A0A0H5RKL3 · A0A0H5RKL3_9EUKA
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1516 (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.
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
- Recommended nameShikimate kinase
- EC number
- Short namesSK
- Recommended name3-dehydroquinate dehydratase
- EC number
- Short names3-dehydroquinase
- Recommended nameShikimate dehydrogenase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Sar > Rhizaria > Endomyxa > Phytomyxea > Plasmodiophorida > Plasmodiophoridae > Spongospora
Accessions
- Primary accessionA0A0H5RKL3
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 82-337 | 3-dehydroquinate synthase | ||||
Sequence: PGGELLKTRKMKACLEDYLLSNSCGRDTVLIGLGGGALGDLVGFVAATFMRGIPYIHIPTTLLSMVDSSIGGKTAINTDFGKNLLGAFYQPIAVFCDLDFLTVLPSRHISNGLAEIIKCGMIADRELFEYCADNAHLITSDRDQEALMHIICSSIAIKARIVSEDSHERGMRAILNFGHSIGHAIERILSPELLHGECVAIGMVYEAMISRSLGFCRSDVILRLCSCLKQYQLPVLMPSSLNHDDILAKMSSDKKN | ||||||
Domain | 378-801 | Enolpyruvate transferase | ||||
Sequence: SPTAQVQGIISVPGSKSISNRVLLLAALSNSKVTISGMLYSEDTEVMIKSLRALGVSINIDGNSNIHVQGNSGKFHAPSEPLFLANAGTASRFLTSVAALLPEGQDCIISGCQRMHDRPINDLVDVLRSCGVEVEYIGLRKDCLPIRVCGGGLKGGNLTLKGSISSQFVSSILMVAPFASNDINLTISGDKVVSRPYIDMTVALMSQFGVQVVCPNLKTFEIKKGQQYKCQDLINVEGDASSASYPLAIAAITRGKVTVSNVGQLSLQGDSQFCQVLQSMGCEVEQSPTTTTVKGPPDGKLLQAVDIDLNSMTDTFMTLAACAAVASGRSFIRNIDNQRVKECNRIQATVSELTKIGIKAGELSDGIWIEGDPLYSGPRAPTAIDCHSDHRIAMMFATLSCRFSNIIISDKNCVGKTYPEFWDD | ||||||
Domain | 1241-1322 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LFGYPIDRSPSSAMHNAAFTHLRLPHQYSNFSSELISSELRNCIKDHDFGGGSVTIPLKEKIHSLVDRVTDVAKKIGAINTL | ||||||
Domain | 1477-1502 | SDH C-terminal | ||||
Sequence: LLYQGIAAFRLWSGYKAPEAIMAKAI |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,516
- Mass (Da)165,207
- Last updated2015-10-14 v1
- Checksum24FB7A6A5AFA0A48