[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Fibroblast; DOI=10.1016/0006-291X(90)91666-G; PubMed=2109605 [NCBI, ExPASy, EBI, Israel, Japan] Dai W., Gupta S.L.; "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA."; Biochem. Biophys. Res. Commun. 168:1-8(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Lung; DOI=10.1093/nar/18.2.367; PubMed=2326172 [NCBI, ExPASy, EBI, Israel, Japan] Tone S., Takikawa O., Habara-Ohkubo A., Kadoya A., Yoshida R., Kido R.; "Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA."; Nucleic Acids Res. 18:367-367(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0006-291X(92)91590-M; PubMed=1449503 [NCBI, ExPASy, EBI, Israel, Japan] Kadoya A., Tone S., Maeda H., Minatogawa Y., Kido R.; "Gene structure of human indoleamine 2,3-dioxygenase."; Biochem. Biophys. Res. Commun. 189:530-536(1992).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1073/pnas.0508996103; PubMed=16477023 [NCBI, ExPASy, EBI, Israel, Japan] Sugimoto H., Oda S., Otsuki T., Hino T., Yoshida T., Shiro Y.; "Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase."; Proc. Natl. Acad. Sci. U.S.A. 103:2611-2616(2006).

Comments

FUNCTION: Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.
CATALYTIC ACTIVITY: D-tryptophan + O₂ = N-formyl-D-kynurenine.
CATALYTIC ACTIVITY: L-tryptophan + O₂ = N-formyl-L-kynurenine.
COFACTOR: Binds 1 heme group per subunit.
INDUCTION: By interferon gamma.
SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M34455; AAA36081.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17668; CAA35663.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M86472; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86473; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86474; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86475; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86476; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86477; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86478; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86479; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86480; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M86481; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC027882; AAH27882.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PC1161; PC1161.

NP_002155.1; -.

3D structure databases

PDB

2D0T; X-ray; 2.30 A; A/B=1-403.	[ExPASy / RCSB / EBI]
2D0U; X-ray; 3.40 A; A/B=1-403.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2D0T; -.
2D0U; -.

ModBase

P14902.

Enzyme and pathway databases

Reactome

REACT_11127; Metabolism of vitamins and cofactors.

Organism-specific databases

HIX0007467; -.

HGNC:6059; INDO.

147435; gene. [NCBI / EBI]

PharmGKB

PA29869; -.

GeneCards

P14902.

Gene expression databases

ArrayExpress

P14902; -.

CleanEx

HS_INDO; -.

GermOnline

ENSG00000131203; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0009055;	Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0004833;	Molecular function: tryptophan 2,3-dioxygenase activity (inferred from experiment from Reactome).
GO:0007565;	Biological process: female pregnancy (traceable author statement from ProtInc).
GO:0019674;	Biological process: NAD metabolic process (inferred from experiment from Reactome).
GO:0006569;	Biological process: tryptophan catabolic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000898; Indolamine_dOase.
Graphical view of domain structure.

Pfam

PF01231; IDO; 1.
Pfam graphical view of domain structure.

PROSITE

PS00876; IDO_1; 1.
PS00877; IDO_2; 1.

BLOCKS

P14902.

Genome annotation databases

Ensembl

ENSG00000131203; Homo sapiens. [Contig view]

GeneID

3620; -.

KEGG

hsa:3620; -.

Phylogenomic databases

HOGENOM

P14902; -.

HOVERGEN

P14902; -.

Other

BindingDB

P14902; -.

DrugBank

DB00150; L-Tryptophan.

INDO; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Dioxygenase; Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 403`	`403`	`Indoleamine 2,3-dioxygenase.`	`PRO_0000215204`
`METAL`	`346 346`		`Iron (heme proximal ligand).`
`STRAND`	`14 16`	`3`
`TURN`	`19 21`	`3`
`HELIX`	`34 36`	`3`
`HELIX`	`37 44`	`8`
`HELIX`	`46 51`	`6`
`HELIX`	`55 61`	`7`
`HELIX`	`73 92`	`20`
`STRAND`	`95 97`	`3`
`STRAND`	`101 103`	`3`
`HELIX`	`105 118`	`14`
`HELIX`	`126 129`	`4`
`STRAND`	`132 138`	`7`
`HELIX`	`145 147`	`3`
`STRAND`	`148 151`	`4`
`HELIX`	`160 178`	`19`
`HELIX`	`181 189`	`9`
`HELIX`	`193 214`	`22`
`HELIX`	`217 220`	`4`
`HELIX`	`223 228`	`6`
`HELIX`	`230 233`	`4`
`STRAND`	`237 239`	`3`
`HELIX`	`241 243`	`3`
`STRAND`	`247 249`	`3`
`TURN`	`250 252`	`3`
`HELIX`	`264 266`	`3`
`HELIX`	`268 276`	`9`
`STRAND`	`284 286`	`3`
`HELIX`	`287 295`	`9`
`HELIX`	`296 298`	`3`
`HELIX`	`301 311`	`11`
`HELIX`	`316 321`	`6`
`HELIX`	`326 353`	`28`
`HELIX`	`355 358`	`4`
`HELIX`	`382 397`	`16`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 45326 Da [This is the MW of the unprocessed precursor]

CRC64: E92CF57AD0D0BA8D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI ESGQLRERVE 

        70         80         90        100        110        120 
KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR KVLPRNIAVP YCQLSKKLEL 

       130        140        150        160        170        180 
PPILVYADCV LANWKKKDPN KPLTYENMDV LFSFRDGDCS KGFFLVSLLV EIAAASAIKV 

       190        200        210        220        230        240 
IPTVFKAMQM QERDTLLKAL LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN 

       250        260        270        280        290        300 
PQLSDGLVYE GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP 

       310        320        330        340        350        360 
PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV TKYILIPASQ 

       370        380        390        400 
QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL KEG

P14902 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools