A0A9Q5HYH4 · A0A9Q5HYH4_SANBA

Function

function

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.

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

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Pathway

Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 3/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site46O2 (UniProtKB | ChEBI)
Binding site50Fe cation (UniProtKB | ChEBI); catalytic
Binding site56Fe cation (UniProtKB | ChEBI); catalytic
Binding site56substrate
Binding site94Fe cation (UniProtKB | ChEBI); catalytic
Binding site98substrate
Binding site108substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-hydroxyanthranilate 3,4-dioxygenase activity
Molecular Functionferrous iron binding
Molecular FunctionRNA binding
Biological Process'de novo' NAD biosynthetic process from tryptophan
Biological Processanthranilate metabolic process
Biological Processquinolinate biosynthetic process
Biological Processtryptophan catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3-hydroxyanthranilate 3,4-dioxygenase
  • EC number
  • Alternative names
    • 3-hydroxyanthranilate oxygenase
      (3-HAO
      )
    • 3-hydroxyanthranilic acid dioxygenase
      (HAD
      )
    • Biosynthesis of nicotinic acid protein 1

Gene names

    • Name
      BNA1
    • ORF names
      A7U60_g4709

Organism names

Accessions

  • Primary accession
    A0A9Q5HYH4

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain, repeat.

TypeIDPosition(s)Description
Region253-316Disordered
Compositional bias260-302Acidic residues
Domain376-764PUM-HD
Repeat434-469Pumilio
Repeat597-636Pumilio

Sequence similarities

Belongs to the 3-HAO family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    914
  • Mass (Da)
    104,040
  • Last updated
    2023-09-13 v1
  • Checksum
    26D052746216931B
MVLAPPLKLNQWLSENAEKLQPPVNNFCLYSGKDFIVMAVGGPNERNDYHVNETEEWFYQHKGAMLLRVVDGNEFRDIHIKEGEMFLLPGNTPHNPVRFANTVGLVVERVRPTEAIVERVRPTEAIDQLRWYCKSGTHATPTIIREESLRVTDLGTQLKPIIQAWTKYYXDGKDGSYRHCFGVYDYVTGKFVPKSSSISLTEDEILTMAATKNAKKRTAPTNSGIAHKKQHLEQTAACLGKARRKAPVTRIQVVAEVSDKTDEESDDEQSEEDDWEDLASSGVDFEEIEGEEAEFEDSDESGMSVGEEAKPKSAVVQQKDSTSAHILAVFILLLFLRFSGQTDTRESRKAQKVLQQSRRSSKQHFDVLAQAKPLWERARRKNLSPEERKKHVGELMEIVRGKVQDVVFKHDASRIIQTLVKYGSQDMRDEVARELKGRYKDLAQNKYSKFIVTKLIRILPKHRVSILLEFRGHVIRLLLHREASSVIADAYELYANAFERSLLLYDFYGKEVNLFSSALKRGNIADADAKEKEMLKKGLKGVLEDADSERRKRVLAAVKENLELVMNNPEKGAMSHAIFHRVLWEYLSQINELKDEALQEKCQEQMAEMVHTKDGSRVVREVIAQGTAKDRKQIVKVLKPHIERICNDEEAQNVLFTALDVIDDTKLTGKSLVPEITSRAQVLYKSPQGRRALLYLLVPRVSRHFTPVQTAILEETDPIRAKTSKKDERIRREEVLRAASPVLIELLKEKERTERMLRDPGGSLFVTEIMLYAEGDKTKATETLVSLINEPYPSPSDNMPHVIDIPHASRVYKTLLQGGHFSHATQTIIPAPERTFSPIQFSRAWMRGVDKERTREIGLSGGTFVVAALVERVLENGEDEEKREVKRWFDEVFLKKLTESEARGKKVLLDALGN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias260-302Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LNZH02000183
EMBL· GenBank· DDBJ
OCB88190.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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