I23O_YEAST
ID I23O_YEAST Reviewed; 453 AA.
AC P47125; D6VWP8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Indoleamine 2,3-dioxygenase;
DE Short=IDO;
DE EC=1.13.11.52;
DE AltName: Full=Biosynthesis of nicotinic acid protein 2;
GN Name=BNA2; OrderedLocusNames=YJR078W; ORFNames=J1840;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA Rytka J., Herbert C.J.;
RT "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL FEBS Lett. 517:97-102(2002).
RN [5]
RP INDUCTION.
RX PubMed=12756250; DOI=10.1074/jbc.m300076200;
RA Rutherford J.C., Jaron S., Winge D.R.;
RT "Aft1p and Aft2p mediate iron-responsive gene expression in yeast through
RT related promoter elements.";
RL J. Biol. Chem. 278:27636-27643(2003).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=12972620; DOI=10.1128/mcb.23.19.7044-7054.2003;
RA Bedalov A., Hirao M., Posakony J., Nelson M., Simon J.A.;
RT "NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+
RT levels in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:7044-7054(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=18828915; DOI=10.1186/gb-2008-9-10-r146;
RA Greenall A., Lei G., Swan D.C., James K., Wang L., Peters H., Wipat A.,
RA Wilkinson D.J., Lydall D.;
RT "A genome wide analysis of the response to uncapped telomeres in budding
RT yeast reveals a novel role for the NAD+ biosynthetic gene BNA2 in
RT chromosome end protection.";
RL Genome Biol. 9:RESEARCH0146.1-RESEARCH0146.17(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21170645; DOI=10.1007/s00239-010-9412-5;
RA Yuasa H.J., Ball H.J.;
RT "Molecular evolution and characterization of fungal indoleamine 2,3-
RT dioxygenases.";
RL J. Mol. Evol. 72:160-168(2011).
RN [10]
RP INDUCTION.
RX PubMed=23481038; DOI=10.1016/j.bbamcr.2013.02.015;
RA Rodriguez-Colman M.J., Sorolla M.A., Vall-Llaura N., Tamarit J., Ros J.,
RA Cabiscol E.;
RT "The FOX transcription factor Hcm1 regulates oxidative metabolism in
RT response to early nutrient limitation in yeast. Role of Snf1 and Tor1/Sch9
RT kinases.";
RL Biochim. Biophys. Acta 1833:2004-2015(2013).
CC -!- FUNCTION: Catalyzes the first step in tryptophan catabolism in order to
CC supply de novo nicotinamide adenine dinucleotide (NAD(+)) via the
CC kynurenine pathway. Plays a role in the cellular response to telomere
CC uncapping. {ECO:0000269|PubMed:12062417, ECO:0000269|PubMed:12972620,
CC ECO:0000269|PubMed:18828915, ECO:0000269|PubMed:21170645}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tryptophan + O2 = N-formyl-D-kynurenine;
CC Xref=Rhea:RHEA:14189, ChEBI:CHEBI:15379, ChEBI:CHEBI:57719,
CC ChEBI:CHEBI:60051; EC=1.13.11.52;
CC Evidence={ECO:0000269|PubMed:21170645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58629; EC=1.13.11.52;
CC Evidence={ECO:0000269|PubMed:21170645};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=412 uM for L-tryptophan {ECO:0000269|PubMed:21170645};
CC KM=9.2 mM for D-tryptophan {ECO:0000269|PubMed:21170645};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC {ECO:0000269|PubMed:12062417}.
CC -!- INDUCTION: Expression is mediated by the AFT2, HCM1, and SUM1
CC transcription factors. Up-regulated in absence of NPT1.
CC {ECO:0000269|PubMed:12756250, ECO:0000269|PubMed:12972620,
CC ECO:0000269|PubMed:23481038}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; Z49578; CAA89606.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39303.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08864.1; -; Genomic_DNA.
DR PIR; S57097; S57097.
DR RefSeq; NP_012612.3; NM_001181736.3.
DR AlphaFoldDB; P47125; -.
DR SMR; P47125; -.
DR BioGRID; 33834; 66.
DR IntAct; P47125; 1.
DR STRING; 4932.YJR078W; -.
DR MaxQB; P47125; -.
DR PaxDb; P47125; -.
DR PRIDE; P47125; -.
DR EnsemblFungi; YJR078W_mRNA; YJR078W; YJR078W.
DR GeneID; 853541; -.
DR KEGG; sce:YJR078W; -.
DR SGD; S000003839; BNA2.
DR VEuPathDB; FungiDB:YJR078W; -.
DR eggNOG; ENOG502QV6W; Eukaryota.
DR HOGENOM; CLU_010089_0_0_1; -.
DR InParanoid; P47125; -.
DR OMA; CMPKGLV; -.
DR BioCyc; MetaCyc:YJR078W-MON; -.
DR BioCyc; YEAST:YJR078W-MON; -.
DR Reactome; R-SCE-71240; Tryptophan catabolism.
DR SABIO-RK; P47125; -.
DR UniPathway; UPA00253; -.
DR PRO; PR:P47125; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47125; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0033754; F:indoleamine 2,3-dioxygenase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:RHEA.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IGI:SGD.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central.
DR InterPro; IPR000898; Indolamine_dOase.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR PANTHER; PTHR28657; PTHR28657; 1.
DR Pfam; PF01231; IDO; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
DR PROSITE; PS00876; IDO_1; 1.
DR PROSITE; PS00877; IDO_2; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..453
FT /note="Indoleamine 2,3-dioxygenase"
FT /id="PRO_0000215208"
FT BINDING 331
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 50775 MW; A8BF1702F6827EC9 CRC64;
MNNTSITGPQ VLHRTKMRPL PVLEKYCISP HHGFLDDRLP LTRLSSKKYM KWEEIVADLP
SLLQEDNKVR SVIDGLDVLD LDETILGDVR ELRRAYSILG FMAHAYIWAS GTPRDVLPEC
IARPLLETAH ILGVPPLATY SSLVLWNFKV TDECKKTETG CLDLENITTI NTFTGTVDES
WFYLVSVRFE KIGSACLNHG LQILRAIRSG DKGDANVIDG LEGLAATIER LSKALMEMEL
KCEPNVFYFK IRPFLAGWTN MSHMGLPQGV RYGAEGQYRI FSGGSNAQSS LIQTLDILLG
VKHTANAAHS SQGDSKINYL DEMKKYMPRE HREFLYHLES VCNIREYVSR NASNRALQEA
YGRCISMLKI FRDNHIQIVT KYIILPSNSK QHGSNKPNVL SPIEPNTKAS GCLGHKVASS
KTIGTGGTRL MPFLKQCRDE TVATADIKNE DKN
