A0A1Y1W5F7 · A0A1Y1W5F7_9FUNG
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1560 (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 | 51-53 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 91-94 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ETSK | ||||||
Binding site | 122-124 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 127 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 138 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 147-148 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 154 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 160 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 169 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 170 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 198 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 202 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 202-205 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVVK | ||||||
Binding site | 264 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 274 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 285 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 285 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 289 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 301 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 301 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 373 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 807 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Active site | 1173 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1203 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Zoopagomycota > Kickxellomycotina > Kickxellomycetes > Kickxellales > Kickxellaceae > Linderina
Accessions
- Primary accessionA0A1Y1W5F7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 116-137 | Helical | ||||
Sequence: MVLALGGGVIGDLVGFVAATFM |
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-401 | 3-dehydroquinate synthase | ||||
Sequence: MSKTELQLAEVEKIPVLGSDSIVCGFHLTDYIWHDIFTNLTKASTYVLITDTNLAPLYLHKYQDSFARAWASINGSKASPRLLVRVLPPGETSKSRATKGEIEDWMLSQRCTRDTMVLALGGGVIGDLVGFVAATFMRGVPFIQIPTSLLAMVDSSIGGKTAIDTPAGKNLVGAFWQPKRIFMDMAVLSTLPAREFSNGMAEVVKTAAIWSPEEFDVLEASAESVRKAVLQGQSGDGLEGLTIATRSEAQKMLLRVIAASARVKAYVVTHDERESGMRGLLNFGHSIGHAIEAIVSPQVLHGECVAVGCVLEAELSRRLGYIGEVGVARLTRCLRAYGLPTAIDDPIIRRLVGDAKLKEVRPARLMEVMRVDKKNVGTQKRIVLLKRLGECVELKPSNVDD | ||||||
Domain | 86-375 | 3-dehydroquinate synthase | ||||
Sequence: VLPPGETSKSRATKGEIEDWMLSQRCTRDTMVLALGGGVIGDLVGFVAATFMRGVPFIQIPTSLLAMVDSSIGGKTAIDTPAGKNLVGAFWQPKRIFMDMAVLSTLPAREFSNGMAEVVKTAAIWSPEEFDVLEASAESVRKAVLQGQSGDGLEGLTIATRSEAQKMLLRVIAASARVKAYVVTHDERESGMRGLLNFGHSIGHAIEAIVSPQVLHGECVAVGCVLEAELSRRLGYIGEVGVARLTRCLRAYGLPTAIDDPIIRRLVGDAKLKEVRPARLMEVMRVDKKN | ||||||
Domain | 428-718 | Enolpyruvate transferase | ||||
Sequence: VVPPGSKSISNRALVLAALGSGECRIRNLLHSDDTQVMLSALQDMGGCGFSWEDDGDTLVVRGGGGQLSVPGSELYLGNAGTAARFLTTTVNLIGGDSGETVLTGNARMKQRPIGPLVDALRANGCQIVYEESQGSLPLRVTHTGKGFPGGTIELAATVSSQYVSSILLSAPYAQTPVHLVLVGGKVISQPYIDMTIAMMAQFGVNVERVSEKEYLIPTMPYTNPAEYVVESDASSATYPLAFAAITGSTVTVPNIGSASLQGDARFAVDVLRPMGCTVEQTATSTTVTGP | ||||||
Domain | 719-819 | Enolpyruvate transferase | ||||
Sequence: ARGVTRIRGIANQHVKECDRIAAMCDELAKFGVTCENHADGIDVHGVRISDLGPVSPSVHCYDDHRVAMSFSILSCVAPLGAEIRERRCVGKTWPQWWDVL | ||||||
Region | 849-1041 | Shikimate kinase | ||||
Sequence: SIVIIGMRGVGKSTLGQAAAEALGLEFVDMDAYLESKISKTIPEIIKADGWPAFRDHERAMLVQALEQEHPEGAVIACGGGVVESEQNRAYLKQYAKTGGAVVCLTPNMKHVAEYLEQDKTRPAYAITSDIYEVYQKRRPLYAECCNYEFLVDKSLVANAWPVIERDFVRLLNFATARSLNRVDLSSPSFFVS | ||||||
Region | 1284-1560 | Shikimate dehydrogenase | ||||
Sequence: ARSFYLFGTPIQHSPSPAMHNAGFAALGLPHMYRLNETSSADPLKAVIAAADFGGASVTIPYKQEIIPMLDELTDAAQTIGAVNTVIPEIRNGKRVLVGDNTDYLGICGCLERARATAGTQKFTSATALVIGAGGTSRAALYALYTLGVRNVALFNRTASRAHQLANEFSGLLNVSVVGQLLDAAELKPTYIIGTIPGCDLVIPEQLFGENGVALDMAYKPRWTPLLETAQRNKWNVVHGVEVLVEQGVHQLAKWTKLSPPVRIMREAVYSKYDAEF | ||||||
Domain | 1289-1369 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGTPIQHSPSPAMHNAGFAALGLPHMYRLNETSSADPLKAVIAAADFGGASVTIPYKQEIIPMLDELTDAAQTIGAVNTV | ||||||
Domain | 1403-1455 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: TQKFTSATALVIGAGGTSRAALYALYTLGVRNVALFNRTASRAHQLANEFSGL | ||||||
Domain | 1523-1552 | SDH C-terminal | ||||
Sequence: GVEVLVEQGVHQLAKWTKLSPPVRIMREAV |
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 dehydroquinate synthase 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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,560
- Mass (Da)168,003
- Last updated2017-08-30 v1
- Checksum75F36D45E0E5CFFB
Keywords
- Technical term