A0A017S5L2 · A0A017S5L2_ASPRC
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1582 (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: EVSK | ||||||
Binding site | 114-116 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 119 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 139-140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 146 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 161 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 162 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179-182 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLET | ||||||
Binding site | 190 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 194 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 194-197 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 250 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 260 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 264-268 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 271 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 271 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 275 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
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 | ||||||
Binding site | 356 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 824 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 871-878 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1180 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1208 | 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
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 > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus
Accessions
- Primary accessionA0A017S5L2
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-384 | 3-dehydroquinate synthase | ||||
Sequence: MSEPTKISILGRESIISDFGIWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAAGITPAPRLLVYYAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGSIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALENNAEVILNAVRSEVKPGQSRFEGIQDIIKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHVGVLKGVAVARVVKCIAAYGLPTSLKDAQIRKLTAGKHCSVEQLLFNMALDKKNDGPKKKVVLLSAIGRTHEPQASVVSN | ||||||
Domain | 77-358 | 3-dehydroquinate synthase | ||||
Sequence: APPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGSIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALENNAEVILNAVRSEVKPGQSRFEGIQDIIKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHVGVLKGVAVARVVKCIAAYGLPTSLKDAQIRKLTAGKHCSVEQLLFNMALDKKN | ||||||
Region | 397-842 | EPSP synthase | ||||
Sequence: VQPGVAPALSVTCAPPGSKSISNRALVLAALASGTCRVKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVNGKGGNLEATPSPLYLGNAGTASRFLTSVATLANASSADSSILTGNNRMKQRPIGDLVDALTANGAEIEYQEKKGSLPLKIAASGGFAGGSINLAAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVVESDASSATYPLSIAAITGTTCTVPNIGSKSLQGDARFAVDVLRPMGCTVEQTAASTTVTGVPGGALKPLPNVDMEPMTDAFLTASVLAAVAQGDNSKHTTRIYGIANQRVKECNRIQAMKDELAKFGVVCREHDDGLEIDGVDRSTLRQPAGGIFCYDDHRVAFSFSVLSLVAPQSTLILERECVGKTWPGWWDTLRQLFAV | ||||||
Domain | 406-836 | Enolpyruvate transferase | ||||
Sequence: SVTCAPPGSKSISNRALVLAALASGTCRVKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVNGKGGNLEATPSPLYLGNAGTASRFLTSVATLANASSADSSILTGNNRMKQRPIGDLVDALTANGAEIEYQEKKGSLPLKIAASGGFAGGSINLAAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVVESDASSATYPLSIAAITGTTCTVPNIGSKSLQGDARFAVDVLRPMGCTVEQTAASTTVTGVPGGALKPLPNVDMEPMTDAFLTASVLAAVAQGDNSKHTTRIYGIANQRVKECNRIQAMKDELAKFGVVCREHDDGLEIDGVDRSTLRQPAGGIFCYDDHRVAFSFSVLSLVAPQSTLILERECVGKTWPGWWDTL | ||||||
Region | 864-1056 | Shikimate kinase | ||||
Sequence: SASVFIVGMRGAGKTTTGHWIAQTLNRPFVDLDTELESSEGITIPDIIKQRGWQGFRDAELNILQRMMKERTTGYVFACGGGVVEIPEARKLLIDYHKGKGNVLLVMRDIKQVMDFLSIDQTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHSGSGALALPSEDFKRFLHVVTGQQDSLNVMKKKKESFFVS | ||||||
Region | 1057-1277 | 3-dehydroquinase | ||||
Sequence: LTLPDLRPSGDILDQVSIGSDAVELRVDLLKDPSSDNDVPSVDYVAEQVSFLRSRISLPLIFTIRTQSQGGCFPDDAHDAAMQLYKLALRSGSEFVDLEIAFPDEMLRAVTEMKGHSKIIASHHDPKGELSWANMSWMKFYNRALEYGDVIKLVGVAKNLDDNTSLRKFKTWAEEAHDVPLIAINMGDNGQLSRILNGFMTPVSHPALPFKAAPGQLSATE | ||||||
Region | 1290-1582 | Shikimate dehydrogenase | ||||
Sequence: AKKFAVFGSPVSASRSPILHNTLFNYMGLPHEYGRLETTNVEDVKDFIRSPDFGGASVTIPLKLDIMPLLDEVAEAAEIIGAVNTIVPVSNGEGKPARLVGYNTDWQGMQLSLRNAGVGNAAGDASAAVVGGGGTARAAIYALHQMGYSPIYIFGRSPAKLESMVSTFPTSYNIRVVEDVSKLDTVPNVAIGTIPGDKPIDPAMRENLCHLFDRTEQVDPDHIKSIDKSPRVLLEMAYKPAVTPLMQLANDSGWNTVPGLEVLVGQGVFQFKHWTDISPPYNDARDAVLGNSS | ||||||
Domain | 1295-1375 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: VFGSPVSASRSPILHNTLFNYMGLPHEYGRLETTNVEDVKDFIRSPDFGGASVTIPLKLDIMPLLDEVAEAAEIIGAVNTI | ||||||
Domain | 1548-1578 | SDH C-terminal | ||||
Sequence: GLEVLVGQGVFQFKHWTDISPPYNDARDAVL |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,582
- Mass (Da)171,118
- Last updated2014-06-11 v1
- Checksum8F5B99AD27E315D1
Keywords
- Technical term