ID M2RLX1_COCSN Unreviewed; 1553 AA.
AC M2RLX1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN ORFNames=COCSADRAFT_352599 {ECO:0000313|EMBL:EMD67609.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD67609.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD67609.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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; KB445639; EMD67609.1; -; Genomic_DNA.
DR RefSeq; XP_007697220.1; XM_007699030.1.
DR STRING; 665912.M2RLX1; -.
DR GeneID; 19138164; -.
DR KEGG; bsc:COCSADRAFT_352599; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001693_0_0_1; -.
DR OMA; WIGVHGK; -.
DR OrthoDB; 2723058at2759; -.
DR Proteomes; UP000016934; 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:UP000016934}.
FT DOMAIN 955..1036
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1553 AA; 172023 MW; 7A74A2E6D9A30482 CRC64;
MAGGHCPAES AAASKNGSRM GPRGCTFSGY AAPGDVHAAF GIPQHANVEE FLRQRERKAI
NELIYSNVPS MAEIKEIQNA KGVKSLDTLN MDERDLLAIA LGAPARQVIL RAEEVGPATG
WRDGYLSTEY GFQPPDTSEA PGALRNSPGR VWMDLCTRMP GCVARGRVRE SIAALPIIQG
TADTIPDKAL WAALVALGML CSIYRYEERH DGNEGINVAA KPFKLKGVPI CDDLGDEVQG
IPRSIGLPYV QISIRMGRSI PHLTFFDQSS FNVDYVDPLS KYPYVGRFDN TKLRWGMFGD
SAENAFLKGC ADTSASFQHG PDAIAACQEH VMNRNNEGLL RELIRLKEIL ERMPTAFNTI
SPNDRSGENY VSPTEYLVMD AFLGRKKYNS FLGAEGVHLR AWLPSNLRAF IASIEYHYQI
PEYVKASGDP RLMGVLDGVV EAYTGERGFM GAHRYKVFGL LECAGKSGRT ETNGASGAAD
AMRPWEKTHA EFSEAMKERL EPFRGQRDIE PHEMRGTFEE CRYRGRILSR NFVDSDPKRS
IAMVTLDIQD TGITFQPGDR LAIMPMNSWT ECAKVAAALG LDTMLSDPVS LDRIWTRYAA
HMGAISHTDK SQLTVIDILR KGHLAPITKK LATKLHTLLR ASSHAVLQVL ATDEWPVRAS
LGDLLQEAVK DTSPRIWDQA FDLAGSLAWL TDLISVEVPR TYSISNYSDE LLPSTVDLTI
SRSEYDLCPL FAGTEKHVRN GVSSGFLNPP VAEEMDVLDD EEILIGVSRP FSFQLPHDDT
SPVALFAGGS GVAPFRSFWQ ARCGQAWGKT VLYLGVQSRQ KFCYESELRQ YVNEGLMEVH
TAFSRDTNGL VYDPVSRDLV EREMPSRYID GLIVEQGQSI CDLVMSKKQG GIGGYLYVCG
SVGVFDSVMS GIRQALYNHR SPTMETVETI LNTAFAERRF MLDVFMTPRP LPCNQPTISL
SQLAVHTGHV KGSRVWIGVH GKVYDVTDFC TMHPGGTNII KSNGGVDCTK SFDLLAHTNN
PEVSSLLTKY YIGELTPKPA FQSEEIGMLY DLWKGYLRVA TEQVVAASFE VGMITESSLV
WFQGDLFNMG GVRRFYHYQS RLLEGGFSTL FGAKLQELYL KISFTLANVS SANTKLSDVL
GVIARAKSSH DAVMASNEIS QIGQFTCDSE SARHHEKGII SYAQRSVKYD MEFLEAIREE
ACTGMDAFDS IMELDALSNP ERVTALSTFL MQVLERMANR LEGFYAKLAR HSVFQPEMER
NPARARWNIL KRKVWDGSFF ILAREASIQP TIRYPTNGVD FDRVVSQIEM SLSRSSPMTP
RIMGLNEQHA ARAMSTASGT PAYEVHTQSN ALKAMSTFID SNKKAIRRLS KLPQAIDLQQ
LMQTYGSLPQ GNHTLPTPPS SRSPSMSSTT RFPMGRRRSR TVNDMPQLLQ RRITGVSDLT
RSNSGASSHP SPTAAMSALM TKMNTRIKSI TSPVYRSPDH SDEDRERSVR ALSLQRPDRM
VGLGNAGSDY GGSSRMDSPH MRSKSTTGNL RAFRLQASTM AGGMNRRSDM GRT
//
