Q17P71 (T23O_AEDAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan 2,3-dioxygenase
Short name=TDO
EC=1.13.11.11

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

Gene names

ORF Names:

AAEL000428

Organism

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

Taxonomic identifier

7159 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Aedini › Aedes › Stegomyia

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring. Ref.1
Catalytic activity	L-tryptophan + O2 = N-formyl-L-kynurenine. Ref.1
Cofactor	Binds 2 heme groups per tetramer By similarity.
Enzyme regulation	Stimulated by low concentrations of hydrogen peroxide (5 µM), ascorbate (0.1-0.3 mM), and sodium hydrosulfite (0.1 mM). Inhibited by high concentrations of hydrogen peroxide (0.1 mM), ascorbate (10 mM), and sodium hydrosulfite (1 mM). Ref.1
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.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. Ref.1 Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tryptophan catabolic process to kynurenine Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	heme binding Inferred from direct assay Ref.1. Source: UniProtKB tryptophan 2,3-dioxygenase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Tryptophan 2,3-dioxygenase		PRO_0000360077
Regions
	Region	26 – 30	5	Substrate binding By similarity
	Region	56 – 60	5	Substrate binding By similarity
Sites
	Metal binding	312	1	Iron (heme axial ligand) By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	134	1	Heme By similarity
	Binding site	327	1	Substrate By similarity
Experimental info
	Sequence conflict	293	1	Q → R in AAL37360. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q17P71 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 6DF3EEF489EBC2F9	FASTA	393	45,412
	10 20 30 40 50 60 MSCPVGNHNG DPQGGQRLGS EAGMLYGEYL MLDKVLSAQR MLSVESNKPV HDEHLFIVTH 70 80 90 100 110 120 QAYELWFKQI IFELDSIRSL FSTEHMEESR TLEILKRLNR IVMILKLLVD QVPILETMTP 130 140 150 160 170 180 LDFMDFRDFL SPASGFQSLQ FRLLENKLGV KTEHRVKYNQ KYSEVFASDP CAIERLSITE 190 200 210 220 230 240 SEPSLADLVQ KWLERTPGLE TNGFNFWGKF EESVEQLLAD QEASAMEEEH ENVKNYRLMD 250 260 270 280 290 300 IEKRREVYKS IFDASVHDAL VARGDRRFTH RALQGAIMIT FYRDEPRFSQ PHQLLMLLMD 310 320 330 340 350 360 IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFIDL FNLSTFLIPR 370 380 390 GSIPPLTCEM QKALNLAWGS PVHQAKQINY AAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biochemical mechanisms leading to tryptophan 2,3-dioxygenase activation." Li J.S., Han Q., Fang J., Rizzi M., James A.A., Li J. Arch. Insect Biochem. Physiol. 64:74-87(2007) [PubMed: 17212352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Genome sequence of Aedes aegypti, a major arbovirus vector." Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P. , Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W. Science 316:1718-1723(2007) [PubMed: 17510324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LVPib12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF325458 mRNA. Translation: AAL37360.1. CH477193 Genomic DNA. Translation: EAT48562.1.
RefSeq	XP_001656460.1. XM_001656410.1.
UniGene	Aae.300.
3D structure databases
ProteinModelPortal	Q17P71.
ModBase	Search...
Protein-protein interaction databases
STRING	Q17P71.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	AAEL000428-RA; AAEL000428-PA; AAEL000428.
GeneID	5577377.
KEGG	aag:AaeL_AAEL000428.
VectorBase	AAEL000428. Aedes aegypti.
Phylogenomic databases
eggNOG	inNOG07042.
GeneTree	EMGT00050000008199.
OMA	KLLVDQV.
OrthoDB	EOG4NCJVC.
PhylomeDB	Q17P71.
Family and domain databases
InterPro	IPR004981. Trp_2_3_dOase. [Graphical view]
KO	K00453.
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

T23O_AEDAE

Accession

Primary (citable) accession number: Q17P71
Secondary accession number(s): Q8WSB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 25, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)