Reviewed, UniProtKB/Swiss-Prot P48775 (T23O_HUMAN)

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:	TDO2
Synonyms:	TDO

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin 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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD metabolic process Inferred from Experiment. Source: Reactome oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW tryptophan 2,3-dioxygenase activity Ref.1 Inferred from Experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Tryptophan 2,3-dioxygenase		PRO_0000072399
Regions
	Region	42 – 46	5	Substrate binding By similarity
	Region	72 – 76	5	Substrate binding By similarity
	Coiled coil	239 – 271	33	Potential
Sites
	Metal binding	328	1	Iron (heme axial ligand) By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	151	1	Heme By similarity
	Binding site	342	1	Substrate By similarity
Amino acid modifications
	Modified residue	155	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P48775-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 1B89901F445B79FE	FASTA	406	47,872
	10 20 30 40 50 60 MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE 70 80 90 100 110 120 TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV 130 140 150 160 170 180 ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY 190 200 210 220 230 240 RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR 250 260 270 280 290 300 IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE 310 320 330 340 350 360 EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK 370 380 390 400 VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat." Comings D.E., Muhleman D., Dietz G., Sherman M., Forest G.L. Genomics 29:390-396(1995) [PubMed: 8666386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U32989 mRNA. Translation: AAB08514.1. AK289418 mRNA. Translation: BAF82107.1. CH471056 Genomic DNA. Translation: EAX04885.1. BC005355 mRNA. Translation: AAH05355.1.
IPI	IPI00011206.
PIR	G02022.
RefSeq	NP_005642.1.
UniGene	Hs.183671
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P48775. 1 interaction.
STRING	P48775.
PTM databases
PhosphoSite	P48775.
Proteomic databases
PRIDE	P48775.
Genome annotation databases
Ensembl	ENST00000281525; ENSP00000281525; ENSG00000151790; Homo sapiens. [Genome view]
GeneID	6999.
KEGG	hsa:6999.
UCSC	uc003ipf.1. human.
Organism-specific databases
CTD	6999.
GeneCards	GC04P157044.
HGNC	HGNC:11708. TDO2.
MIM	191070. gene.
PharmGKB	PA36427.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P48775.
HOVERGEN	P48775.
OMA	MKLILHE.
Enzyme and pathway databases
BRENDA	1.13.11.11. 247.
Reactome	REACT_11193. Metabolism of vitamins and cofactors. REACT_13. Metabolism of amino acids.
Gene expression databases
ArrayExpress	P48775.
Bgee	P48775.
CleanEx	HS_TDO2.
Genevestigator	P48775.
GermOnline	ENSG00000151790. Homo sapiens.
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...
Other Resources
DrugBank	DB00150. L-Tryptophan.
NextBio	27338.
SOURCE	Search...

Entry information

Entry name

T23O_HUMAN

Accession

Primary (citable) accession number: P48775
Secondary accession number(s): A8K053

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 3, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.