Q6FIV4 · ARO1_CANGA

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 site40-42NAD+ (UniProtKB | ChEBI)
Binding site75-78NAD+ (UniProtKB | ChEBI)
Binding site106-108NAD+ (UniProtKB | ChEBI)
Binding site111NAD+ (UniProtKB | ChEBI)
Binding site1227-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site131-132NAD+ (UniProtKB | ChEBI)
Binding site1387-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1447-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site153NAD+ (UniProtKB | ChEBI)
Binding site1547-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site171-174NAD+ (UniProtKB | ChEBI)
Binding site182NAD+ (UniProtKB | ChEBI)
Binding site186Zn2+ (UniProtKB | ChEBI); catalytic
Binding site186-1897-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2497-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site259Proton acceptor; for 3-dehydroquinate synthase activity
Binding site263-2677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2707-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Active site274Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2867-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site286Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3557-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site844For EPSP synthase activity
Binding site886-893ATP (UniProtKB | ChEBI)
Active site1189Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1218Schiff-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
    • Ordered locus names
      CAGL0M11484g

Organism names

Accessions

  • Primary accession
    Q6FIV4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004067111-1579Pentafunctional AROM polypeptide

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-3833-dehydroquinate synthase
Region396-862EPSP synthase
Region881-1071Shikimate kinase
Region1072-12843-dehydroquinase
Region1297-1579Shikimate 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
    1,579
  • Mass (Da)
    174,232
  • Last updated
    2004-07-19 v1
  • Checksum
    51A302AA2AA7CCF8
MLVKVPILGRETIHVGYGVRSHIVETIVGLKSSTYVVINDSNVGRVPYFQELLSDFEAQLPAGSRLLRYVVKPGEANKTRATKEQIEDYLLSEGCTRDTVIVAVGGGIIGDMIGYVAATFMRGVRVVQVPTSLLAMVDSSIGGKTAVDTPLGKNFIGAFWQPEFVLVDIKWLQSLPKREFINGMAEVIKTACIWNADEFQRLETHADEFLHVVNTPKISEKEGFQLYDTDIESIKEHIFKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYLGILSATQVARLSKILVAYGLPVSKDEKWFRELTLNKKTPLDTLLKKMSIDKKNDGSKKKVVLLETIGKCYGKSAHVVSDEDLRFVLTDETLVYPFNNIPRDQNKTVTPPGSKSISNRALVLAALGKGTCRIKNLLHSDDTKHMLTAVQELKGANISWEDNGETVVLEGQGGSTLVACENDLYLGNAGTASRFLTSVAALVNSTSQKDHVILTGNARMQQRPIGPLVDSLRNNGIKIDYVKNEGCLPLKVHTDSVFKGGRIELAATVSSQYVSSILMCAPYAENPVTLALVGGKPISILYVEMTIKMMEKFGIKVEKSTTEEYTYIIPKGHYVNPAEYVIESDASSATYPLAFAALTGTTVTVPNIGSASLQGDARFATDVLQPMGCSVTQTATSTTVTGPPVGHLKPLKHVDMEPMTDAFLTACVVAAVAHDNDPTSKNTTTIEGIANQRVKECNRIEAMCTQLAKFGVRTNELPDGIQVHGLHSINDLKVPSIGNEAVGVCTYDDHRVAMSFSLLAGMVNSEQPNSSNPTPVRILERHCTGKTWPGWWDVLHTELGAQLDGAEPLELNSMKNAKKSVVIIGMRAAGKTTISRWCAAALGYKLVDLDTLFEERYGHGMIKDFVSQHGWEKFREEEARIFKEVIENYGDAGYVFSSGGGLVESSESRRILKSFSKSGGYVLHLHRDIEETIMFLQKDPTRPAYVEEIREVWNRRESWYKDCSNFSFFAPHCNSEVEFQNLRRAFTKFIRTITGVTTVDIPTRRSAFVCLTFENLTEYTNSLKAITYGCDAVEVRVDHLSNMDEDFVSKQISILRASTDGLPIIFTVRTKKQGGKFPDEDYETLQKLLITALKVGVDYIDLELTLPIGIQYKVLNMKRNTKIIGSHHDFASAYPWDHSEWENRYNQALAMDVDIVKFVGMAKSFEDNLMLERFRDSHTTKPLIAINMGAHGRVSRVLNTILTPVTSEHLSEVAAPGQLTVAEINRIYTEMGGITKKDFFVVGSPIGHSRSPVLHNTGYSVLGLPHHFDKFETTSAEEVKKHLLDNKANLGGLAVTIPLKLDIIKYMDELTESAKVIGAVNTVIPLGNSKFKGDNTDWLGIRNSLVSNGVPESVSGLSGLVVGAGGTSRAAIFALHKLGCQKIFIVNRTTEKLEELVKFFPEEYNIVPIKEAEEAEAVNETIGVAVNCVPADKPLDAKLESLLERLLLKSSHTHFVSTLVEAAYKPSVTPVMKLAKDKYQWRVVPGAQMLVHQGVAQFETWNNCRAPFKAIYDAVTEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR380959
EMBL· GenBank· DDBJ
CAG62820.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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