A0AAF0EFF5 · A0AAF0EFF5_9BASI

  • Protein
    Pentafunctional AROM polypeptide
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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

  • 3-dehydroquinate = 3-dehydroshikimate + H2O
    EC:4.2.1.10 (UniProtKB | ENZYME | Rhea)
  • 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
    This reaction proceeds in the forward direction.
    EC:2.5.1.19 (UniProtKB | ENZYME | Rhea)
  • 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
    EC:4.2.3.4 (UniProtKB | ENZYME | Rhea)
  • shikimate + ATP = 3-phosphoshikimate + ADP + H+
    EC:2.7.1.71 (UniProtKB | ENZYME | Rhea)
  • shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
    EC:1.1.1.25 (UniProtKB | ENZYME | Rhea)
  • a 5,6-dihydrouridine in mRNA + NAD+ = a uridine in mRNA + NADH + H+
    This reaction proceeds in the backward direction.
  • a 5,6-dihydrouridine in mRNA + NADP+ = a uridine in mRNA + NADPH + H+
    This reaction proceeds in the backward direction.

Cofactor

Protein has several cofactor binding sites:
FMN (UniProtKB | Rhea| CHEBI:58210 )

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 site454-457NAD+ (UniProtKB | ChEBI)
Binding site485-487NAD+ (UniProtKB | ChEBI)
Binding site490NAD+ (UniProtKB | ChEBI)
Binding site5017-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site510-511NAD+ (UniProtKB | ChEBI)
Binding site5177-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site5237-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site532NAD+ (UniProtKB | ChEBI)
Binding site5337-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site550-553NAD+ (UniProtKB | ChEBI)
Binding site561NAD+ (UniProtKB | ChEBI)
Binding site565Zn2+ (UniProtKB | ChEBI); catalytic
Binding site565-5687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site6297-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site639Proton acceptor; for 3-dehydroquinate synthase activity
Binding site643-6477-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site6507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site650Zn2+ (UniProtKB | ChEBI); catalytic
Active site654Proton acceptor; for 3-dehydroquinate synthase activity
Binding site6667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site666Zn2+ (UniProtKB | ChEBI); catalytic
Binding site7357-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site1195For EPSP synthase activity
Binding site1251-1258ATP (UniProtKB | ChEBI)
Active site1539Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1567Schiff-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 Functionflavin adenine dinucleotide binding
Molecular Functionmetal ion binding
Molecular Functionshikimate 3-dehydrogenase (NADP+) activity
Molecular Functionshikimate kinase activity
Molecular FunctiontRNA dihydrouridine synthase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process
Biological ProcessmRNA processing
Biological Processphosphorylation

Keywords

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
      MEQU1_002107

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 12830
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Malasseziomycetes > Malasseziales > Malasseziaceae > Malassezia

Accessions

  • Primary accession
    A0AAF0EFF5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-7633-dehydroquinate synthase
Domain42-303DUS-like FMN-binding
Domain449-7373-dehydroquinate synthase
Domain790-1207Enolpyruvate transferase
Region1648-1934Shikimate dehydrogenase
Domain1653-1734Shikimate dehydrogenase substrate binding N-terminal
Domain1758-1839Quinate/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 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
    1,934
  • Mass (Da)
    209,009
  • Last updated
    2024-05-29 v1
  • Checksum
    98DE120A329F6C8C
MTTSLRAEECVDEGRTKRLKLDTAMPPPSDPRMPAFDRGLFLAPMVRIGSLPSRLLALEYGADLVWSPEIVDRAIMGTTRRVNATTGLVEFMKGDKQIFSCHPVERPYLIYQVGSSTPENAAEAVRIVTAHDDVAGVDLNCGCPKPFSTLGGMGANLLTEPDLLCDILRQMRRAAPPHVSVTCKIRLLPTQAETLALVEQIVRTRTIRALTIHCRTKPMRPREPALVDRFREIAEHVQKVAAETGQDVPVIYNGDCFGASDWPRLRERTGASAVMMARAAELNPSCFQLQRQCVATVIAPRWMHYAVRFDNPFGNTKYCVTQLAFSTWAGARECEAPRASTGEPGEELPIPTMSEAGGGHKVPSYHAPPYTSELSGATIHELRCLDTRIQLGFHLVPHIVQTLYAELPTSSYVLFTDAHLEALGVIDKFREAFETYKPEGNTSRMLAHVLPPGEESKSRETKAGIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSAVGGKTAIDHPHGKNLIGAFHQPQFVFVDAAWLLTLPEREFANGMAEVVKTAAIWDADDFDKLESESQSIQAAVLSDEARSAPAGLGHTLDTRTPSQTLLLDVIRGSIGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPAILHGECVAVGMIFEAEIARAMHGLPQVVIGRLVRALTNYGLPVSLKDARIAALPQAQAITTARLLDIMRVDKKNAGTAKKIVLLSRIGATVEERASTVPDAVIARVLAPSVQVGSSLGTPREPVTLPTPGSKSVSNRALVLAALAQGTCRLRNLLHSDDTQVMMNALRTLRAADFAWEEDGAQLVVHGGGGRLVACDKPVYLQNAGTAARFMTGVTTLLREGTVTLTGNARMKQRPIGPLVEALCANGAAIACVEAPGALPLRITGRGGLQGGVIRLAADVSSQYVSAVLLCAPYAQEAVTLELVGGKVISQPYIDMTVAMMQSFGVQVERVAEHVYRIPQQVYRAPDVYTVESDASSATYPLAMAAITGTTVTVPSIGSASLQGDARFARDVLAPMGCHVEQTEASTTVTGPPPGTLRQLNEVDMEPMTDAFMTAAVLFAVAQGTSTKITGIANQRVKECDRLRATVTELAKFGVQAHEHDDGIVVYGRPLSELQTSEPIACYDDHRIAMAFSVLASVVPSTRTTLEEKRCVEKTWPSWWDVLSTQLCVPIAAADEDVSLVPLPRASATLHGLPHRYAPDATIVLIGMRASGKSHIGRRLAARMHRTFVDADDVFSQRFDLSAFVAQHGWDAFRMEETRVLEQLLRDCARGHVLALGGGVVESAASRALLTAFQRTGPVVHIVRRYEDIEAFLATSDRPAYGEPLRTVYDRRQPWYEACACMETVNEGDVVTLLERQLATPLGAPGKERPAFFLSLTFPHVRDALPVLATASAGVDVLELRVDLLHPSGVPSIDEVRAQVALLRQHSSLPILYTVRSASEGGRCPDDNEQAYWALVRLGLRLGCEWVDVELRRSADYGRALRAQDVASRIVASAHDTTGQMPWSSSAIARLYERGRQEGDVVKLVGVARTVQDNMALEHFRTAVARDTSTLIAINMHAAGQLSRVLNPLLTPVTHPRLPSKAAPGQLSVQEIHQARHLLGLLPAQRFALLGSPIAHSLSPLIHNTSFELLGLPHKYALHETASVEESVAALIRAPDFGGASVTIPHKCAITSLLHTLSPEAEAIGAVNTVVPQRDAGRLWLRGENTDWQAIYELAQRARPSAHTALVIGAGGSARAALYAMHRLGVSTILLYNRTYAKAMELAAAVPTEWHVQPLKTLSDAVAQAPDVIVSNVPAAGTSLTPGGADIVLPADLLSSAGGVAIDMAYRPEKTPLLTLVEQNPAWHGVRGLEILLTQAFHQFHLWTGLPAPHDEVARAAWQAYHAQAEAHST

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP119903
EMBL· GenBank· DDBJ
WFD23418.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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