S9RGN1 · S9RGN1_SCHOY

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.

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 site83-86NAD+ (UniProtKB | ChEBI)
Binding site114-116NAD+ (UniProtKB | ChEBI)
Binding site119NAD+ (UniProtKB | ChEBI)
Binding site1307-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site139-140NAD+ (UniProtKB | ChEBI)
Binding site1467-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site161NAD+ (UniProtKB | ChEBI)
Binding site1627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site190NAD+ (UniProtKB | ChEBI)
Binding site194Zn2+ (UniProtKB | ChEBI); catalytic
Binding site194-1977-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site260Proton acceptor; for 3-dehydroquinate synthase activity
Binding site264-2687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2717-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Active site275Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2877-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site825For EPSP synthase activity
Binding site869-876ATP (UniProtKB | ChEBI)
Active site1181Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1210Schiff-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

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
      SOCG_00964

Organism names

Accessions

  • Primary accession
    S9RGN1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3843-dehydroquinate synthase
Domain77-3583-dehydroquinate synthase
Domain404-837Enolpyruvate transferase
Region1292-1572Shikimate dehydrogenase
Domain1297-1377Shikimate dehydrogenase substrate binding N-terminal
Domain1541-1570SDH 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,572
  • Mass (Da)
    173,251
  • Last updated
    2013-10-16 v1
  • Checksum
    77021C16A54C1162
MSSESDLITVPILGKETVKVGFGLDEYVATEILKEFQSSTYVVITDSNIAPHHLEPFERIFRDTIKKNGAQSRFLSYIIPPGESSKCRATKAEIEDWMLSQSCTRDTLLIAMGGGVIGDLVGYIAATFMRGIRFVQMPTTLLAMVDSSIGGKTGIDAPLGKNLIGAFWQPLRVYVDLLVLHTLPPRQIINGLAEIIKTAAMWNEKDFQLLENNSALLIEEIHKPAVSGEYKFSKIKDLLQKIILSSIRTKCEVVTLDEREGGLRNLLNFGHSIGHAYEAILYPQILHGECVAIGMMKEVELARHLGILKPNAVGRLAKCLVSYNLPVSVNDPKIKKYAGFKTCPVENLILTMAVDKKNQGTKKRVVILKAIGETYEKHATVVSDDDIRFVLSSDVKVDNFTENSLDVVITPPGSKSISNRALVLAALSQGTCRLTNMLHSDDTQFMMSALESLGAAKFSWEDNGETLVVEGSGGKMSAPKDALYLGNAGTAARFLTGVSALVPTQDKEHGVVLTGNHRMKVRPIGPLVDALRNNGCTVEYLEKEGSLPLSTSSSTGLKGGVIELAATVSSQYVSSILMCAPYASEPVTLKLVGGKPISQLYIDMTIAMMASFGIIVEKSSSEENTYHIPRAKYQSPSKYEIESDASSATYPLAIAAITGTKCTVPNIGSASLQGDSRFARDVLKPMGCLVEQTANSTTVQGPPKGQLKPLESIDMETMTDAFLTASVVAAVSSNAEGDPITRITGIANQRVKECNRIAAMVHELAKFGVRAGELEDGIYIFGQDYKTLKSPTDGVYTYDDHRVAMAFSLLALLTPSPTVVIDKACVEKTWPYWWDVLKQSFKVSLYGSTVEQVEQQNPLSKNASIILIGMRGAGKTTIGKIISKQLNMKFIDLDEWLEDRLAMPITQVIFKLGWDAFRLEEHKLLREFIQERPYGFVAASGGGVIEMNDSRKLLENYVKSGGIVLHVHRNIDHIVSYLSKDSSRPAYKDQENIRDVYARRHEWYRQCRSHYFISPVLDERVVEEKIEYSMSRFLEVITGKSQSLQKLKEKKRSAFLTLNFPDVQQALPLLNDVTLGCDAVEIRVDHLKDPKGKNGVPTLDFVAEQVALLRCHTHLPIIFTVRTKKQGGLFPDDKEADALELILSAIRYGIDYVDVELGWSIESITKIFEHKRNTKLLMSWHDLSGTWSWASPQEWMQMIDLASSFADIIKLVGTAKDIKDNLELENFRKSVTSTMKIPLIAINMGGKGQLSRVFNKFLTPVTHPDLPSKAAPGQLSVKQLNEALALIGEIVPKNFYVFGKPISHSRSPVLHNTAYKLLGLPHSYEAYETDTVEEVEGILRSPDFGGANVTIPYKLPIMQYMDDLSHEARFFGAVNTVIPSMKEGKLHLRGDNTDWRGIYDTFTAALDGMSLAESSALVIGAGGTSRAAIYTLHRLGVSQIYLVNRTLANSYAVQNVFPPEYNIKVLDADKVTSEDLNGVSIASAISTVPADKALPESVDRLVKALIATGDRQSIFLDMAYKPLHTPLMGVASEHGWRCSSGLEVLVRQGLASFQMWTGMNPPFSPVYKKVIE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KE503207
EMBL· GenBank· DDBJ
EPX73209.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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