A0A0L0UX68 · A0A0L0UX68_9BASI

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 site47-49NAD+ (UniProtKB | ChEBI)
Binding site81-84NAD+ (UniProtKB | ChEBI)
Binding site112-114NAD+ (UniProtKB | ChEBI)
Binding site117NAD+ (UniProtKB | ChEBI)
Binding site1287-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site137-138NAD+ (UniProtKB | ChEBI)
Binding site1447-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site159NAD+ (UniProtKB | ChEBI)
Binding site1607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site177-180NAD+ (UniProtKB | ChEBI)
Binding site188NAD+ (UniProtKB | ChEBI)
Binding site192Zn2+ (UniProtKB | ChEBI); catalytic
Binding site2577-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site267Proton acceptor; for 3-dehydroquinate synthase activity
Binding site271-2757-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2787-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site278Zn2+ (UniProtKB | ChEBI); catalytic
Active site282Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2947-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site294Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3637-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site849For EPSP synthase activity
Binding site901-908ATP (UniProtKB | ChEBI)
Active site1228Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1256Schiff-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

    • ORF names
      PSTG_14946

Organism names

Accessions

  • Primary accession
    A0A0L0UX68

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3913-dehydroquinate synthase
Domain75-3653-dehydroquinate synthase
Domain417-861Enolpyruvate transferase
Region1342-1647Shikimate dehydrogenase
Domain1347-1430Shikimate dehydrogenase substrate binding N-terminal
Domain1474-1523Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain1611-1640SDH 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,647
  • Mass (Da)
    178,567
  • Last updated
    2015-11-11 v1
  • Checksum
    FC21B23A84B1AB77
MAHLICDVQSVSILGKPSIRLGYHLAPYIAHTVLTELRSSTYILITDSNVSPRHVPALKAAFEDQLPASSRLLTYILPPGEQSKCREMKAVLEDWLLDHRCTRDTVVLALGGGVIGDLIGFVSATFMRGIRFCQIPTTLLAMVDSSVGGKTAIDTPLGKNLVGAFWQPSFIFIDASYLETLPEREFVNGMAEMIKTAAIWDESQFEKLESNVESIRSAVLSPPPRDPMNPFPGRDVGSRSQAQNLLLEVIADSVGVKSEVVTKDEKETGLRNLVNFGHTIGHAIEAVLTPAILHGECVSIGMILEAEVARARGCLSSSAVARLSKCLKAHGLPVSLNDPKIQSSPNASKLSLDRLLDLMSVDKKNEGKVKKIVLLSRIGKTFEERATGVEDSLIRRVLAPAVRVYPGPPPANIKEVTLRTPGSKSISNRALILAALGNGTCRLKNLLHSDDTQVMIDALESMKGASFSWEDNGATLVVSGGGGQLSSPVNGKHVYLGNAGTAARFLTTVCSLVKSQDSSHSSTVITGNARMQERPIGPLVNALRTNGVQIEYLRNEGCLPLRISTEDGFPGGMIELAASVSSQYVSSVLLSAPFAQAPVTLSLVGGAVISQPYIDITISMMSTFGIHVERVKDSATGLPSNTYRIPNGTYTNPAVYEIESDASSATYPLAMAALNGLSLTLETIGSASLQGDAQFAKKVLEPMGCQVIQTERETKVIGPSNVSELRQIGDIDMEEMTDAFLTACVLLGVAVQPSTKGQRTSTRIVGIANQRVKECNRIAAMVAELGKMGIRAEELDDGIEVFGTPVDDLAKCGDQVRIHCYDDHRIAMAFSVLGTVPGGKGLILNEKRCVEKTWPSWWDDLSVKLGIQLDGVPVHDEVSAKVPAVSWEAKKPETPSILLCGMRGSGKSFSGQVAASTLGWPLIDTDLYFQEKYDCTIRDFISKNDWARFREEECAVLEEILKQFPSRHVISLGGGIVETEKGRTILMNYANSTGPVVEIIRPVEEVITYLNEDGNRPSLGESIEQIWARRAPWYRLCSNSEYFNLVHPTVDHALISEVRQAKRAMRQFFRFITGVDTNHVPLNPPVPRNTHFLCLTFPSLSPCPEAHLASLDRFEELTAGCDAVELRVDLLSTSGKAPRTPTIPPTEFVVKQVAALRRLTPLPIIYTVRTCSQGGMFPDGQTEEWCKLAAMGFRTGCEYVDIELGLTPEQNKALCSQKGHSKVIASYHDFSGRLKWDSSEMIQRYHELRAYGDMVKLVSRAADGLDDNMAMLEFRKKHATSEQERQSLITINMGRSGQMSRILSPVLSPTTHPLLPGPPAAPGQLSFHQIQIAQGLLGQIPPKQFWLFGNPIGQSRSPLIHGTGFTTLGLEGYRYEKCETSSVTNDTVLDKIHASDFGGASVTIPLKVEIIKHLDQLTPDAQAVGAVNTVVPVSQPCGKIKLLGANTDWQAIKAKIEANLPAQQALGLITPGQLVRASGVVIGAGGTARAAVYALHSLGYEQIYIHNRTRSKAEEVAKNFPSYFGIRVIDSLGYLCSGQEGVWLPSAIISAVPAHATRLSSDPSSDKLEIPLGLFDRSGGGVVIEMSYSLGKSSPVLRAVENNVGWKSVDGFEVLIEQGARQFQLWTGKLLSLKAVSQAVYQEASSP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJIL01000194
EMBL· GenBank· DDBJ
KNE91638.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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