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Identification
HMDB Protein ID HMDBP00437
Secondary Accession Numbers
  • 5674
  • HMDBP05592
Name Indoleamine 2,3-dioxygenase 1
Synonyms
  1. IDO-1
  2. Indoleamine-pyrrole 2,3-dioxygenase
Gene Name IDO1
Protein Type Unknown
Biological Properties
General Function Involved in heme binding
Specific Function Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.
Pathways
  • African trypanosomiasis
  • L-tryptophan degradation via kynurenine pathway
  • Tryptophan Metabolism
  • Tryptophan metabolism
Reactions
D-Tryptophan + Oxygen → N'-Formylkynurenine details
L-Tryptophan + Oxygen → L-Formylkynurenine details
Oxitriptan + Oxygen → 5-Hydroxy-N-formylkynurenine details
Serotonin + Oxygen → Formyl-5-hydroxykynurenamine details
Melatonin + Oxygen → Acetyl-N-formyl-5-methoxykynurenamine details
GO Classification
Biological Process
tryptophan catabolic process
female pregnancy
positive regulation of apoptotic process
response to lipopolysaccharide
cytokine production involved in inflammatory response
kynurenic acid biosynthetic process
negative regulation of activated T cell proliferation
negative regulation of interleukin-10 production
negative regulation of T cell apoptotic process
positive regulation of chronic inflammatory response
positive regulation of interleukin-12 production
positive regulation of T cell tolerance induction
positive regulation of type 2 immune response
tryptophan catabolic process to kynurenine
behavior
multicellular organismal response to stress
Cellular Component
cytosol
smooth muscle contractile fiber
stereocilium bundle
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
iron ion binding
heme binding
Molecular Function
electron carrier activity
oxygen binding
metal ion binding
indoleamine 2,3-dioxygenase activity
tryptophan 2,3-dioxygenase activity
heme binding
amino acid binding
Cellular Location Not Available
Gene Properties
Chromosome Location 8
Locus 8p12-p11
SNPs IDO1
Gene Sequence
>1212 bp
ATGGCACACGCTATGGAAAACTCCTGGACAATCAGTAAAGAGTACCATATTGATGAAGAA
GTGGGCTTTGCTCTGCCAAATCCACAGGAAAATCTACCTGATTTTTATAATGACTGGATG
TTCATTGCTAAACATCTGCCTGATCTCATAGAGTCTGGCCAGCTTCGAGAAAGAGTTGAG
AAGTTAAACATGCTCAGCATTGATCATCTCACAGACCACAAGTCACAGCGCCTTGCACGT
CTAGTTCTGGGATGCATCACCATGGCATATGTGTGGGGCAAAGGTCATGGAGATGTCCGT
AAGGTCTTGCCAAGAAATATTGCTGTTCCTTACTGCCAACTCTCCAAGAAACTGGAACTG
CCTCCTATTTTGGTTTATGCAGACTGTGTCTTGGCAAACTGGAAGAAAAAGGATCCTAAT
AAGCCCCTGACTTATGAGAACATGGACGTTTTGTTCTCATTTCGTGATGGAGACTGCAGT
AAAGGATTCTTCCTGGTCTCTCTATTGGTGGAAATAGCAGCTGCTTCTGCAATCAAAGTA
ATTCCTACTGTATTCAAGGCAATGCAAATGCAAGAACGGGACACTTTGCTAAAGGCGCTG
TTGGAAATAGCTTCTTGCTTGGAGAAAGCCCTTCAAGTGTTTCACCAAATCCACGATCAT
GTGAACCCAAAAGCATTTTTCAGTGTTCTTCGCATATATTTGTCTGGCTGGAAAGGCAAC
CCCCAGCTATCAGACGGTCTGGTGTATGAAGGGTTCTGGGAAGACCCAAAGGAGTTTGCA
GGGGGCAGTGCAGGCCAAAGCAGCGTCTTTCAGTGCTTTGACGTCCTGCTGGGCATCCAG
CAGACTGCTGGTGGAGGACATGCTGCTCAGTTCCTCCAGGACATGAGAAGATATATGCCA
CCAGCTCACAGGAACTTCCTGTGCTCATTAGAGTCAAATCCCTCAGTCCGTGAGTTTGTC
CTTTCAAAAGGTGATGCTGGCCTGCGGGAAGCTTATGACGCCTGTGTGAAAGCTCTGGTC
TCCCTGAGGAGCTACCATCTGCAAATCGTGACTAAGTACATCCTGATTCCTGCAAGCCAG
CAGCCAAAGGAGAATAAGACCTCTGAAGACCCTTCAAAACTGGAAGCCAAAGGAACTGGA
GGCACTGATTTAATGAATTTCCTGAAGACTGTGAGAAGTACAACTGAGAAATCCCTTTTG
AAGGAAGGTTAA
Protein Properties
Number of Residues 403
Molecular Weight 45325.89
Theoretical pI 7.295
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Indoleamine 2,3-dioxygenase 1
MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVE
KLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLEL
PPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKV
IPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGN
PQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMP
PAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQ
QPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P14902
UniProtKB/Swiss-Prot Entry Name I23O1_HUMAN
PDB IDs
GenBank Gene ID M34455
GeneCard ID IDO1
GenAtlas ID IDO1
HGNC ID HGNC:6059
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Dai W, Gupta SL: Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA. Biochem Biophys Res Commun. 1990 Apr 16;168(1):1-8. [PubMed:2109605 ]
  4. 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. 1990 Jan 25;18(2):367. [PubMed:2326172 ]
  5. Kadoya A, Tone S, Maeda H, Minatogawa Y, Kido R: Gene structure of human indoleamine 2,3-dioxygenase. Biochem Biophys Res Commun. 1992 Nov 30;189(1):530-6. [PubMed:1449503 ]
  6. Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC: Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 2007 Aug 1;67(15):7082-7. [PubMed:17671174 ]
  7. Yuasa HJ, Takubo M, Takahashi A, Hasegawa T, Noma H, Suzuki T: Evolution of vertebrate indoleamine 2,3-dioxygenases. J Mol Evol. 2007 Dec;65(6):705-14. Epub 2007 Nov 17. [PubMed:18026683 ]
  8. 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. 2006 Feb 21;103(8):2611-6. Epub 2006 Feb 13. [PubMed:16477023 ]