A0A8H7PW36 · A0A8H7PW36_MORIS

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 site51-53NAD+ (UniProtKB | ChEBI)
Binding site93-96NAD+ (UniProtKB | ChEBI)
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 site2667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site276Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2877-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Active site291Proton acceptor; for 3-dehydroquinate synthase activity
Binding site3037-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site303Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3727-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site846For EPSP synthase activity
Active site1226Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1254Schiff-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
      INT43_008404

Organism names

Accessions

  • Primary accession
    A0A8H7PW36

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-4003-dehydroquinate synthase
Domain89-3743-dehydroquinate synthase
Domain428-858Enolpyruvate transferase
Region1334-1609Shikimate dehydrogenase
Domain1339-1419Shikimate dehydrogenase substrate binding N-terminal
Domain1462-1528Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain1574-1600SDH C-terminal

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 dehydroquinate synthase 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
    1,609
  • Mass (Da)
    176,542
  • Last updated
    2022-01-19 v1
  • Checksum
    D9F7766A5C6588F7
MSPAPSEIEPLVTKVSILGSESIILGFHLTEYILKDILTNIPASNYVIITDTNLAPIYLPNLVERFNHHSAEISAAKGQKASRLFTRALPPGELTKSRSTKAEIEDWLLSNAVTRDTCFIAMGGGVIGDLIGFVAATFMRGVPVVQMPTTLLSMVDSAIGGKTAIDTPQGKNLVGAFWQPKRIYIDLAFLQTLPEREFSNGMAEVIKTAAIWCEEDFVKLENGVEKIREAVLGKSNRVPFQGATLETRTEGQTLLMDVVSASARVKAYVVTEDEREGGLRGLLNFGHSIGHGIEALVSPMMLHGECVSVGMIKEAELSRNLGHLNQVAVGRLTRCLASYGLPVSMDEKRVRDLIGTAYCHVDDIMEVMKVDKKNQGDKKRIVLLAAIGKTLEPRASVVADVDIHKVISPEQLVLPVTESPKGPKKEVTLSTPGSKSISNRVLLIASLGAGTTRIKGLLHSDDTQFMRAALKDLGAADFDWEDNGDTLVVKGGGGKLRVPDKELYVGNAGTASRFLTTVLALIQERTGDQPEAAILTGNARMKQRPIAPLLTALIANGAKIKSTEKEGFLPIAVKPNGGFKGGRIELAASISSQYVSSILLCAPYAQEPVELVLTGGQVISQPYIDMTIAMMESFGVNVDRLPNNTYRIAQAVYQNPDVYMVESDASSATYPLAIAAITGTTCTVSNIGTASLQGDATFAVNILRPMGCTVMQTESSTTVTGPPVGQLRPIPTVDMETMTDAFLTASVLAAATQAPEGTENITRITGIANQRVKECNRIAAMVHELTKFGVTCSELPDGIQIHGKPIKDLKAPAEGVHCYDDHRVAMSFAVLSTVVPNGTIIQEKKCVEKTWPQWWDDLENKLGVQLRGVDQGQKLEAISSQLGTLSNRRLKPTDHAKSIFIIGMRGVGKTTLGQYSAQVLGFNFVDVDQYLEKTRKTTIPEIVNTYGWPRYREEETACLREILAPASPYARNYIISCGGGIVETESCRDLLKQYCKDGGKVLHIVRDMDQVVKFLNQDKTRPMFGEDMLNVWRRRKPWYHDICNFEFIAYAKSMVQDKWVDPVEWQAIQKELRRFLMFITGQDTNQVPDCVSASGSPSTFVSLTLRDLREAEDKLVEICEGADVVELRVDLLRAPHQASAIPSSDFVGEQLAILRRHVDTPVLFTVRSKGQAGAFPDDAEAEMFDLLRWGQKWGCEYIDMEIIWSQAVTDDLVAHCGESKLVASWHDISNLTPWGSRALNDRYETADKYGDIIKLIGTATSLADNVTLEQFRAKKQSSKPLIAMNMGTVGQMSRVLNNFLTPITHSSLPTKAAPGQLTLKEINQARHLLGLIPAKKFYLFGTPIAHSMSPTLHNTGFHTIGLPYQYELLECSSVAYAEHVLYEENFGGASVTIPHKISIMKYLDEVTDNVKAIGAVNTVYPVYVKDENGEMKRQLHGENTDYLGIKGCVQKLLLNPDNVAEGLVIGSGGTSRAALYALHTLGVKKIHLWNRTISKAHELRDHFAQYFEVNVIESLEADIHPQVIISTIPADNGVKVPDALFGGIRGICCDMAYKPRRTELLKQAEQHGWSTVEGIEVLIEQGYGQFKIWTNKVAPKQAMATEVNKKYDL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPQZ010000005
EMBL· GenBank· DDBJ
KAG2180825.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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