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A0A9D4P6K1 · A0A9D4P6K1_DERFA

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.

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

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.

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell presynaptic membrane
Cellular Componentother organism cell membrane
Cellular Componentplasma membrane
Molecular Functionchitin binding
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functiontoxin activity
Molecular Functiontryptophan 2,3-dioxygenase activity
Biological Processexocytosis
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

    • ORF names
      HUG17_0360

Organism names

  • Taxonomic identifier
  • Strain
    • JKM2019
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Analgoidea > Pyroglyphidae > Dermatophagoidinae > Dermatophagoides

Accessions

  • Primary accession
    A0A9D4P6K1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer. Dimer of dimers.

Family & Domains

Features

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

Type
IDPosition(s)Description
Repeat564-596ANK
Repeat658-690ANK
Repeat691-723ANK
Repeat724-756ANK
Compositional bias801-824Polar residues
Region801-832Disordered
Region876-970Disordered
Compositional bias891-917Polar residues
Compositional bias918-932Basic and acidic residues
Compositional bias933-966Polar residues
Region1336-1365Disordered
Region1438-1637Disordered
Compositional bias1454-1469Polar residues
Compositional bias1513-1532Polar residues
Domain1692-1752Chitin-binding type-2

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,777
  • Mass (Da)
    198,267
  • Last updated
    2023-05-03 v1
  • MD5 Checksum
    83571853FC8A3BB1944E72A3D8826E39
MDNDNENLNQESTMTTNGQCPAVNGFRSISTNCSATPSIGMNVLYNDFNDVNQESIKINVSNGGDHPPILVGGGGGCPFGNGGGVSFGYGNFPKLNESTSREIPKGGMLYGEYLHIDKLLSCQEPVTRLVGNEVHDEHLFIITHQAYELWFKQILFEIDSVREIMNKRVKDEANLLIITSRLNRVVLILKLLVDQVTILETMTPLDFMEFRGYLSPASGFQSVQFRLLENKLGIRNDLRTNYGKNYYLKIFEDPKVIDIIKQSEDEHSLCELLQIWLEQTPGLDSPEFNFWERYKLVVNEMLEQIRTSAEEEDDETLKRNGLDEYQRKSELFDSIFDVNKHNALMARGDRRFTHKALQGALMISLYRDEPRFNLPFQILLLLMDIDSLITKWRSNHVEMVLRMIGAHQFGTGGSSGYHYLRSTLSDRYKVFVDLFNLSTFLIPRHCIPPLTVAMKKRLSMMDDSTMIKDLSAKIEKQQQQNENEEKYKILAAFVLSSQNLFIQSFDEQSTMTSPTTIMIHNAAINNDLDLMKKLLLKSDNQMDENYDENNKQRITQLIDCRDSESNTSLLLAALNGHREMVQFLLDIGASINVQNFFNNTALHEAAWKGFSETLEILCNNYQKKQNELMMIMANDNRNHNNDEEMDQLVLNLHLKNKQGHTALHLAAQKGHNQSTRVLLLAGCKPNVKNNFGDTPLHSASRYGHVGVVRILISAFANVNELNKNDDTALHIAAAMNRKKLAKILLENGCNPTIVNRQGETPMNIALRKSYFDIQELIASPPPLKLLYRNISDYSESSLRSRSNNELYTKSSNRNQLQQQQYYEKNHHPTRSETYSYFSAPQIHSSELINRYRIRDPNEQKILHTLLSRVCTPTTQAASSIEPRNKQKSLKKKNPTATLQSRRTIKLYFPLKQSQYRSRNRSNKYEKQQRRRYRNQQQQQQQQQHINNISPQPQSSSSLNSNGYELTRPKLDTLPIDPLGRGEKYFMDLSGHIHKDDNHHHHHQCRQSDRQKSTKINHHRIRNCQSPIMFCTTDQQLLLSSSTLSSCFSRSKSKFQSKSILKSKLISIFSLVHSLIIILSALNVLYNVNANEFNEIWQPQAAQVFEIEYPFVVEPSPLQINSSDIVINDTVAINKVNNNNETNSNLNMNDVLSKYEPELSYEDELNLIGHRTNDDGLIEEDEDGYENENEIEDNSNDNDVDDRWNNSTSRLKREIFRGQNYHYQRGYELSRLRYENRLRTDPTAAKPKAFFIREFHQGRDVPRELLRLTHGDIISDTIQPSTTSPPIISTGHDSDMKTMSDYQQQLFATKAALKAALQSGDKDFSILDYLNKMKAKIDSERQQQQQQKQGSGGHSGSIGGGVGAPLIPTTIGGGGGSTGNIGGIPGGAIIHPDQIIEQIKDIDQKHGGIDGGNLGVRFDEQIKEDLNKILPYDPSKQFGERIRPFRPSWIGSTPGAEPGQGSSGSSAGIAGGGSGNPADDYLNKIRRLYPHLFPGHSGQGIPGQRPGAGGGTGSASPSYGSSGDGSRTSGSGEAGRDSDGDGTGSRPGVGQTGYGGSGGGNDPYSGSGAGPSGGSGAGSGAPYASGGGPSGPFGPSGGGSGPSNQYGGGTGPSGLGVRPVISPPFVTPIGNRTGTYPPLPTLGTPASAYPSRFPGRLLSALTLYPGVRNSTFPGFPGYIRFDYPGYNTVPYTGFRCELQAYKIGYYADVAAGCQVFHICQRDGRMDSFLCPNGTLFHQKVMTCDWWYLVNCPASPSYYYLNGRIGVLPPLPATLGRFD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias801-824Polar residues
Compositional bias891-917Polar residues
Compositional bias918-932Basic and acidic residues
Compositional bias933-966Polar residues
Compositional bias1454-1469Polar residues
Compositional bias1513-1532Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SDOV01000001
EMBL· GenBank· DDBJ
KAH7644822.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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