A0A093ZYW5 · A0A093ZYW5_9PEZI

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

TypeIDPosition(s)Description
Binding site1789-1791NAD+ (UniProtKB | ChEBI)
Binding site1826-1829NAD+ (UniProtKB | ChEBI)
Binding site1857-1859NAD+ (UniProtKB | ChEBI)
Binding site1862NAD+ (UniProtKB | ChEBI)
Binding site18737-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1882-1883NAD+ (UniProtKB | ChEBI)
Binding site18897-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site18957-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1904NAD+ (UniProtKB | ChEBI)
Binding site19057-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1922-1925NAD+ (UniProtKB | ChEBI)
Binding site1933NAD+ (UniProtKB | ChEBI)
Binding site1937Zn2+ (UniProtKB | ChEBI); catalytic
Binding site1937-19407-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site19937-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site2003Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2007-20117-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site20147-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2014Zn2+ (UniProtKB | ChEBI); catalytic
Active site2018Proton acceptor; for 3-dehydroquinate synthase activity
Binding site20307-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2030Zn2+ (UniProtKB | ChEBI); catalytic
Binding site20997-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site2562For EPSP synthase activity
Binding site2609-2616ATP (UniProtKB | ChEBI)
Active site2918Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site2946Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentRNA polymerase I complex
Molecular Function3-dehydroquinate dehydratase activity
Molecular Function3-dehydroquinate synthase activity
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA-directed 5'-3' RNA polymerase activity
Molecular Functionmetal ion binding
Molecular Functionshikimate 3-dehydrogenase (NADP+) activity
Molecular Functionshikimate kinase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process
Biological ProcessDNA-templated transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pentafunctional AROM polypeptide

Including 5 domains:

  • Recommended name
    3-dehydroquinate synthase
  • EC number
  • Short names
    DHQS
  • Recommended name
    3-phosphoshikimate 1-carboxyvinyltransferase
  • EC number
  • Alternative names
    • 5-enolpyruvylshikimate-3-phosphate synthase
      (EPSP synthase
      ; EPSPS
      )
  • Recommended name
    Shikimate kinase
  • EC number
  • Short names
    SK
  • Recommended name
    3-dehydroquinate dehydratase
  • EC number
  • Short names
    3-dehydroquinase
  • Recommended name
    Shikimate dehydrogenase
  • EC number

Gene names

    • ORF names
      V490_06200

Organism names

  • Taxonomic identifier
  • Strain
    • VKM F-3557
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Pseudeurotiaceae > Pseudogymnoascus

Accessions

  • Primary accession
    A0A093ZYW5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-21273-dehydroquinate synthase
Region290-326Disordered
Compositional bias306-326Polar residues
Domain370-698RNA polymerase N-terminal
Region1369-1484Disordered
Compositional bias1466-1484Basic and acidic residues
Region2602-2794Shikimate kinase
Region3026-3303Shikimate dehydrogenase

