A0AA43TTR4 · A0AA43TTR4_9LECA

  • Protein
    Pentafunctional AROM polypeptide
  • Gene
    ARO1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

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.

Type
IDPosition(s)Description
Binding site47-49NAD+ (UniProtKB | ChEBI)
Binding site84-87NAD+ (UniProtKB | ChEBI)
Binding site119-121NAD+ (UniProtKB | ChEBI)
Binding site124NAD+ (UniProtKB | ChEBI)
Binding site1357-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site144-145NAD+ (UniProtKB | ChEBI)
Binding site1517-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1577-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site166NAD+ (UniProtKB | ChEBI)
Binding site1677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site184-187NAD+ (UniProtKB | ChEBI)
Binding site195NAD+ (UniProtKB | ChEBI)
Binding site199Zn2+ (UniProtKB | ChEBI); catalytic
Binding site199-2027-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2557-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site265Proton acceptor; for 3-dehydroquinate synthase activity
Binding site269-2737-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2767-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site276Zn2+ (UniProtKB | ChEBI); catalytic
Active site280Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2927-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site292Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3617-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site854For EPSP synthase activity
Binding site899-906ATP (UniProtKB | ChEBI)
Active site1211Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1239Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-dehydroquinate dehydratase activity
Molecular Function3-dehydroquinate synthase activity
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
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 Processphosphorylation

Keywords

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

    • Name
      ARO1
    • ORF names
      OHK93_006679

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LIQ254RAFAR
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Lecanoromycetes > OSLEUM clade > Lecanoromycetidae > Lecanorales > Lecanorineae > Ramalinaceae > Ramalina

Accessions

  • Primary accession
    A0AA43TTR4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3893-dehydroquinate synthase
Domain78-3633-dehydroquinate synthase
Domain414-866Enolpyruvate transferase
Region1321-1607Shikimate dehydrogenase
Domain1326-1406Shikimate dehydrogenase substrate binding N-terminal
Domain1575-1595SDH C-terminal

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.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,607
  • Mass (Da)
    174,229
  • Last updated
    2024-01-24 v1
  • Checksum
    5692FEE43BBB0E46
MGSTPRPTKVSILGNESIFVDYDLWGSFIASDLLQNVTSSTYVLITDTNLHDVYVPGFQKAFEKVAASLRIESRLLTYQIPPGETSKSRSMKAEVEDWMLSEERNPPCDTKTVMIALGGGVIGDSIGFVAATFKRGIRFVQVPTSLLAMVDSSIGGKTAIDTPAGKNLVGAFWQPSRIYIDLQFLNSLPTREFINGMAEVIKTAAIWDVKAFEGLESNASQLMEAIQKQPTMGPERLSTVRSILKEAVLGSVRVKAHVVSADEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAVGMHLEAVLARFLGVLDEGAVTRLVKCLSAYKLPTSLKDKTLKERSNYKHCSVDRIFTIMGVDKKNDGKKKRIVLLSGIGQTHERQASVVADKDVRVVLSSGIQVKPGVREGQKVSCTPPGSKSISNRALVLAALGNGTCRIRNLLHSDDTEVMMTALTQLQAASFSWEEDGRVLVVNGHGGNLHASKDELYVGNAGTASRFLTSVATLAKPTRAAHSILTGNARMKQRPIGPLVDALRGNGAEVSFMKQVNSGYIEKSGQELDDKGGQCLPLQISASDGMEGGDIRLKAQVSSQFVSSILMCAPRAKKPVTLRMDVSEGPPISQPYIDMTTAMMASFGVHVTRSKTEQHTYHIPKAEYQNPAEYIIESDASSATYPLAIAALTGTTCTIPNIGSNSLQGDATFATEVLALMGCTVEQTATSTTVTGPPKGSLKPIEEVDMTNMTDAFLTASVLAATARSSSGKSTTRITGIANQQKKECERISVMKEQLAQFGVTCRLWPIQDTTPNGIEIDGIEIDRLQTPSHGVNCYDDHRVAMSFSVLAAVTPGGALIRERECVGKTWPGWWDILQRSFGVHLQGVDLEGPTAPQRNENHSKSIFLIGMRGAGKTTFGRWAASVLERPFFDLDSELENLKRLTIPEIIKNDGWEGFREQELALLKKSIQAQSHGHVFACGGGIVETAEGRQLLVDYRDSGGPVILVQREIRDVMAFLQIDKSRPAYVDDMMSVWERRKEWYNQCSNFQYFGERAPNESRLEKPPNVSRFLATITGQNRSLKKILSKERSFFVSLTVPDLATASHTLPQVAVGSDAIELRVDLLEDPESPGQLPGPDFVTRQLATLQKSTCLPIIYTVRTKDQGGRFPISTGEDRARLVSLLELALRSGVEILDVEMSLPDSLLNRISSIKAHTSIIASHHDPHGALSWEGGSWDDIYKRAIQYGDVVKLVGVARSQEDNSSLLQLRKKALAIKGVPLIAINMGTEGQLSRIQNTILTPVSHPALPFKAAPGQLSAAEIRLALSLHGVIKSRKFVLVGEPISQSRSPALHNALFKQAGLPHRYDLLPTSDASALRGTLHSNDFGGMSVTIPLKLDIMPLLDEVAEDARVIGAVNTVVVDESRISDKHPGFHLTGRNTDWQGMRLVLENVGAQSAGGQSGLVIGGGGTARAAIYTLHAMGYSPLYLLGRSAQKIDELADSFPKEYNISPMTKFDQFHKDQLPLTAISTIPGDKPIDSGMQTVLDSLFGATGGSGSRSRVLLEMAYKPAVTPLMDKAQKAGWSVIPGLEVLAGQGVYQFEAWTGIKPVFSDARAIVLGK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPUFD010000005
EMBL· GenBank· DDBJ
MDI1487409.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp