A0A2S4VPY3 · A0A2S4VPY3_9BASI
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1607 (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 | 47-49 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSN | ||||||
Binding site | 81-84 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: EQSK | ||||||
Binding site | 112-114 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 128 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137-138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 144 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 150 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 159 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 160 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 177-180 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: YLET | ||||||
Binding site | 188 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 192 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 257 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 267 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 271-275 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLVN | ||||||
Binding site | 278 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 278 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 282 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 294 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 294 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 363 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 830 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 882-889 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGSGKS | ||||||
Active site | 1209 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1237 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Pucciniomycetes > Pucciniales > Pucciniaceae > Puccinia
Accessions
- Primary accessionA0A2S4VPY3
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-391 | 3-dehydroquinate synthase | ||||
Sequence: MAHLICDVQSVSILGKPSIRLGYHLAPYIAHTVLTELRSSTYILITDSNVSPRHVPALKAAFEDQLPASSRLLTYILPPGEQSKCREMKAVLEDWLLDHRCTRDTVVLALGGGVIGDLIGFVSATFMRGIRFCQIPTTLLAMVDSSVGGKTAIDTPLGKNLVGAFWQPSFIFIDASYLETLPEREFVNGMAEMIKTAAIWDESQFEKLESNVESIRSAVLSPPPRDPMNPFPGRDVGSRSQAQNLLLEVIADSVGVKSEVVTKDEKETGLRNLVNFGHTIGHAIEAVLTPAILHGECVSIGMILEAEVARARGCLSSSAVARLSKCLKAHGLPVSLNDPKIQSSPNASKLSLDRLLDLMSVDKKNEGKVKKIVLLSRIGKTFEERATGVED | ||||||
Domain | 75-365 | 3-dehydroquinate synthase | ||||
Sequence: YILPPGEQSKCREMKAVLEDWLLDHRCTRDTVVLALGGGVIGDLIGFVSATFMRGIRFCQIPTTLLAMVDSSVGGKTAIDTPLGKNLVGAFWQPSFIFIDASYLETLPEREFVNGMAEMIKTAAIWDESQFEKLESNVESIRSAVLSPPPRDPMNPFPGRDVGSRSQAQNLLLEVIADSVGVKSEVVTKDEKETGLRNLVNFGHTIGHAIEAVLTPAILHGECVSIGMILEAEVARARGCLSSSAVARLSKCLKAHGLPVSLNDPKIQSSPNASKLSLDRLLDLMSVDKKN | ||||||
Domain | 417-842 | Enolpyruvate transferase | ||||
Sequence: TLRTPGSKSISNRALILAALGNGTCRLKNLLHSDDTQVMIDALESMKGASFSWEDNGATLVVSGGGGQLSSPVNGKHVYLGNAGTAARFLTTVCSLVKSQDSSHSSTVITGNARMQERPIGPLVNALRTNGVQIEYLRNEGCLPLRISTEDGFPGGMIELAASVSSQYVSSVLLSAPFAQAPVTLSLVGGAVISQPYIDITISMMSTFGIHVERVKDSATGLPSNTYRIPNGTYTNPAVYEIESDASSATYPLAMAALNGLSMTLETIGSASLQDREGDKGHWTKQRLWLRQIGDIDMEEMTDAFLTACVLLGVAVQPSTKGQRTSTRIVGIANQRVKECNRIAAMVAELGKMGIRAEELDDGIEVFGTPVDDLAKCGDQVRIHCYDDHRIAMAFSVLGTVPGGKGLILNEKRCVEKTWPSWWDDL | ||||||
Region | 1323-1607 | Shikimate dehydrogenase | ||||
Sequence: PKQFWLFGNPIGQSRSPLIHGTGFTTLGLEGYRYEKCETSSVTNDTVLDKIHASDFGGASVTIPLKVEIIKHLDQLTPDAQAVGAVNTVVPVSQPCGKIKLLGANTDWQAIKAKIEANLPAQQALGLITPGQLVRASGVVIGAGGTARAAVYALHSLGYEQIYIHNRTRSKAEEVAKNFPSYFGIRVIDSLGYLCSGQEGVCSDKLEIPLGLFDRSGGGVVIEMSYSLGKSSPVLRAVENNVGWKSVDGFEVLIEQGARQFQLWTGKLLSLKAVSQAVYQEASSP | ||||||
Domain | 1328-1411 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGNPIGQSRSPLIHGTGFTTLGLEGYRYEKCETSSVTNDTVLDKIHASDFGGASVTIPLKVEIIKHLDQLTPDAQAVGAVNTV | ||||||
Domain | 1455-1504 | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | ||||
Sequence: LVRASGVVIGAGGTARAAVYALHSLGYEQIYIHNRTRSKAEEVAKNFPSY | ||||||
Domain | 1571-1600 | SDH C-terminal | ||||
Sequence: GFEVLIEQGARQFQLWTGKLLSLKAVSQAV |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,607
- Mass (Da)174,623
- Last updated2018-07-18 v1
- ChecksumB2F3E69E3C986DA9
Keywords
- Technical term