Q8RF47 · AROB_FUSNN

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
NAD+ (UniProtKB | Rhea| CHEBI:57540 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 divalent metal cation per subunit. Can use either Co2+ or Zn2+.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site61-66NAD+ (UniProtKB | ChEBI)
Binding site95-99NAD+ (UniProtKB | ChEBI)
Binding site119-120NAD+ (UniProtKB | ChEBI)
Binding site132NAD+ (UniProtKB | ChEBI)
Binding site141NAD+ (UniProtKB | ChEBI)
Binding site159-162NAD+ (UniProtKB | ChEBI)
Binding site174Zn2+ (UniProtKB | ChEBI)
Binding site238Zn2+ (UniProtKB | ChEBI)
Binding site255Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-dehydroquinate synthase activity
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
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
    Bifunctional 3-dehydroquinate synthase/phosphatase

Including 2 domains:

Gene names

    • Name
      aroB
    • Ordered locus names
      FN0871

Organism names

Accessions

  • Primary accession
    Q8RF47

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001408141-664Bifunctional 3-dehydroquinate synthase/phosphatase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-3523-dehydroquinate synthase
Region353-664GPPA/PPX

Sequence similarities

In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
In the C-terminal section; belongs to the GppA/Ppx family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    664
  • Mass (Da)
    76,592
  • Last updated
    2002-06-01 v1
  • Checksum
    BAA617D1664402AF
MKKIFDDIYVGSNIISKLNDYTEDFDKILIFSNETIADLYFEKFKSTLNEKDKVFYFAIKDGEEYKNIESILPVYDFMLENNFSRKSLIISLGGGVICDMGGYISATYMRGIEFIQVPTSLLAQVDASVGGKVAINHPKCKNMIGSFKNPYRVIIDVEFLKTLPKREFKSGMGELLKHSFLTKDKSYLEYIENNVEKIKNLDNEVLENIVEQSIRIKKHYVDIDPFEKGERAFLNLGHTYAHALESFFDYKAYTHGEAVSKGIIFDLELSLLRGQIDKEYLERARNIFKLFDIDTDLIYLPSDKFIPLMRKDKKNSFNKIITILLDSEGHLSKTEVKEDEIVKIIDKYKNNFLRASIDIGTNSCRLLIAEVEKDNENITFKKEIYKDLEIVKLGEDVNKNKFLKEEAIERTLKCLKKYRKIIDKYSIEEKNIICFATSATRDSTNKDYFIKKVFDETKIKINCISGDKEAYINFKGVISSFDRDFKDNILVFDIGGGSTEFTLGNMQGIEKKISLNIGSVRITEKFFLNNKLYNYSEENRIKAKDWVKENLKELEDFKKLNFSLIGVAGTTTTQVSVREKMEVYDSEKIHLSNLTSKEINDNLSLFIKNINKQEIKGLDPKRKDVIIGGTIILKEILDYFGKDFIIVSENDNLMGAILEGVENK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE009951
EMBL· GenBank· DDBJ
AAL95067.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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