A0A158RZH7 · A0A158RZH7_9SPHN

Function

function

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.

Catalytic activity

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Note: Binds 1 heme group per subunit.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site28-32substrate
Binding site90substrate
Binding site94substrate
Binding site217Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site231substrate

GO annotations

AspectTerm
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functiontryptophan 2,3-dioxygenase activity
Biological Processtryptophan catabolic process to acetyl-CoA
Biological Processtryptophan catabolic process to kynurenine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tryptophan 2,3-dioxygenase
  • EC number
  • Short names
    TDO
  • Alternative names
    • Tryptamin 2,3-dioxygenase
    • Tryptophan oxygenase
      (TO
      ; TRPO
      )
    • Tryptophan pyrrolase
    • Tryptophanase

Gene names

    • Name
      kynA
    • ORF names
      SPHV1_2230051

Organism names

  • Taxonomic identifier
  • Strain
    • KN65.2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Novosphingobium

Accessions

  • Primary accession
    A0A158RZH7

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    259
  • Mass (Da)
    29,364
  • Last updated
    2016-06-08 v1
  • Checksum
    AE04EE2569719ABB
MTYARYLALDDLLAAQHPVSDEHDELLFIIIHQTKELWLKQILSELHLAIDLVQRDALIEAYKSLARVSRIQSVMTLAWEVLATMTPSDYSTFRPVLGSSSGFQSDQFRTMEFLLGLKQAGHLEFQADRPHARAAMEKALRQPSLWDEANRALARAGFALPPEALERDFSATYEPSPRVEAAWLEVYRDPHRHWDLYQLAEKLVDIDDALSTWRHKHVLTVSRIIGGKPGTGGTSGVPYLASTVTKRAFPELWSLRTSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CCBH010000139
EMBL· GenBank· DDBJ
CDO35320.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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