Reviewed, UniProtKB/Swiss-Prot Q55DB4 (T23O_DICDI)

Names and origin

Protein names

Recommended name:
    Tryptophan 2,3-dioxygenase
      Short name=TDO
    EC=1.13.11.11
Alternative name(s):
    Tryptophan pyrrolase
      Short name=Tryptophanase
    Tryptophan oxygenase
      Short name=TRPO
      Short name=TO
    Tryptamin 2,3-dioxygenase

Gene names

Name:	tdo
ORF Names:	DDB_G0269714

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity.
Catalytic activity	L-tryptophan + O2 = N-formyl-L-kynurenine.
Cofactor	Binds 2 heme groups per tetramer By similarity.
Pathway	Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the tryptophan 2,3-dioxygenase family.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Domain	Coiled coil
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: InterPro
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW tryptophan 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	Tryptophan 2,3-dioxygenase		PRO_0000327794
Regions
	Region	45 – 49	5	Substrate binding By similarity
	Region	75 – 79	5	Substrate binding By similarity
	Coiled coil	194 – 257	64	Potential
Sites
	Metal binding	332	1	Iron (heme axial ligand) By similarity
	Binding site	146	1	Substrate By similarity
	Binding site	153	1	Heme By similarity
	Binding site	346	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55DB4-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 2C3BC0FC9C9D4072	FASTA	400	46,608
	10 20 30 40 50 60 MSGCQFNQPY CPRSEEKKSI AESIEKATLM EPSIDAQSAQ KGVYYGSYLK LDELLNIQEC 70 80 90 100 110 120 ESVKVGAPAH EEMLFIIIHQ TYELWFKQMI HEIDSIRSIM STPPTPERLN GVIVNRLGRI 130 140 150 160 170 180 TEIQKLLVDQ ISILETMTSV DFLEFRNLLV PASGFQSVQF RMIENKLGIL PNTRVQYQQH 190 200 210 220 230 240 HYHSFFNEKD RKALQATENE VSLLQLVIQW LERNPFLYYK GYDFWSSYKS AVDQILENDL 250 260 270 280 290 300 QRIQANNDLS QDMKDQSTKE AKKNMESFST LFDEVAYNER LEKGEVRLSY KALQSAILIY 310 320 330 340 350 360 LYKDEPIFHT PFLILNLLTE IDELLTMWRF RHTMMVQRII GAKIGTGGSS GYHYLRTTVG 370 380 390 400 DRYKIFLDLF NISSYLIPKN TLPQLPKVVK EQMDFAWSIL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000005 Genomic DNA. Translation: EAL72207.1.
RefSeq	XP_646217.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3397237.
KEGG	ddi:DDB_0231363.
Organism-specific databases
dictyBase	DDB_G0269714. tdo.
Phylogenomic databases
OMA	Q55DB4. HYRDNFR.
Enzyme and pathway databases
BRENDA	1.13.11.11. 424.
Family and domain databases
InterPro	IPR004981. Trp_2_3_dOase. [Graphical view]
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

T23O_DICDI

Accession

Primary (citable) accession number: Q55DB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)