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 283 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 352 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 819 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 866-873 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1176 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1204 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
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 | |
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 > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Myxotrichaceae > Oidiodendron
Accessions
- Primary accessionA0A0C3HLM9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 106-127 | Helical | ||||
Sequence: VIIALGGGVVGDLLGFVAATYM |
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-380 | 3-dehydroquinate synthase | ||||
Sequence: MAAPTKISILGRESIVADYGIWGEYIVRDLLSNISSTTYLLVTDTNLGPIYKNTFEKAFSDAAGALSPNPRLLIKEIPPGENSKSRQGKADIEDWMLRNLCGRDTVIIALGGGVVGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLLGAIWQPTRIYIDLEFLNTLPEREFINGMAEVIKTAAISDEQEFTALENNAASILAAARSKPSTGRFDQVRNVLKQHIVASARHKAYVVTADEHEGGLRNLLNLGHSIGHAIETILTPQILHGECVAIGMVRELELARYLGVLKAVNVSRMIKCLSSYGLPTSLKDPRVKKFTAGKHCSIDQIMVNMALDKKNDGTKKKIVLLSAIGRTYEPKASNVAD | ||||||
Domain | 76-354 | 3-dehydroquinate synthase | ||||
Sequence: EIPPGENSKSRQGKADIEDWMLRNLCGRDTVIIALGGGVVGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLLGAIWQPTRIYIDLEFLNTLPEREFINGMAEVIKTAAISDEQEFTALENNAASILAAARSKPSTGRFDQVRNVLKQHIVASARHKAYVVTADEHEGGLRNLLNLGHSIGHAIETILTPQILHGECVAIGMVRELELARYLGVLKAVNVSRMIKCLSSYGLPTSLKDPRVKKFTAGKHCSIDQIMVNMALDKKN | ||||||
Domain | 406-831 | Enolpyruvate transferase | ||||
Sequence: SPPGSKSISNRALVLAALGSGTVRIKNLLYSDDTEVMMDALEQLGAASFAWEEEGEVLVVHGNGGRLQATATELYLGNAGTASRFLTTVATLATKGFADYNILTGNNRMKQRPIGDLVNALQANGAGIDYLESTGSLPLKIAASSGLHGGRINLAAKVSSQYVSSLLMCAPYTKEPVTLKLGGKPISQLYIDMTTAMMRSFGINVEKSTTEAYTYHIPQGAYVNPPEYVIESDASSATYPLAVAALTGTTCTVPNIGSASIQGDARFAVKVLRPMGCKVEQTATSTTVTGPKDGVLRPLPNINMEPMTDAFLGASVLAAVAQGEGSNHTTRIYGIANQRVKECNRIEAMREELAKFGVVCREHDDGLEIDGIDRSALRHPVEGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPTYWDML | ||||||
Region | 1053-1273 | 3-dehydroquinase | ||||
Sequence: LTLPDLRGTGDLLRIVSSGSDAVELRVDLLKDPSSSTELPSLEYVAEQISFYRSRVSVPIIFTIRTKSQGGRFPDNAHEAAFDLIRLAIRSGCEFVDLEITFPDDLLRSIAETKGYSKIIASHHDPQGKLNWSSGSWIQYYNKALQCGDIIKLVGVAKNLNDNAALQEFKDWAEKAHSIPVICINMGDKGQLSRILNRFMTPVSHPRLPFKAAPGQLSAAE | ||||||
Region | 1286-1580 | Shikimate dehydrogenase | ||||
Sequence: PKKFALFGKPIEASRSPVLHNRLFKIAGLPHNYTRLETDRAQDVKEFIRSPDFGGASITIPLKLDVIPLVDDVLDEAKVIGAINTIVPVEAEDGTTRLIGRNTDWQGMVRCLREVGAYGGEVASNALVVGAGGTARAAVYALHSMGYSPVYLLGRSPTNIENMASTFPADFDIRILTDITEVKTVPRVIISTIPGDKPMDASLREVLCSIFQRGKDIDRVAKGQGVGPHQRVLLEMAYKPSATPLMQLAADSGWVTIPGSEALVGQGIYQFEYWTGISPVYEDAKNAVLGTNGRE | ||||||
Domain | 1291-1371 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGKPIEASRSPVLHNRLFKIAGLPHNYTRLETDRAQDVKEFIRSPDFGGASITIPLKLDVIPLVDDVLDEAKVIGAINTI |
Sequence similarities
Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase 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 sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,580
- Mass (Da)172,024
- Last updated2015-04-01 v1
- Checksum1C338C5F5287FE42
Keywords
- Technical term