Q5XNP0 · ARO1_SCLSC
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1590 (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
- 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
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 | 49-51 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 86-89 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ENSK | ||||||
Binding site | 117-119 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 122 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 133 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 142-143 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 149 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 155 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 164 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 182-185 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLET | ||||||
Binding site | 193 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 197 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 197-200 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 253 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 263 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 267-271 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNILN | ||||||
Binding site | 274 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 274 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 278 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 290 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 290 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 359 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 823 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 870-877 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1179 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1207 | 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
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Sclerotinia
Accessions
- Primary accessionQ5XNP0
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000406740 | 1-1590 | Pentafunctional AROM polypeptide | |||
Sequence: MGSTTFENPTRIEILGKEDIIVDFDIWRNFVAEDLLSDLPSSTYVLITDTNLSPLYVPAFQQSFEALAAKSSSTPRLLTYEIPPGENSKSRETKAEIEDWMLSHQCTRDSVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAFWQPQRIYIDLRFLETLPVREFINGMAEVVKTAAIWDEAEFSALEDNANLIMTTIRAKNTDCSTRLGPIRDILKRIVLGSAKTKADVVSADEREGGLRNILNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARHLGVLKPGAVARLVKCIASYGLPTSLADKRIQKLTAGKLCPVDVLLEKMGVDKKNDGRKKKIVLLSAIGKTYEPKASVVEDRSIRVVLSDSVEVRPSVPETLNVEVTPPGSKSISNRALVLAALGTGPCRIKNLLHSDDVEFMLTSIGKLGGATYAWEDAGEVLCVQGKGGDLHASPTELYIGNAGTASRFLTTVVSLCKPSASTKSTILTGNARMKVRPIGPLVDSLRANGVDIEYLEKEHSLPLNVAASGGFTGGDINLAATVSSQYVSSLLMCAPYAKNPVTLRLVGGKPISQLYIDMTTAMMAAFGIHVVRSQTGEHTYHIPQGVYKNPEEYVVESDASSATYPLAVAATSGTTCTIPNIGCKSIQGDARFAIDVLKPTGCKVVQTDYSTTVTGPPIGSLQAIEEVDMEPMTDAFLTASVLGAVAKGTTKIRGIANQRVKECNRIKAMKDELAKFGVTCRELEDGIEVDGVPIKDLKHPAEGIHCYDDHRVAMSFSVLSVAASQPVLIEERECVGKTWPGWWDILSKSFQVELAGKEVKATHSKKIGIPTLPDKSIFIIGMRGAGKTTAGAWAAKILGRPYKDLDVELERISGMSIPDMVRSKGWDFFRAAELDLLKHCLTDQPEKHVFACGGGVVEMPEARELLINFHKSGGIVLLVHRDTEQVMDYLRIDKTRPAYVEDMMGVYSRRKPWFNECSNFQYHSKGSGASALSVAEQDFARFLHHISGKSLHFDEMRNKPQSFFVSLTMPDISGAAYILPSVAVGSDAVEVRVDLLEDPSSTNGIPGTDFLSVQIAHLRSVVHLPVIFTVRTVSQGGRFPDAAHEEALKLYKLAVKMGIEYIDLEIAFPDELLQEVTEAKGFSRIIASHHDPQGTLSWKNGGWFQHYNRALQYGDIIKLVGSAKSIEDNFALAKFKKTMAAAHDTPLIAINMGVTGKLSRVLNGFMTPVSHPSLPFKAAPGQLSAAEIRSTLSTLGEIEPKSFYLFGTPISQSRSPALHNTLFKQTGLPHRYSRLETDRVADVQDVIRAPDFGGASVTIPLKLDIIPLLDSVTDAVKVIGAVNTIIPTPDNPPRLVGENTDWLGMTHSLMSASHTPSPVDSPSPALVIGAGGTARAAIYALHSLGHSPIYMVARTPSKLDTLINSFPSSFNIIPLPSTTSATELTTPPAVAISTIPADRPIESNMRETLAVLLRHEKKDEGKQRTLLEMAYKPSQTPLMRMAEDAGWVAIPGLEVLSAQGWYQVSLFPFHLLVCYEVIFLNGFTKIYRLVSKMDKHPTFVC |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-387 | 3-dehydroquinate synthase | ||||
Sequence: MGSTTFENPTRIEILGKEDIIVDFDIWRNFVAEDLLSDLPSSTYVLITDTNLSPLYVPAFQQSFEALAAKSSSTPRLLTYEIPPGENSKSRETKAEIEDWMLSHQCTRDSVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAFWQPQRIYIDLRFLETLPVREFINGMAEVVKTAAIWDEAEFSALEDNANLIMTTIRAKNTDCSTRLGPIRDILKRIVLGSAKTKADVVSADEREGGLRNILNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARHLGVLKPGAVARLVKCIASYGLPTSLADKRIQKLTAGKLCPVDVLLEKMGVDKKNDGRKKKIVLLSAIGKTYEPKASVVED | ||||||
Region | 400-841 | EPSP synthase | ||||
Sequence: VRPSVPETLNVEVTPPGSKSISNRALVLAALGTGPCRIKNLLHSDDVEFMLTSIGKLGGATYAWEDAGEVLCVQGKGGDLHASPTELYIGNAGTASRFLTTVVSLCKPSASTKSTILTGNARMKVRPIGPLVDSLRANGVDIEYLEKEHSLPLNVAASGGFTGGDINLAATVSSQYVSSLLMCAPYAKNPVTLRLVGGKPISQLYIDMTTAMMAAFGIHVVRSQTGEHTYHIPQGVYKNPEEYVVESDASSATYPLAVAATSGTTCTIPNIGCKSIQGDARFAIDVLKPTGCKVVQTDYSTTVTGPPIGSLQAIEEVDMEPMTDAFLTASVLGAVAKGTTKIRGIANQRVKECNRIKAMKDELAKFGVTCRELEDGIEVDGVPIKDLKHPAEGIHCYDDHRVAMSFSVLSVAASQPVLIEERECVGKTWPGWWDILSKSFQV | ||||||
Region | 863-1055 | Shikimate kinase | ||||
Sequence: DKSIFIIGMRGAGKTTAGAWAAKILGRPYKDLDVELERISGMSIPDMVRSKGWDFFRAAELDLLKHCLTDQPEKHVFACGGGVVEMPEARELLINFHKSGGIVLLVHRDTEQVMDYLRIDKTRPAYVEDMMGVYSRRKPWFNECSNFQYHSKGSGASALSVAEQDFARFLHHISGKSLHFDEMRNKPQSFFVS | ||||||
Region | 1056-1276 | 3-dehydroquinase | ||||
Sequence: LTMPDISGAAYILPSVAVGSDAVEVRVDLLEDPSSTNGIPGTDFLSVQIAHLRSVVHLPVIFTVRTVSQGGRFPDAAHEEALKLYKLAVKMGIEYIDLEIAFPDELLQEVTEAKGFSRIIASHHDPQGTLSWKNGGWFQHYNRALQYGDIIKLVGSAKSIEDNFALAKFKKTMAAAHDTPLIAINMGVTGKLSRVLNGFMTPVSHPSLPFKAAPGQLSAAE | ||||||
Region | 1289-1590 | Shikimate dehydrogenase | ||||
Sequence: PKSFYLFGTPISQSRSPALHNTLFKQTGLPHRYSRLETDRVADVQDVIRAPDFGGASVTIPLKLDIIPLLDSVTDAVKVIGAVNTIIPTPDNPPRLVGENTDWLGMTHSLMSASHTPSPVDSPSPALVIGAGGTARAAIYALHSLGHSPIYMVARTPSKLDTLINSFPSSFNIIPLPSTTSATELTTPPAVAISTIPADRPIESNMRETLAVLLRHEKKDEGKQRTLLEMAYKPSQTPLMRMAEDAGWVAIPGLEVLSAQGWYQVSLFPFHLLVCYEVIFLNGFTKIYRLVSKMDKHPTFVC |
Sequence similarities
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate 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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,590
- Mass (Da)172,659
- Last updated2004-11-23 v1
- Checksum0EFD2D13CB685AD6