A0A8H3QZ20 · A0A8H3QZ20_9GLOM

  • Protein
    Pentafunctional AROM polypeptide
  • 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.

TypeIDPosition(s)Description
Binding site124-126NAD+ (UniProtKB | ChEBI)
Binding site129NAD+ (UniProtKB | ChEBI)
Binding site1407-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site149-150NAD+ (UniProtKB | ChEBI)
Binding site1567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site171NAD+ (UniProtKB | ChEBI)
Binding site1727-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site189-192NAD+ (UniProtKB | ChEBI)
Binding site200NAD+ (UniProtKB | ChEBI)
Binding site204Zn2+ (UniProtKB | ChEBI); catalytic
Binding site204-2077-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2887-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Active site292Proton acceptor; for 3-dehydroquinate synthase activity
Binding site3047-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site304Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3737-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site847For EPSP synthase activity
Active site1173Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1201Schiff-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

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
      RCL2_002336100

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HR1
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Glomeromycotina > Glomeromycetes > Glomerales > Glomeraceae > Rhizophagus

Accessions

  • Primary accession
    A0A8H3QZ20

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-4013-dehydroquinate synthase
Domain87-3753-dehydroquinate synthase
Domain423-858Enolpyruvate transferase
Region1283-1559Shikimate dehydrogenase
Domain1288-1368Shikimate dehydrogenase substrate binding N-terminal
Domain1521-1548SDH 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
    1,559
  • Mass (Da)
    172,550
  • Last updated
    2022-01-19 v1
  • Checksum
    7153FA964AB80010
MTLEQPEPDVVKVSILNEESIILGFHLTKFMLRDVISNIPSSNYVIITDENLAPIYLSKIKDDFNKITSEITSAKDKETSEPRLITYTVPSVRQVKSRDTKAEIEDFLLSKACGRDTCILAMGGGIIGDLAGFVAATFMRGIPYVQIPTTLIAMVDSSIGGKTAVDTPHGKNLIGSFWQPKRIYIDLVFLETIPEREFTNGMAEVIKSAIISSESNFINLENGISHIREAVFSNSKRNVPFQGATLATRTPSQSLLLSAIMEAAKFKADIVTHDERDSGLRSLLNFGHTIGHAIEAILSPELLHGECISIGMIKEAEIARHLGHLNQVPVSRLYRVLQDYGLPVSLEEKKIKDLVGKKSCTVDKLMEIMKVDKKIQGDQKRIVMLSSIGNTYEKKATIVADSVIRKILSPAIKILPVTSSNISSIHVTMTTPGSKSISNRALILAALGNGTCRLKGLLYSDDTQVMMVALQKLRGAKFEWENDGETLAVTGGGGNLQVPDDELYLGNAGTASRFLTTVCTLISAETANQKKCTILTGNARMKQRPIGPLVMALQENGSQIRYVENEGSLPIEITPSLNKFKGGKINLSASISSQYVTSILLSAPYASEPVTLSLTGDKVISQPYIDMTIAMMESFGIKIERLEGNIYRIPQGKYTNPSEYVIESDTSSATYPLAVAAITGITCTLPNIGTTSLQGDAAFAVKVLEPMGCTVTQTETSTTVQGPPIGSLRPLPNIDMETMTDAFLTASVLAAVALNNEEKECITRITGIANQRVKECNRISVMVHELNKFGVIASELPDGIQIHGSKIQFLKGPVDGVKCHDDHRIAMSFSVLGCVVPDGTIIREKKCVEKTWPEWWDDFESKLKMNTVGIDSESHHDSIIFIGMRGVGKTTLGREVANALNQEFLDLDQHFEAILSTPIPNFIEEHGWDAFRAKEFEILRSLLNTHASDYIITCGGGVVEYPPSRELLKQYSQNHGDVVHIVRDINDVIRYLNRDASRPSLSEDLLHVWNRRKPFYNECSNIDINTINTFGRMTVENLVEIIRKTRRTFFISLTFPDITPALKIMPTITHGVDAIELRVDLLSENGDIPSVEYICGQLASLRRSSSLPIIFTVRSQSQGGKYPDTQETEYFNLLEQAIKNGCEYVDVEIHKSPTLIENLIKMKGDTKIIASWHDLTGTMKWDGEEVRRKFRAAHNIGDIIKIVGRAKCLSDNFRLREFVEWQQQHIKKPIIAINMDVEGQLSRILNQTFTPVTHPLLPLKAAPGQLSVAEIHKGLHLIGQLPKKKFYLFGNPIVHSMSPTIHNTGFEILGLPHHYDLFESENVEAVKPIIEDIEFGGASVTIPHKISIIPFLDQISVHSKSIGAVNTIIVTENETGRKLIGENTDWLGIFYSIKPLIEINSETVGLVIGGGGTSRAGIYALHQLGLQTIYLYNRTQAKIEELKNQFPKYGIVGLSSLSDEQIKQKPPQIIVSTIPATSNIEIPYELFASGKGGVIVEMAYKPRRTQLLEKGAEKGWIGVEGIQVLIEQGLCQFEEWTGRRAPRNIIEENVYRKYNNIYS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BLAL01000252
EMBL· GenBank· DDBJ
GES96742.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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