E5ADS1 · E5ADS1_LEPMJ
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1591 (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 | 50-52 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 87-90 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ETSK | ||||||
Binding site | 118-120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 123 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 134 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 143-144 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 150 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 156 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 165 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 183-186 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLES | ||||||
Binding site | 194 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 198 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 198-201 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 254 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 264 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 268-272 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 275 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 275 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 279 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 291 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 291 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 360 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 832 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 879-886 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1188 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1216 | 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Leptosphaeriaceae > Plenodomus > Plenodomus lingam/Leptosphaeria maculans species complex
Accessions
- Primary accessionE5ADS1
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-388 | 3-dehydroquinate synthase | ||||
Sequence: MATEGTSVEPTKVKILGKDSIVVDYGLWQGYIAQDLLSNIPSSTYVLITDTNIGPLYTPTFERAFSTAASTLSTTPRLLTYQIPPGETSKSRSTKAAVEDWLLSQGCVRDTVIIALGGGVIGDMIGYVAATYMRGIKFVNVPTTLLAMVDSSIGGKTAIDVPAGKNLVGAFWQPERIYIDLQFLESLPKREVINGMAEVVKTAAIWNEEEFTALEGNANTILAAIDQKPVHGRRNFDGIASILKRIVLGSVRVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQILHGECVAIGMVKEAELARYLGVLDPSAVARLTKCIASYGLPTSLADKTVRRRSANKHCPVDELIKIMAVDKKNAGAVKKIVLLSGIGRTYEKKASSVAD | ||||||
Domain | 81-362 | 3-dehydroquinate synthase | ||||
Sequence: YQIPPGETSKSRSTKAAVEDWLLSQGCVRDTVIIALGGGVIGDMIGYVAATYMRGIKFVNVPTTLLAMVDSSIGGKTAIDVPAGKNLVGAFWQPERIYIDLQFLESLPKREVINGMAEVVKTAAIWNEEEFTALEGNANTILAAIDQKPVHGRRNFDGIASILKRIVLGSVRVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQILHGECVAIGMVKEAELARYLGVLDPSAVARLTKCIASYGLPTSLADKTVRRRSANKHCPVDELIKIMAVDKKN | ||||||
Domain | 407-844 | Enolpyruvate transferase | ||||
Sequence: SDLDVTCTPPGSKSISNRVLVLAALGTGPCRITNLLHSDDTQVMLDALAKMQGASFAWEDDGKVLVVTGNGGNLKATSSELYLGNAGTAARFLTSVTALCRPVESITSTIVTGNARMKERPIAPLVKSLRTMGVEIEYVEKEGGLPLRIQACSGFGSDSFTGDIELTANVSSQYVSSILLSAPYSKKPVTLRLVGGKVISQPYIDMTIAMMASFGVQVERSASDPNTYHIPNKPYTNPSTYEVESDASSATYPLAIAAITGTTCTVPNIGSGSLQGDARFAIEVLRPMGCKVEQSKTSTTVTGPPRGELKAVKEIDMEPMTDAFLTASVLAAVASSDGTSTTTRIYGIANQRVKECNRIQAMEDELAKFGVTCRQFDDGIEVDGKGYDLATPQVGIHCYDDHRVAMSFAVLSLVAPAPVLILEKDCTGKTWPGYWDSL | ||||||
Region | 872-1064 | Shikimate kinase | ||||
Sequence: DRSIFIIGMRGAGKTTAGGWAARTLGRPLIDLDTALEEHVGMTIPEFISTRGWDGFRDEELQLLKRTVKEKPTGYVFACGGGIVESPEAREVLVDWHKQGGIVLLVSRDITKVVEFLQIDKSRPAYVEDIMPVWLRRKPFYDQCSNYRFHSQALESVGLASTQAQFARFLNTITGKNSVLKALKKKKHSFFVC | ||||||
Region | 1065-1285 | 3-dehydroquinase | ||||
Sequence: LSAPELQSCIQTLPEIVVGADAVELRVDLLVDPNGQEGLPTPEYVIEQLTILRTVTTTPIIFTIRTKAQGGKFPDTAYDEARALYLTALRLGCEFVDLEMTMSEDILREVSEGRGYTEIIASHHDPKSELNWSNGSWMKYYNRALQYGTVIKLVGVAQSIKDNFALAEFKSWADTAHPVPLIAINMGEHGKLSRILNGFLTPVSHPLLPSATAPGQLSAAD | ||||||
Region | 1298-1591 | Shikimate dehydrogenase | ||||
Sequence: TKKFFIFGSPVSQSPSPRLHNRLFRETGLPHVYSRFETTDASSVRDIIRAPDFGGASVTIPLKQDVRTLLDGVGPEVEAIGALNTIVPETSIDETTGQEVTRLIGLNTDYLGMILVLKNAGALSQSGSALVIGGGGTSRGAIYALREMGYAPIYLLGRNLSKITALKDDFPAEYNVQIISSPEQVESLESMPAVAIGTIPADQPIDPAIRETLCALFAKAKKGEADVGSNGRILLEMAYKPPVTALIQLAQDAGWTTVNGLEVLVGQGVHQFEYWTGIKPLYAVAREAVMESSG | ||||||
Domain | 1303-1383 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: IFGSPVSQSPSPRLHNRLFRETGLPHVYSRFETTDASSVRDIIRAPDFGGASVTIPLKQDVRTLLDGVGPEVEAIGALNTI | ||||||
Domain | 1557-1587 | SDH C-terminal | ||||
Sequence: GLEVLVGQGVHQFEYWTGIKPLYAVAREAVM |
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
- Length1,591
- Mass (Da)171,501
- Last updated2011-02-08 v1
- Checksum46C864AF82A1BABF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FP929139 EMBL· GenBank· DDBJ | CBY01360.1 EMBL· GenBank· DDBJ | Genomic DNA |