A0A093ZYW5 · A0A093ZYW5_9PEZI
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3303 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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 | 1789-1791 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 1826-1829 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ESSK | ||||||
Binding site | 1857-1859 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 1862 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1873 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1882-1883 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 1889 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1895 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1904 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1905 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1922-1925 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLET | ||||||
Binding site | 1933 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1937 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 1937-1940 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 1993 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 2003 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 2007-2011 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 2014 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2014 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 2018 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 2030 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2030 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 2099 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 2562 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 2609-2616 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 2918 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 2946 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | RNA polymerase I complex | |
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 | DNA binding | |
Molecular Function | DNA-directed 5'-3' RNA polymerase activity | |
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 | DNA-templated transcription |
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 > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Pseudeurotiaceae > Pseudogymnoascus
Accessions
- Primary accessionA0A093ZYW5
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-2127 | 3-dehydroquinate synthase | ||||
Sequence: MNISQPVSSAIGSVDFAFLSPDEIKRLSVKAIQNPTTFDTLLNPVPGGLYDPALGAWGDIQCTTCHLGALSCPGHVGHITLPVPVYHPTFMDQLLRLLRAKCAYCHHFKMSRKDVNLYHCKLRLIQAGLLSAAEEVENIDLVAKKAAAVGQEDDSSSDSGDDNGVESTIKQRLSFVKKAIRDAKATPWDWKLEKNESVADARREVIKSFLKSITISKTCANCKAISNGFRKDRFVKIFEKPMTAKEEAKNAQQNLKAVNAMRVVSKDAGHAKNSNGYASDEGIADIDLSSNEEDEGEGDNLDVAGGLASRSTSGTTTISKQKPATTGERYVNPMEVRASLTLLFEKEQEILSLVYASRSSSKKAAVITAEFFFLQTLLVPPNKYRPEARTGAGEIAEAQQNALYKQILTAGHMTAQISKELDNPALADLKYRRRDFSDLQESWVKLQDSVNSLIDRDRNPIQGAAGKKNEDGIKQKLEKKEGLFRKNMMGKRVNFAARSVISPDPNIETNEIGVPPVFARKLTYPEPVTSHNFKELQQAVINGADKWPGAAAIENENGQVINLRTKTPDERQSLANQLLASSGIGANGARNKKVHRHLTNGDVVLMNRQPTLHKPSIMGHRARVLPGEKTIRMHYANCNTYNADFDGDEMNMHFPQNEVARAEALQIADTDHQYLAATAGKPLRGLIQDHISVSVWMTNRDTFFDRATYQQLVYNCLRPESGHIIGERIETVPPAIIKPFPQWTGKQIITTILKNITPLGYTPLNLISKSQVPFERWGPKSEEGQVFFQDGELITGILDKSQLGPSGGGLIHSLHEAHGPTVAGKMLSILGRLLTKFLHMRAFSCGMEDLLLTSEGEKTRKEKLKDVHLIGLEVATKYVTLEDRKPTANDPELRNRLEDVLRDDTKQEGLDVMMNGSSNKLSSEITKACLPLGLVKQFPKNQMQNMTVSGAKGSAVNANLISCNLGQQVLEGRRVPVMVSGKTLPCFKPFETNVRAGGYIANRFLTGIRPQEYYFHAMAGREGLIDTAVKTSRSGYLQRCLIKGMEGLKVEYDTSVRDSDGSMVQFLYGEDGLDVTKTKHLTDFKFLLQNIESVVAQMKLGDDLEVIGEHQEKIQKMMKRGIKTAKANGNDVSDPVLAHYHPGRHLYSTSEQFNRSLSTYIKENPDNLIKSKSNPNAYSKKELGPILNVKYLKSVVEPGEAVGIVAGQSIGEPSTQMTLNTFHLAGHSAKNVTLGIPRLREIVMTASNNISTPSMTLHVNEEMTEEAGQKFAKGISKLSLAEILDEASVSERIGRGTSQSRAKIYDINLKFFPPQEYKDTYAIDVADVIATLEKKFVPKLQSLARKALGKKKGEKKLKSAANTAAVPEIGKSVGVIEEARPEGESAPRDEDDDDEDDDGDATNAKQKANRGQAVSYGANDEEDDAVQSQMQREASPEDEDDGDDEGFQGRGSRVGNDEDYEDEEDSGSAGKALSDDRQSKVMSKNADVSRFRCDEGGSWCKLTLEYDASSPKILMLNILESALHTSLIQQISGLDTSTYVAAKNSDPAVVFVSGVNLKAMQNYSDYINPNKISTNDIAAMLEHYGVEACRATIIQELSGVFGGHGIAVDNRHLNLIADFMTRGGGFSPFNRNGLKGSVSPFLKMSFETTIGFLKDAVMDGDWDDLRSPSARIVIGRTGKVGTGAFDVLTRVPVDNDTDHVMSVPPLYITYSSKPPIHEVQASTAVKPTNDRPLLLIVEKMAAARANGGPTRISILGNEDIIVDFDIWRSFVVGDLLENLKSSTYVLITDTNLGGLYVESFETAFRESTSKLEAPPRLLVYEIPPGESSKGRATKAEIEDWMLSHQCTRDTVVIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAFWQPQRIYIDLRFLETLPIREFINGMAEVIKTAAIWDEAEFSTLESNATLIMETIRSPSSDRSSRLTPIRDILKRIVLGSARVKAEVVSADEREGGLRNLLNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARYLGVLKPGAVARLVKCISSYELPTSLDDSLVKKRTAGKKCPVDVLLNKMGVDKKNDGRKKKIVLLSAIGKTHEQKASVVED | ||||||
Region | 290-326 | Disordered | ||||
Sequence: SNEEDEGEGDNLDVAGGLASRSTSGTTTISKQKPATT | ||||||
Compositional bias | 306-326 | Polar residues | ||||
Sequence: GLASRSTSGTTTISKQKPATT | ||||||
Domain | 370-698 | RNA polymerase N-terminal | ||||
Sequence: EFFFLQTLLVPPNKYRPEARTGAGEIAEAQQNALYKQILTAGHMTAQISKELDNPALADLKYRRRDFSDLQESWVKLQDSVNSLIDRDRNPIQGAAGKKNEDGIKQKLEKKEGLFRKNMMGKRVNFAARSVISPDPNIETNEIGVPPVFARKLTYPEPVTSHNFKELQQAVINGADKWPGAAAIENENGQVINLRTKTPDERQSLANQLLASSGIGANGARNKKVHRHLTNGDVVLMNRQPTLHKPSIMGHRARVLPGEKTIRMHYANCNTYNADFDGDEMNMHFPQNEVARAEALQIADTDHQYLAATAGKPLRGLIQDHISVSVWMT | ||||||
Region | 1369-1484 | Disordered | ||||
Sequence: IGKSVGVIEEARPEGESAPRDEDDDDEDDDGDATNAKQKANRGQAVSYGANDEEDDAVQSQMQREASPEDEDDGDDEGFQGRGSRVGNDEDYEDEEDSGSAGKALSDDRQSKVMSK | ||||||
Compositional bias | 1466-1484 | Basic and acidic residues | ||||
Sequence: SGSAGKALSDDRQSKVMSK | ||||||
Region | 2602-2794 | Shikimate kinase | ||||
Sequence: DRSIFIVGMRGAGKTTAGGWASAKLGRPLIDLDQLLEQTIGMTIPELIKARGWEAFRDEELALLKRVMVEKSNGYVFACGGGVVEMPEARDLLINYHKNGGVVLLVHRDTDNVMSYLQIDKTRPAYVEDMMGVYVRRKPWFQACSNFQYHSHTTEKGALSLAKDNFLRFLSLTTGESTHFDEIKAKKHSFFVS | ||||||
Region | 3026-3303 | Shikimate dehydrogenase | ||||
Sequence: PRNFYLFGKPISASRSPALHNSLFKKNGLSDVYDLFETDVAQDVEQLLKSEAFGGASVTIPLKLDVIPLLDNLSEAAKTIGAVNTIVKVRSSTNSTSLYGDNTDWIGIKKTLAAAGAHPGSGLIIGSGGTARAAIFALQSMGFSPVYIVGRSASKVEELVSSFPGLVHIRSAEEAQSLETPPSVAVGTIPSSLPIDAGIREILVSIFHHKEAGDVQRVLLEMAYTASSTTALMNMATDAGWKSIEGVEALIWQGIEQFRIWTGISPEYKDARAAVIGE |
Sequence similarities
Belongs to the EPSP synthase family.
Belongs to the RNA polymerase beta' chain 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 sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,303
- Mass (Da)360,049
- Last updated2014-11-26 v1
- Checksum1456CED0FF4560F4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 306-326 | Polar residues | ||||
Sequence: GLASRSTSGTTTISKQKPATT | ||||||
Compositional bias | 1466-1484 | Basic and acidic residues | ||||
Sequence: SGSAGKALSDDRQSKVMSK |
Keywords
- Technical term