W2HZ93 · W2HZ93_PHYNI

Function

function

The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.

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.

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
  • 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
      L916_19194

Organism names

Accessions

  • Primary accession
    W2HZ93

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain79-3373-dehydroquinate synthase
Domain380-804Enolpyruvate transferase
Domain1260-1344Shikimate dehydrogenase substrate binding N-terminal
Domain1382-1480Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,548
  • Mass (Da)
    167,887
  • Last updated
    2014-03-19 v1
  • MD5 Checksum
    B48415E5DD043FF52AE9972288A996E1
MSVAPQVVPCGSYDIVLGSLLLQSRFVAEDLLQRLPNTSTFVILTDANVGPLYAEPLRAQLAELLQAQGNTARRVLLHAVPAGEASKCREMKAKIEDEVLFPNRCHRDTCVVAVGGGVVGDLAGYVASTYMRGVPFVQVPTSLLACVDSSIGGKTGIDVEAGKNLLGAFHMPQRVYIDLNVLHTLPKRELVNGMGEVIKSGAIFNAELFELLENSAETILSLSDMDVVQRVVALTVQVKATVVTQDTKEMGLRAILNFGHSIGHGIEALLQPEYLHGECVSMGCIKEAEIARGMGICTSATVGRLRRCLAAYGLPVRVPDHVATRDVLVKMEVDKKNSQGVKKIVLLEEIGKVLANPYARAVKDHQIELVLEKQVRMVPGAKANGTIRVPGSKSISNRVLLMAALGKGSCRITGLLHSDDTQVMMNALQKVGAKFSWEDNGAVLVVEGTAGKFATVADGEEIYLSNAGTAARFLTSAMTLVPSQNGGTVVVTGNYRMKERPIAPLVDALRGNGCEISYLETEGCPPLAIRGTGLRGGTVRLAAKVSSQYVSSVLISAPYAKEPLVLELEEEEPTSLPYILMTTQLMKQFGIPVETLAPNRYRVPCGVYENPKEVSVEVDASSATYPLAFAAITGGQVTVEALGNTSLQGDAAFHTLLRSMGCTTTQDATSTTVSGPQDGTPLKAVEIDMETMTDAFMTAVALAAVADGTTKITGIANQRVKECNRIEVMVTELRKIGVECGELPDGIWIKGTAGKTDHLKKASIACHNDHRIAMSFAVLGSVVDNVIITDKECTDKTYPEFWDHVQMHLGLEVAPVVEEKTNNIDAETTIPGVFVIGMRGAGKSSLAKAASAALKLDLLDTDKVLEKEFGESIADFVARHNHTWEAFREKQKELLLRLIANPPPATIISCGGGVVETPEIVDALEKYPHVVHVQRDIKDVLAYLDSVEESHRPSLGDSHANIWTRREPLYQRSSTFDFVVNAGDVDYPRIDRDFVRFLSVILPGLPTSFDYRSSCRSDTFFLSLTFPDVNDARSLISDISKGADALELRVDLLKNPEDTKFVAAQVALLRSLSTLPIIFTVRSKGQGGAFPDGEEHEQKMFELLQLGVRLGCEFIDMETCWSRKAREQLLTHRHRSAIISSFHAVQKPTSEAETKAIFRECYSQGRVQIVKVVVKAYSPADALMVDRVAKDFATAWQQQMPIISLCTTEAGKLTRVLNRTLTPVTHPMLPAAAAPGQLSVEEIMTLRKQLGLLPAREFFLFGSPIQKSPSPAMHNAGFASTSLTSLFTYGLHDTTDVLEIVKRMQAFDTNFGGGSVTIPLKVDIMEHLDELSPAAQAIGAVNTIMRQDRNGAPYWKGDNTDWLGILRPISKRLATLSVNKPAHELTALVVGAGGTSMAASYAMRQLGVGKLFIFNRTLEKAQAVAVRFDAEALSELTVESLAQVDVVVGTIPAQAGFQLPEHLVAPRADGSKVVVLDAAYMPPITPMLAHAHAAGGALCIQGYEMLYEQGIEQFYRWHKATQVWTVDEEAIKEACRQHVPVDQRLSQA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI676000
EMBL· GenBank· DDBJ
ETL27235.1
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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help