Q6FIV4 · ARO1_CANGA
- ProteinPentafunctional AROM polypeptide
- GeneARO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1579 (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 | 40-42 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSN | ||||||
Binding site | 75-78 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EANK | ||||||
Binding site | 106-108 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGI | ||||||
Binding site | 111 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 131-132 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 138 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 144 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 153 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 154 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 171-174 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: WLQS | ||||||
Binding site | 182 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 186 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 186-189 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 249 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 259 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 263-267 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 270 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 270 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 274 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 286 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 286 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 355 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 844 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 886-893 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRAAGKT | ||||||
Active site | 1189 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1218 | 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 > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Nakaseomyces
Accessions
- Primary accessionQ6FIV4
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000406711 | 1-1579 | Pentafunctional AROM polypeptide | |||
Sequence: MLVKVPILGRETIHVGYGVRSHIVETIVGLKSSTYVVINDSNVGRVPYFQELLSDFEAQLPAGSRLLRYVVKPGEANKTRATKEQIEDYLLSEGCTRDTVIVAVGGGIIGDMIGYVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPEFVLVDIKWLQSLPKREFINGMAEVIKTACIWNADEFQRLETHADEFLHVVNTPKISEKEGFQLYDTDIESIKEHIFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYLGILSATQVARLSKILVAYGLPVSKDEKWFRELTLNKKTPLDTLLKKMSIDKKNDGSKKKVVLLETIGKCYGKSAHVVSDEDLRFVLTDETLVYPFNNIPRDQNKTVTPPGSKSISNRALVLAALGKGTCRIKNLLHSDDTKHMLTAVQELKGANISWEDNGETVVLEGQGGSTLVACENDLYLGNAGTASRFLTSVAALVNSTSQKDHVILTGNARMQQRPIGPLVDSLRNNGIKIDYVKNEGCLPLKVHTDSVFKGGRIELAATVSSQYVSSILMCAPYAENPVTLALVGGKPISILYVEMTIKMMEKFGIKVEKSTTEEYTYIIPKGHYVNPAEYVIESDASSATYPLAFAALTGTTVTVPNIGSASLQGDARFATDVLQPMGCSVTQTATSTTVTGPPVGHLKPLKHVDMEPMTDAFLTACVVAAVAHDNDPTSKNTTTIEGIANQRVKECNRIEAMCTQLAKFGVRTNELPDGIQVHGLHSINDLKVPSIGNEAVGVCTYDDHRVAMSFSLLAGMVNSEQPNSSNPTPVRILERHCTGKTWPGWWDVLHTELGAQLDGAEPLELNSMKNAKKSVVIIGMRAAGKTTISRWCAAALGYKLVDLDTLFEERYGHGMIKDFVSQHGWEKFREEEARIFKEVIENYGDAGYVFSSGGGLVESSESRRILKSFSKSGGYVLHLHRDIEETIMFLQKDPTRPAYVEEIREVWNRRESWYKDCSNFSFFAPHCNSEVEFQNLRRAFTKFIRTITGVTTVDIPTRRSAFVCLTFENLTEYTNSLKAITYGCDAVEVRVDHLSNMDEDFVSKQISILRASTDGLPIIFTVRTKKQGGKFPDEDYETLQKLLITALKVGVDYIDLELTLPIGIQYKVLNMKRNTKIIGSHHDFASAYPWDHSEWENRYNQALAMDVDIVKFVGMAKSFEDNLMLERFRDSHTTKPLIAINMGAHGRVSRVLNTILTPVTSEHLSEVAAPGQLTVAEINRIYTEMGGITKKDFFVVGSPIGHSRSPVLHNTGYSVLGLPHHFDKFETTSAEEVKKHLLDNKANLGGLAVTIPLKLDIIKYMDELTESAKVIGAVNTVIPLGNSKFKGDNTDWLGIRNSLVSNGVPESVSGLSGLVVGAGGTSRAAIFALHKLGCQKIFIVNRTTEKLEELVKFFPEEYNIVPIKEAEEAEAVNETIGVAVNCVPADKPLDAKLESLLERLLLKSSHTHFVSTLVEAAYKPSVTPVMKLAKDKYQWRVVPGAQMLVHQGVAQFETWNNCRAPFKAIYDAVTEI |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-383 | 3-dehydroquinate synthase | ||||
Sequence: MLVKVPILGRETIHVGYGVRSHIVETIVGLKSSTYVVINDSNVGRVPYFQELLSDFEAQLPAGSRLLRYVVKPGEANKTRATKEQIEDYLLSEGCTRDTVIVAVGGGIIGDMIGYVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPEFVLVDIKWLQSLPKREFINGMAEVIKTACIWNADEFQRLETHADEFLHVVNTPKISEKEGFQLYDTDIESIKEHIFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYLGILSATQVARLSKILVAYGLPVSKDEKWFRELTLNKKTPLDTLLKKMSIDKKNDGSKKKVVLLETIGKCYGKSAHVVSD | ||||||
Region | 396-862 | EPSP synthase | ||||
Sequence: VYPFNNIPRDQNKTVTPPGSKSISNRALVLAALGKGTCRIKNLLHSDDTKHMLTAVQELKGANISWEDNGETVVLEGQGGSTLVACENDLYLGNAGTASRFLTSVAALVNSTSQKDHVILTGNARMQQRPIGPLVDSLRNNGIKIDYVKNEGCLPLKVHTDSVFKGGRIELAATVSSQYVSSILMCAPYAENPVTLALVGGKPISILYVEMTIKMMEKFGIKVEKSTTEEYTYIIPKGHYVNPAEYVIESDASSATYPLAFAALTGTTVTVPNIGSASLQGDARFATDVLQPMGCSVTQTATSTTVTGPPVGHLKPLKHVDMEPMTDAFLTACVVAAVAHDNDPTSKNTTTIEGIANQRVKECNRIEAMCTQLAKFGVRTNELPDGIQVHGLHSINDLKVPSIGNEAVGVCTYDDHRVAMSFSLLAGMVNSEQPNSSNPTPVRILERHCTGKTWPGWWDVLHTELGA | ||||||
Region | 881-1071 | Shikimate kinase | ||||
Sequence: SVVIIGMRAAGKTTISRWCAAALGYKLVDLDTLFEERYGHGMIKDFVSQHGWEKFREEEARIFKEVIENYGDAGYVFSSGGGLVESSESRRILKSFSKSGGYVLHLHRDIEETIMFLQKDPTRPAYVEEIREVWNRRESWYKDCSNFSFFAPHCNSEVEFQNLRRAFTKFIRTITGVTTVDIPTRRSAFVC | ||||||
Region | 1072-1284 | 3-dehydroquinase | ||||
Sequence: LTFENLTEYTNSLKAITYGCDAVEVRVDHLSNMDEDFVSKQISILRASTDGLPIIFTVRTKKQGGKFPDEDYETLQKLLITALKVGVDYIDLELTLPIGIQYKVLNMKRNTKIIGSHHDFASAYPWDHSEWENRYNQALAMDVDIVKFVGMAKSFEDNLMLERFRDSHTTKPLIAINMGAHGRVSRVLNTILTPVTSEHLSEVAAPGQLTVAE | ||||||
Region | 1297-1579 | Shikimate dehydrogenase | ||||
Sequence: KKDFFVVGSPIGHSRSPVLHNTGYSVLGLPHHFDKFETTSAEEVKKHLLDNKANLGGLAVTIPLKLDIIKYMDELTESAKVIGAVNTVIPLGNSKFKGDNTDWLGIRNSLVSNGVPESVSGLSGLVVGAGGTSRAAIFALHKLGCQKIFIVNRTTEKLEELVKFFPEEYNIVPIKEAEEAEAVNETIGVAVNCVPADKPLDAKLESLLERLLLKSSHTHFVSTLVEAAYKPSVTPVMKLAKDKYQWRVVPGAQMLVHQGVAQFETWNNCRAPFKAIYDAVTEI |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,579
- Mass (Da)174,232
- Last updated2004-07-19 v1
- Checksum51A302AA2AA7CCF8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR380959 EMBL· GenBank· DDBJ | CAG62820.1 EMBL· GenBank· DDBJ | Genomic DNA |