A0A8H7SY11 · A0A8H7SY11_9FUNG

  • 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 site46-48NAD+ (UniProtKB | ChEBI)
Binding site88-91NAD+ (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 site2617-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site271Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2827-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site282Zn2+ (UniProtKB | ChEBI); catalytic
Active site286Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2987-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site298Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site842For EPSP synthase activity
Active site1223Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1251Schiff-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
      INT48_000808

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WA0000018081
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Mucoraceae > Thamnidium

Accessions

  • Primary accession
    A0A8H7SY11

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-3953-dehydroquinate synthase
Domain83-3693-dehydroquinate synthase
Domain423-854Enolpyruvate transferase
Region1331-2149Shikimate dehydrogenase
Domain1336-1417Shikimate dehydrogenase substrate binding N-terminal
Domain1460-1525Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain1572-1602SDH C-terminal
Compositional bias1721-1742Polar residues
Region1721-1769Disordered
Compositional bias1755-1769Polar residues
Region1824-1853Disordered
Region1911-1942Disordered
Region2049-2088Disordered
Compositional bias2050-2072Polar residues
Region2101-2123Disordered

Sequence similarities

Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 2nd section; belongs to the type-I 3-dehydroquinase 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 shikimate kinase 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
    2,149
  • Mass (Da)
    238,006
  • Last updated
    2022-01-19 v1
  • Checksum
    FE4ACC5331CA3955
MTNKRDVAKISILGSESIIAGFHLSEYLIRDVLNNIPASNYVLVTDSNLAPIYLDTYTETFKKVSSEISTAKGEKEPRFFTRVLPPGETSKSRKVKADIEDWLLSNAVTRDTCFLAMGGGVIGDLIGYVAATFMRGAPFVQIPTTLLAMVDSSIGGKTAIDVPAGKNLIGAFWQPKRIFIDINFLKTLPEREFSNGMAELIKTAAISDENDFCKLENGVEAIRHAVLGNDSKVPDQGATLETRTDSQAMLMDVVLASARFKAFVVTNDEREGGLRGLLNFGHSIGHGIEAIVSPLMLHGECVSIGCMKEAELARNLGHLNQVAVGRLARCFQSYGLPICMEEKKVKDRIGSLYCHVDDIMEIMKVDKKNQGDKKRIVMLSAIGKTLEPRASVIADADIYKVLCPQQLVLPVTESSTGPKKKVKLTTPGSKSISNRALLIAALGKGTVRVKNLLHSDDTQFMLAALKSLDAADFEWEDNGETLVVHGGGGRLSVPDKEIYVGNAGTASRFLTSVLTMIPTAENSKNATAVLTGNARMKMRPIAPLLDALKSNGAEIVSLEKEGFLPVAVTPNGGLKGGRIELSASISSQYVSSILLCAPYAINEVELALVGGQVISQPYIDMTIAMMESFGAAVERLPENTYRIKQTTYKNPDHYVVESDASSATYPLAIAAITGTTCTVTSIGSSSLQGDATFAINVLRPMGCTVIQTETSTTVTGPPIGQLRPLPSIDMETMTDAFMTATVLAAVTSSADPKGENITRITGIANQRVKECDRIAAMVHELTKFGVQASELPDGIQIHGKPIKDLKAPKEGVHTYDDHRIAMSFSVFATVVPHGTIIMEKKCVEKTWPTWWDDLEGKLGVRLNGVDLGDRLSQAGKSLGRTTFTKVSKNMDVGKSMVIVGMRGVGKTTLGQYAAEVLGFKFIDVDLYFEETLKTTVFEFINTWGWDQFRIKESECLKQLLSKDSIYGCEYVISCGGGIIETAESRDILKDHTKRGGKVLHLVRDLDQVVRYLNRDKTRPMFGEDMMNVWRRRRSWYKEVCNFEFVAYANSIVDDGYVSPTEWLAIKRDLQRFLYFICGRDTNQVNTTAGRIGVPTTFVSLTSKDLNSVVDKLEEICEGADAVELRVDLLQKPDEKHEMTYIEYVGEQLALLRRVVPIPVIFTVRSKGQAGAFADNDEEGMFELLTWGQRWGCEYIDVEICWTPATIEKLVANKGESLIISSWHDVQNMTPWDDKAIQLKYETAEKYGDIIKLVGNAQTFQDNMTLETFRASKQDGKDLIAINMGAAGQLSRVINECLTPITHTALPHKAAPGQLSLAEINKARHLIGLLPAQSFWLIGTPIQHSMSPTLHNTGFQVLGLPHQYSLLECHMVEYAEDAIFKDSSFGGASVTIPHKVAIMKYLDEVTENAKAIGAVNTIFVRDTVVNGDKKRQFIGENTDYIGMKRRIQSLMLDPTNPPEQGLVIGAGGTARAALYTLQKIGIQKIYLWNRTISKARDLQKAFEGIIDVEVIDSLDAKIEPGVIISTVPADSGIELPEALYGGIKGIICDMAYKPRRTKLLLQAERKGWSCVEGIEILISQGIAQFELWTGKRAPVTKIEEEVLKKDHEDTYLDTKVLADLANQFNSPLLAELSKLKPNDYSIGLADPILRTFAQFKRAPKEEYIWESVQLPLENMEHVIDREGERQIKTEPTSPPSLHQMLPESRNAMALDKVLLNSNELRRQSILESPNKRQRIGTTSSPSHVSEIDRERRPHSLSAVTTASNQPISRQIRKIQSYPAAETEEQQPASPNKRLSTKHKNSLNLTIFAPSYHEQLAGVRSAPINSNFNRPIPNQPTQQHSRSNYANHGPMTASHNIAPASATIARPPFAHQPSPRRHEFAIPPIVPSQQQPPHSAHPTSRENVMYQQQYVPSPSLYGSHHHTKPQPSSYQRNHESQQKQPQQLAVNAASIPLPPKTPTTNSFAALQRQQYLQPFEHLFDTIETTRTLKSTLDDQIRRSSSLMQTLQASATTIEGLVRNQVKEAQWETMSQMEQTVDALVRRIEIVENRFDRNDSNGSNSAIRRQVQKQPDLRTDIGSLPSPLPSATREERAVAEDLVAFSERKRDGNELEELQTPPTIVRSQNDIGPQEYHNMLDTLRERLDRLERQIES

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1721-1742Polar residues
Compositional bias1755-1769Polar residues
Compositional bias2050-2072Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPRE010000016
EMBL· GenBank· DDBJ
KAG2236508.1
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