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Protein

Indoleamine 2,3-dioxygenase

Gene

BNA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in tryptophan catabolism in order to supply de novo nicotinamide adenine dinucleotide (NAD+) via the kynurenine pathway. Plays a role in the cellular response to telomere uncapping.4 Publications

Catalytic activityi

D-tryptophan + O2 = N-formyl-D-kynurenine.1 Publication
L-tryptophan + O2 = N-formyl-L-kynurenine.1 Publication

Cofactori

hemeBy similarityNote: Binds 1 heme group per subunit.By similarity

Kineticsi

  1. KM=412 µM for L-tryptophan1 Publication
  2. KM=9.2 mM for D-tryptophan1 Publication

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in the pathway NAD(+) biosynthesis, which is part of Cofactor biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi331 – 3311Iron (heme proximal ligand)By similarity

    GO - Molecular functioni

    • heme binding Source: InterPro
    • indoleamine 2,3-dioxygenase activity Source: SGD
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • 'de novo' NAD biosynthetic process from tryptophan Source: SGD
    • tryptophan catabolic process to kynurenine Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-8164.
    YEAST:YJR078W-MONOMER.
    ReactomeiR-SCE-71240. Tryptophan catabolism.
    UniPathwayiUPA00253.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Indoleamine 2,3-dioxygenase (EC:1.13.11.52)
    Short name:
    IDO
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 2
    Gene namesi
    Name:BNA2
    Ordered Locus Names:YJR078W
    ORF Names:J1840
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiFungiDB:YJR078W.
    SGDiS000003839. BNA2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Indoleamine 2,3-dioxygenasePRO_0000215208Add
    BLAST

    Proteomic databases

    MaxQBiP47125.
    PRIDEiP47125.

    Expressioni

    Inductioni

    Expression is mediated by the AFT2, HCM1, and SUM1 transcription factors. Up-regulated in absence of NPT1.3 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi33834. 32 interactions.
    IntActiP47125. 1 interaction.
    MINTiMINT-4807574.

    Structurei

    3D structure databases

    ProteinModelPortaliP47125.
    SMRiP47125. Positions 49-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the indoleamine 2,3-dioxygenase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000002154.
    HOGENOMiHOG000190192.
    InParanoidiP47125.
    KOiK00463.
    OMAiAPIIPLM.
    OrthoDBiEOG7NGQMM.

    Family and domain databases

    InterProiIPR000898. Indolamine_dOase.
    [Graphical view]
    PfamiPF01231. IDO. 1 hit.
    [Graphical view]
    PROSITEiPS00876. IDO_1. 1 hit.
    PS00877. IDO_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P47125-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNNTSITGPQ VLHRTKMRPL PVLEKYCISP HHGFLDDRLP LTRLSSKKYM
    60 70 80 90 100
    KWEEIVADLP SLLQEDNKVR SVIDGLDVLD LDETILGDVR ELRRAYSILG
    110 120 130 140 150
    FMAHAYIWAS GTPRDVLPEC IARPLLETAH ILGVPPLATY SSLVLWNFKV
    160 170 180 190 200
    TDECKKTETG CLDLENITTI NTFTGTVDES WFYLVSVRFE KIGSACLNHG
    210 220 230 240 250
    LQILRAIRSG DKGDANVIDG LEGLAATIER LSKALMEMEL KCEPNVFYFK
    260 270 280 290 300
    IRPFLAGWTN MSHMGLPQGV RYGAEGQYRI FSGGSNAQSS LIQTLDILLG
    310 320 330 340 350
    VKHTANAAHS SQGDSKINYL DEMKKYMPRE HREFLYHLES VCNIREYVSR
    360 370 380 390 400
    NASNRALQEA YGRCISMLKI FRDNHIQIVT KYIILPSNSK QHGSNKPNVL
    410 420 430 440 450
    SPIEPNTKAS GCLGHKVASS KTIGTGGTRL MPFLKQCRDE TVATADIKNE

    DKN
    Length:453
    Mass (Da):50,775
    Last modified:November 1, 1995 - v1
    Checksum:iA8BF1702F6827EC9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49578 Genomic DNA. Translation: CAA89606.1.
    L47993 Genomic DNA. Translation: AAB39303.1.
    BK006943 Genomic DNA. Translation: DAA08864.1.
    PIRiS57097.
    RefSeqiNP_012612.3. NM_001181736.3.

    Genome annotation databases

    EnsemblFungiiYJR078W; YJR078W; YJR078W.
    GeneIDi853541.
    KEGGisce:YJR078W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49578 Genomic DNA. Translation: CAA89606.1.
    L47993 Genomic DNA. Translation: AAB39303.1.
    BK006943 Genomic DNA. Translation: DAA08864.1.
    PIRiS57097.
    RefSeqiNP_012612.3. NM_001181736.3.

    3D structure databases

    ProteinModelPortaliP47125.
    SMRiP47125. Positions 49-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33834. 32 interactions.
    IntActiP47125. 1 interaction.
    MINTiMINT-4807574.

    Proteomic databases

    MaxQBiP47125.
    PRIDEiP47125.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYJR078W; YJR078W; YJR078W.
    GeneIDi853541.
    KEGGisce:YJR078W.

    Organism-specific databases

    EuPathDBiFungiDB:YJR078W.
    SGDiS000003839. BNA2.

    Phylogenomic databases

    GeneTreeiENSGT00390000002154.
    HOGENOMiHOG000190192.
    InParanoidiP47125.
    KOiK00463.
    OMAiAPIIPLM.
    OrthoDBiEOG7NGQMM.

    Enzyme and pathway databases

    UniPathwayiUPA00253.
    BioCyciMetaCyc:MONOMER-8164.
    YEAST:YJR078W-MONOMER.
    ReactomeiR-SCE-71240. Tryptophan catabolism.

    Miscellaneous databases

    NextBioi974257.
    PROiP47125.

    Family and domain databases

    InterProiIPR000898. Indolamine_dOase.
    [Graphical view]
    PfamiPF01231. IDO. 1 hit.
    [Graphical view]
    PROSITEiPS00876. IDO_1. 1 hit.
    PS00877. IDO_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
      Huang M.-E., Manus V., Chuat J.-C., Galibert F.
      Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae."
      Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M., Rytka J., Herbert C.J.
      FEBS Lett. 517:97-102(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PATHWAY.
    5. "Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements."
      Rutherford J.C., Jaron S., Winge D.R.
      J. Biol. Chem. 278:27636-27643(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae."
      Bedalov A., Hirao M., Posakony J., Nelson M., Simon J.A.
      Mol. Cell. Biol. 23:7044-7054(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "A genome wide analysis of the response to uncapped telomeres in budding yeast reveals a novel role for the NAD+ biosynthetic gene BNA2 in chromosome end protection."
      Greenall A., Lei G., Swan D.C., James K., Wang L., Peters H., Wipat A., Wilkinson D.J., Lydall D.
      Genome Biol. 9:RESEARCH0146.1-RESEARCH0146.17(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Molecular evolution and characterization of fungal indoleamine 2,3-dioxygenases."
      Yuasa H.J., Ball H.J.
      J. Mol. Evol. 72:160-168(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "The FOX transcription factor Hcm1 regulates oxidative metabolism in response to early nutrient limitation in yeast. Role of Snf1 and Tor1/Sch9 kinases."
      Rodriguez-Colman M.J., Sorolla M.A., Vall-Llaura N., Tamarit J., Ros J., Cabiscol E.
      Biochim. Biophys. Acta 1833:2004-2015(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiI23O_YEAST
    AccessioniPrimary (citable) accession number: P47125
    Secondary accession number(s): D6VWP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: May 11, 2016
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 149 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.