ID M2T2R5_COCH5 Unreviewed; 1590 AA.
AC M2T2R5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN ORFNames=COCHEDRAFT_1212955 {ECO:0000313|EMBL:EMD91850.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD91850.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD91850.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007119}.
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DR EMBL; KB445575; EMD91850.1; -; Genomic_DNA.
DR STRING; 701091.M2T2R5; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001693_0_0_1; -.
DR OMA; WIGVHGK; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR Gene3D; 1.20.58.480; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000898; Indolamine_dOase.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF01231; IDO; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016936}.
FT DOMAIN 992..1073
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 176133 MW; EF51E6B94F4C1825 CRC64;
MSLRSEQCPV SGMAGGHCPA ESAAASKNGS RMGPRGCTFS GYAAPGDVHA AFGIPQHANV
EEFLRQRERK AINELIYSNV PSMAEIKEIQ NAKGVKSLDT LNMDERDLLA IALGAPARQV
ILRAEEVGPA TGWRDGYLST EYGFQPPDTS EAPGALRNSP GRVWMDLCTR MPGCVARGRV
RESIAALPII QGTADTIPDK ALWAALVALG MLCSIYRYEE RHDGNEGINV AAKPFKLKGV
PICDDLGDEV QGIPRSIGLP YVQISIRMGR SIPHLTFFDQ SSFNVDYMDP LSKYPYVGRF
DNIKLRWGMF GDSAENAFLK GCADTSASFQ HGPDAIAACQ EHVMNRNNEG LLRELIRLKE
ILERMPTAFN TISPNDRSGE NYVSPTEWVR WAKFSAPLSK RCPATSGLQF PPYLVMDAFL
GRKKYNSFLG AEGVHLRAWL PSNLRAFIAS IEYHYQIPEY VKASGDPRLI GVLDGVVEAY
TGERGFMGAH RYKVFGLLEC AGKSGRTETN GASGAADAMR PWEKTHAEFS EAMKERLEPF
RGQRDIEPHE MRGTFEECRY RGRILSRNFV DSDPKRSIAM VTLDIQDTGI TFQPGDRLAV
MPMNSWTECA KVAAALGLDT MLSDPVSLDR IWTRYAAHMG AISHTDKPQL TVIDILRKGH
LAPITKKLAT KLHTLLRASS HVVLQVLATD EWPVRASLGD LLQEAVKDTS PRIWDQAFDL
SGNLAWLTDL ISVEVPRTYS ISNYSDELLP STVDLTISRS EYDLCPLFAG TEKHVRNGVS
SGFLNPPVAE EMDVLDDEEI LIGVSRPFSF QLPHDDTSPV ALFAGGSGVA PFRSFWQARC
GQAWGKTVLY LGVQSRQKFC YESELRQYVN EGLMEVHTAF SRDTNGLVYD PVSRDLVERE
MPSRYIDGLI VEQGQSVCDL VMSKKQGGIG GYLYVCGSVG VFDSVMSGIR QALYNHRSPT
METVETILNT AFAERRFMLD VFMTPRPLPC NQPTISLSQL AVHTGHVKDS RVWIGVHGKV
YDVTDFCTMH PGGTNIIKSN GGVDCTKSFD LLAHTNNPEV SSLLTKYYIG ELTPKPAFQS
EEIGMLYDLW KGYLRVATEQ VVAASFEVGM ITESSLVWFQ GDLFNMGGVR RFYHYQSRLL
EGGFSTLFGA KLQELYLKIS FTLANVSSAN TKLSDVLGVI ARAKSSHDAV TASNEISQIG
QFTCDSESAR HHEKGIIAYA QRSVKYDMEF LEAIREEACT GMDAFDSIME LDASSNSERV
TALSTFLMQV LERMANRLEG FYAKLARHSV FQPEMERNPA RARWNILKRK VWDGSFFILA
REASIQPTIR YPTNGVDFDR VVSQIEMSLS KSSPMTPRIM GLNEQHAARA MSTASGTPAY
EVHTQSNALK AMSTFIDSNK KAIRRLSKLP QAIDLQQLMQ TYGSLPQGNH TLPTPPSSRS
PSMSSSTRFP MGRRRSRTVN DMPQLLQRRT TGVSDLTRSN LGASAHPSPT ATMSALMTKM
NTRTKSITSP IHRSPDHYDQ DRARSVQALS LQRPDRMVGT GNAGSEYGGS TRMDSPHMRS
KSTTGNLRAF RLQASTMAGG MNRRSDMGRT
//
