C8Z543 · ARO1_YEAS8

Function

function

The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.

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 site43-45NAD+ (UniProtKB | ChEBI)
Binding site78-81NAD+ (UniProtKB | ChEBI)
Binding site109-111NAD+ (UniProtKB | ChEBI)
Binding site114NAD+ (UniProtKB | ChEBI)
Binding site1257-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site134-135NAD+ (UniProtKB | ChEBI)
Binding site1417-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1477-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site156NAD+ (UniProtKB | ChEBI)
Binding site1577-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site174-177NAD+ (UniProtKB | ChEBI)
Binding site185NAD+ (UniProtKB | ChEBI)
Binding site189Zn2+ (UniProtKB | ChEBI); catalytic
Binding site189-1927-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2587-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site268Proton acceptor; for 3-dehydroquinate synthase activity
Binding site272-2767-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2797-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site279Zn2+ (UniProtKB | ChEBI); catalytic
Active site283Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2957-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site295Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3647-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site853For EPSP synthase activity
Binding site895-902ATP (UniProtKB | ChEBI)
Active site1198Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1227Schiff-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

Keywords

Enzyme and pathway databases

    • UPA00053UER00085
    • UPA00053UER00086
    • UPA00053UER00087
    • UPA00053UER00088
    • UPA00053UER00089

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
      EC1118_1D0_3829g

Organism names

Accessions

  • Primary accession
    C8Z543

Proteomes

    • Identifier
    • Component
      Chromosome IV, Scaffold EC1118_1D0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004067511-1588Pentafunctional AROM polypeptide

Proteomic databases

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-3923-dehydroquinate synthase
Region405-871EPSP synthase
Region890-1080Shikimate kinase
Region1081-12933-dehydroquinase
Region1306-1588Shikimate dehydrogenase

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,588
  • Mass (Da)
    174,739
  • Last updated
    2009-11-03 v1
  • Checksum
    B7CCED2C799B1080
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKHIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN393063
EMBL· GenBank· DDBJ
CAY78632.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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