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 status
    Complete
  • Length
    3,303
  • Mass (Da)
    360,049
  • Last updated
    2014-11-26 v1
  • Checksum
    1456CED0FF4560F4
MNISQPVSSAIGSVDFAFLSPDEIKRLSVKAIQNPTTFDTLLNPVPGGLYDPALGAWGDIQCTTCHLGALSCPGHVGHITLPVPVYHPTFMDQLLRLLRAKCAYCHHFKMSRKDVNLYHCKLRLIQAGLLSAAEEVENIDLVAKKAAAVGQEDDSSSDSGDDNGVESTIKQRLSFVKKAIRDAKATPWDWKLEKNESVADARREVIKSFLKSITISKTCANCKAISNGFRKDRFVKIFEKPMTAKEEAKNAQQNLKAVNAMRVVSKDAGHAKNSNGYASDEGIADIDLSSNEEDEGEGDNLDVAGGLASRSTSGTTTISKQKPATTGERYVNPMEVRASLTLLFEKEQEILSLVYASRSSSKKAAVITAEFFFLQTLLVPPNKYRPEARTGAGEIAEAQQNALYKQILTAGHMTAQISKELDNPALADLKYRRRDFSDLQESWVKLQDSVNSLIDRDRNPIQGAAGKKNEDGIKQKLEKKEGLFRKNMMGKRVNFAARSVISPDPNIETNEIGVPPVFARKLTYPEPVTSHNFKELQQAVINGADKWPGAAAIENENGQVINLRTKTPDERQSLANQLLASSGIGANGARNKKVHRHLTNGDVVLMNRQPTLHKPSIMGHRARVLPGEKTIRMHYANCNTYNADFDGDEMNMHFPQNEVARAEALQIADTDHQYLAATAGKPLRGLIQDHISVSVWMTNRDTFFDRATYQQLVYNCLRPESGHIIGERIETVPPAIIKPFPQWTGKQIITTILKNITPLGYTPLNLISKSQVPFERWGPKSEEGQVFFQDGELITGILDKSQLGPSGGGLIHSLHEAHGPTVAGKMLSILGRLLTKFLHMRAFSCGMEDLLLTSEGEKTRKEKLKDVHLIGLEVATKYVTLEDRKPTANDPELRNRLEDVLRDDTKQEGLDVMMNGSSNKLSSEITKACLPLGLVKQFPKNQMQNMTVSGAKGSAVNANLISCNLGQQVLEGRRVPVMVSGKTLPCFKPFETNVRAGGYIANRFLTGIRPQEYYFHAMAGREGLIDTAVKTSRSGYLQRCLIKGMEGLKVEYDTSVRDSDGSMVQFLYGEDGLDVTKTKHLTDFKFLLQNIESVVAQMKLGDDLEVIGEHQEKIQKMMKRGIKTAKANGNDVSDPVLAHYHPGRHLYSTSEQFNRSLSTYIKENPDNLIKSKSNPNAYSKKELGPILNVKYLKSVVEPGEAVGIVAGQSIGEPSTQMTLNTFHLAGHSAKNVTLGIPRLREIVMTASNNISTPSMTLHVNEEMTEEAGQKFAKGISKLSLAEILDEASVSERIGRGTSQSRAKIYDINLKFFPPQEYKDTYAIDVADVIATLEKKFVPKLQSLARKALGKKKGEKKLKSAANTAAVPEIGKSVGVIEEARPEGESAPRDEDDDDEDDDGDATNAKQKANRGQAVSYGANDEEDDAVQSQMQREASPEDEDDGDDEGFQGRGSRVGNDEDYEDEEDSGSAGKALSDDRQSKVMSKNADVSRFRCDEGGSWCKLTLEYDASSPKILMLNILESALHTSLIQQISGLDTSTYVAAKNSDPAVVFVSGVNLKAMQNYSDYINPNKISTNDIAAMLEHYGVEACRATIIQELSGVFGGHGIAVDNRHLNLIADFMTRGGGFSPFNRNGLKGSVSPFLKMSFETTIGFLKDAVMDGDWDDLRSPSARIVIGRTGKVGTGAFDVLTRVPVDNDTDHVMSVPPLYITYSSKPPIHEVQASTAVKPTNDRPLLLIVEKMAAARANGGPTRISILGNEDIIVDFDIWRSFVVGDLLENLKSSTYVLITDTNLGGLYVESFETAFRESTSKLEAPPRLLVYEIPPGESSKGRATKAEIEDWMLSHQCTRDTVVIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAFWQPQRIYIDLRFLETLPIREFINGMAEVIKTAAIWDEAEFSTLESNATLIMETIRSPSSDRSSRLTPIRDILKRIVLGSARVKAEVVSADEREGGLRNLLNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARYLGVLKPGAVARLVKCISSYELPTSLDDSLVKKRTAGKKCPVDVLLNKMGVDKKNDGRKKKIVLLSAIGKTHEQKASVVEDEAIRIILSKSIIVTPGIPKALSVEVTPPGSKSVSNRALVMAALGLGPCRIRNLLHSDDTEVMLTAIGKLGGATYSWEDEGEVLLVNGKGGDLHASPSELYLGNAGTASRFLTTVAALCKPSTVGSTVLTGNSRMKVRPIGPLVESLRGNGVEIKYLEKEKSLPIDVAASGGFVGGTIELAATVSSQYVSSLLMCAPYAKNPVTLRLVGGKPISQPYIDMTTAMMAAFGIKVTRSETEEHTYHIPQGVYQNPTDYTIESDASSATYPLAIAAISGTTCTIPNIGSSSLQGDSRFAIDVLRPMGCTVEQTATSTTVTGPAPGGLKGLEDIDMEPMTDAFLTASVLAAVSKGTTKIRGIANQRVKECNRIKAMKDELKKFGVECRETEDGIEVDGKPMGTLSNPEEGVFCYDDHRVAMSFSVLATAVPEPTLILERECTAKTWPGWWDVMSLFFQVQLSGKEVEEDRLHQETKTLSSDRSIFIVGMRGAGKTTAGGWASAKLGRPLIDLDQLLEQTIGMTIPELIKARGWEAFRDEELALLKRVMVEKSNGYVFACGGGVVEMPEARDLLINYHKNGGVVLLVHRDTDNVMSYLQIDKTRPAYVEDMMGVYVRRKPWFQACSNFQYHSHTTEKGALSLAKDNFLRFLSLTTGESTHFDEIKAKKHSFFVSLTMPDASKMLDVLPEVVVGSDAVELRVDLLVDPASEDGIPTLDFVYEQVSILRSAISLPLIFTVRTVGQGGRFPNDAHSQALALYQAAVRMAIEYIDVEIQFPTELLQTVCSNKGLSRIIASHHDPAGTLSWKNAGWAQYYNRALEYGDIVKLVGVAKSMEDNFALAKFKNDMTHETPLIAINMGAKGKLSRVLNGFMTPVSHPALPFKAAPGQLSATEIRSGLSLLGELEPRNFYLFGKPISASRSPALHNSLFKKNGLSDVYDLFETDVAQDVEQLLKSEAFGGASVTIPLKLDVIPLLDNLSEAAKTIGAVNTIVKVRSSTNSTSLYGDNTDWIGIKKTLAAAGAHPGSGLIIGSGGTARAAIFALQSMGFSPVYIVGRSASKVEELVSSFPGLVHIRSAEEAQSLETPPSVAVGTIPSSLPIDAGIREILVSIFHHKEAGDVQRVLLEMAYTASSTTALMNMATDAGWKSIEGVEALIWQGIEQFRIWTGISPEYKDARAAVIGE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias306-326Polar residues
Compositional bias1466-1484Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPJS01001817
EMBL· GenBank· DDBJ
KFX90906.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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