H3GHV1 · H3GHV1_PHYRM

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

Organism names

Accessions

  • Primary accession
    H3GHV1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain78-3363-dehydroquinate synthase
Domain379-803Enolpyruvate transferase
Domain1259-1343Shikimate dehydrogenase substrate binding N-terminal
Domain1382-1456Quinate/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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,547
  • Mass (Da)
    167,786
  • Last updated
    2012-04-18 v1
  • Checksum
    D72E5013C3470CEC
MSAPQVVSCGSYDIVLGSSLLQSRFVAEDLLQRLPSTATFVILTDANVGPLYAEPLRVQLAALLHAQGNTTRRVLLHAIPSGEASKCREMKAKIEDEVLFPNRCHRDTCIVAVGGGVVGDLSGYVASTYMRGVPFVQVPTSLLACVDSSIGGKTGIDVEAGKNLLGAFHMPQRVYIDLSVLHTLPKRELINGMGEVVKSGAIFNAELFELLETSAESILALSDMDLVQRVVALTVQVKATVVTQDTKEMGLRAILNFGHSIGHGIEALVQPEYLHGECVSMGCIKEAEIARGMGVCSSATVGRLRRCLASYGLPVRVPEHVATRDVLVKMEVDKKNSQGVKKIVLLEKIGKVLADPYARAVKDHQIELVLEKQVRMVPGAKANGTIRVPGSKSISNRVLLMAALGKGACRITGLLHSDDTQVMMTALQKVGAKFSWEDNGAVLVVEGTAGKFATVADGEEIYLSNAGTAARFLTSAMTLVPSENDGTVVVTGNYRMKERPIAPLVEALRGNGCDISYLETEGCPPLAIRGTGLRGGTVRLAAKVSSQYVSSVLISAPYAKEPLVLELDEEQPTSLPYILMTTQLMQQFGIPVETLAPNRYRVPCGVYENPKEVSVEVDASSATYPLAFAAITGGQVTVEALGNTSLQGDAAFHTLLRSMGCTTTQDATSTTVIGPQDGTPLKAVDIDMETMTDAFMTAVALAAVADGTTKITGIANQRVKECNRIEVMVTELHKIGVECGELPDGIWIKGTAGKTDHLKQASIACHNDHRIAMSFAVLGSVVGNVVITDKECTDKTYPEFWDHVQMHLGLQVAPVVEETTDSNDSDTSIPGVFMIGMRGAGKSSLAKAASATLKLNLLDTDKVLEKEFGESIADFVARHNHTWEAFREKQKELLLRLIANPPPATIISCGGGVVETPEIVAALEKYPYVVHVHRDIRDVLAYLDTVEESHRPSLGDSHANVWARREPLYQRSATFEFVVTAGDVDYPRLDRDFVRFLSVITPGLPTNFDYRSSCRADTFFLSLTFPDMNDARPIISDISKGADALELRVDLLKYPQDTKFVAAQVALLRTLSSLPIIFTVRSKGQGGAFPDGEENELKMFELLQLGVRLGCEFVDMETCWSRKAREHLLAHRYRSAIISSFHAVQKPTSEAETKLIFRECYSQGRVQIVKVVVKAYSPQDALMVDRVAKDFANAWQQQMPIISLCTTEAGKLTRVLNRTLTPVTHPLLPAAAAPGQLSIEEIMILRKQLGLLPAREFFLFGSPIQKSPSPAMHNAGFESTSLSSLFTYGLHDTTDVLEIVKRMQAPDTCFGGGSVTIPLKVDIMAHLNELSPAARAIGAVNTIMREDRNGSPYWKGDNTDWLGILRPISKRLATLSVRKPAHELTALVVGAGGTSMAASYAMRQLGVGKLFIFNRTLEKAQAVAARFDAEALSELTPETLAQVDVVVGTIPAQAGFQLPDHLVAPRADGSKVVVLDAAYMPPITPMLAHAHASGGALCIQGYEMLYEQGIEQFYRWHKATQVWVVNEEAIKEACRQHVPIDQRLSQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS566010
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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