A0AAF0EFF5 · A0AAF0EFF5_9BASI
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1934 (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
- a 5,6-dihydrouridine in mRNA + NAD+ = a uridine in mRNA + NADH + H+This reaction proceeds in the backward direction.
- a 5,6-dihydrouridine in mRNA + NADP+ = a uridine in mRNA + NADPH + H+This reaction proceeds in the backward direction.
Cofactor
Protein has several cofactor binding sites:
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 | 454-457 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EESK | ||||||
Binding site | 485-487 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 490 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 501 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 510-511 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 517 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 523 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 532 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 533 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 550-553 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: WLLT | ||||||
Binding site | 561 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 565 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 565-568 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 629 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 639 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 643-647 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLVN | ||||||
Binding site | 650 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 650 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 654 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 666 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 666 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 735 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 1195 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 1251-1258 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRASGKS | ||||||
Active site | 1539 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1567 | 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 | flavin adenine dinucleotide binding | |
Molecular Function | metal ion binding | |
Molecular Function | shikimate 3-dehydrogenase (NADP+) activity | |
Molecular Function | shikimate kinase activity | |
Molecular Function | tRNA dihydrouridine synthase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | mRNA processing | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
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 > Basidiomycota > Ustilaginomycotina > Malasseziomycetes > Malasseziales > Malasseziaceae > Malassezia
Accessions
- Primary accessionA0AAF0EFF5
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-763 | 3-dehydroquinate synthase | ||||
Sequence: MTTSLRAEECVDEGRTKRLKLDTAMPPPSDPRMPAFDRGLFLAPMVRIGSLPSRLLALEYGADLVWSPEIVDRAIMGTTRRVNATTGLVEFMKGDKQIFSCHPVERPYLIYQVGSSTPENAAEAVRIVTAHDDVAGVDLNCGCPKPFSTLGGMGANLLTEPDLLCDILRQMRRAAPPHVSVTCKIRLLPTQAETLALVEQIVRTRTIRALTIHCRTKPMRPREPALVDRFREIAEHVQKVAAETGQDVPVIYNGDCFGASDWPRLRERTGASAVMMARAAELNPSCFQLQRQCVATVIAPRWMHYAVRFDNPFGNTKYCVTQLAFSTWAGARECEAPRASTGEPGEELPIPTMSEAGGGHKVPSYHAPPYTSELSGATIHELRCLDTRIQLGFHLVPHIVQTLYAELPTSSYVLFTDAHLEALGVIDKFREAFETYKPEGNTSRMLAHVLPPGEESKSRETKAGIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSAVGGKTAIDHPHGKNLIGAFHQPQFVFVDAAWLLTLPEREFANGMAEVVKTAAIWDADDFDKLESESQSIQAAVLSDEARSAPAGLGHTLDTRTPSQTLLLDVIRGSIGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPAILHGECVAVGMIFEAEIARAMHGLPQVVIGRLVRALTNYGLPVSLKDARIAALPQAQAITTARLLDIMRVDKKNAGTAKKIVLLSRIGATVEERASTVPD | ||||||
Domain | 42-303 | DUS-like FMN-binding | ||||
Sequence: LAPMVRIGSLPSRLLALEYGADLVWSPEIVDRAIMGTTRRVNATTGLVEFMKGDKQIFSCHPVERPYLIYQVGSSTPENAAEAVRIVTAHDDVAGVDLNCGCPKPFSTLGGMGANLLTEPDLLCDILRQMRRAAPPHVSVTCKIRLLPTQAETLALVEQIVRTRTIRALTIHCRTKPMRPREPALVDRFREIAEHVQKVAAETGQDVPVIYNGDCFGASDWPRLRERTGASAVMMARAAELNPSCFQLQRQCVATVIAPRWM | ||||||
Domain | 449-737 | 3-dehydroquinate synthase | ||||
Sequence: VLPPGEESKSRETKAGIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSAVGGKTAIDHPHGKNLIGAFHQPQFVFVDAAWLLTLPEREFANGMAEVVKTAAIWDADDFDKLESESQSIQAAVLSDEARSAPAGLGHTLDTRTPSQTLLLDVIRGSIGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPAILHGECVAVGMIFEAEIARAMHGLPQVVIGRLVRALTNYGLPVSLKDARIAALPQAQAITTARLLDIMRVDKKN | ||||||
Domain | 790-1207 | Enolpyruvate transferase | ||||
Sequence: PTPGSKSVSNRALVLAALAQGTCRLRNLLHSDDTQVMMNALRTLRAADFAWEEDGAQLVVHGGGGRLVACDKPVYLQNAGTAARFMTGVTTLLREGTVTLTGNARMKQRPIGPLVEALCANGAAIACVEAPGALPLRITGRGGLQGGVIRLAADVSSQYVSAVLLCAPYAQEAVTLELVGGKVISQPYIDMTVAMMQSFGVQVERVAEHVYRIPQQVYRAPDVYTVESDASSATYPLAMAAITGTTVTVPSIGSASLQGDARFARDVLAPMGCHVEQTEASTTVTGPPPGTLRQLNEVDMEPMTDAFMTAAVLFAVAQGTSTKITGIANQRVKECDRLRATVTELAKFGVQAHEHDDGIVVYGRPLSELQTSEPIACYDDHRIAMAFSVLASVVPSTRTTLEEKRCVEKTWPSWWDVL | ||||||
Region | 1648-1934 | Shikimate dehydrogenase | ||||
Sequence: AQRFALLGSPIAHSLSPLIHNTSFELLGLPHKYALHETASVEESVAALIRAPDFGGASVTIPHKCAITSLLHTLSPEAEAIGAVNTVVPQRDAGRLWLRGENTDWQAIYELAQRARPSAHTALVIGAGGSARAALYAMHRLGVSTILLYNRTYAKAMELAAAVPTEWHVQPLKTLSDAVAQAPDVIVSNVPAAGTSLTPGGADIVLPADLLSSAGGVAIDMAYRPEKTPLLTLVEQNPAWHGVRGLEILLTQAFHQFHLWTGLPAPHDEVARAAWQAYHAQAEAHST | ||||||
Domain | 1653-1734 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LLGSPIAHSLSPLIHNTSFELLGLPHKYALHETASVEESVAALIRAPDFGGASVTIPHKCAITSLLHTLSPEAEAIGAVNTV | ||||||
Domain | 1758-1839 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: LAQRARPSAHTALVIGAGGSARAALYAMHRLGVSTILLYNRTYAKAMELAAAVPTEWHVQPLKTLSDAVAQAPDVIVSNVPA |
Sequence similarities
Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 2nd section; belongs to the type-I 3-dehydroquinase 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 shikimate kinase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,934
- Mass (Da)209,009
- Last updated2024-05-29 v1
- Checksum98DE120A329F6C8C
Keywords
- Technical term