ID T0KTM5_COLGC Unreviewed; 1695 AA.
AC T0KTM5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN ORFNames=CGLO_04022 {ECO:0000313|EMBL:EQB55993.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB55993.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQB55993.1}.
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DR EMBL; AMYD01000816; EQB55993.1; -; Genomic_DNA.
DR STRING; 1237896.T0KTM5; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001693_0_0_1; -.
DR OMA; PWEETHR; -.
DR OrthoDB; 2723058at2759; -.
DR Proteomes; UP000015530; 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; 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; 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.
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:UP000015530}.
FT DOMAIN 994..1075
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1695 AA; 185738 MW; A9F1DA551D7E855A CRC64;
MAFSERSCPV SGSMGGRGRC PAGAAATGRQ SRSSSRMGPR GCSFSGFSQP GDIHTAFDIP
RGVDAEEWLR MRERKSINQI LYSSYPSQQE IDSAKDQKQM DAMNVNEQDL LAVALGAPAR
QVMLRAEEIG PATGWKDGYL SIEHGFCPPD YDEAAGALAR SPGRIWSDLA ERMPGCVSRG
RVRESIAAAP VIEGTEDIIP DQALWAALVA LGMLCSIYRF EQKYDGHDGV NATTNPSKLR
LNCKMGDYLG EELVGIPLSI ALPYFQVSRR MGRTLPHLTF VDQSSYNLKV KDATSSFPYV
ARFDNIELRW PMFGERAEVA FLKGVADTSA SFQHGPDAIA ACQEHVMNRN NEGLLHEMIR
LKEILERMPG AFHSISTNPN AGENYVPVQQ WVRWAKFSAP LSKRCPASSG LQFPPYLVMD
AFLGRKKYTS FLGAEGVHLR AWLPSNLRAF IAAIEYHYRI PEYVQQSGDP RLMGVLDGIV
EAYTGERGFM GVHRYKVFGI LEVAAKTGRT ETNGASGAAD GERPWEETHR QFSEAMKERL
EPYRGALPVE PHQMRGTFEE CRYVTRVLSR SFVDSDPSRS IAMVTLDIRD TGITWAPGDR
LAVMPLNGWE ECAKVIAALG LEEHIDAPVE TTGTWARFEM HLGSVRRTAT PKLTVGDILR
RGHLAPITKE MALKIHGMLH ASSNTVLQVL STDEWPVRGS LGDLLQDAVT DTPPQIWDRV
FNLEDLSWLA DLVKLEVPRT YSIASYTEEL LPETVDLAVS RSEYKLCSTF AKGRDISRSG
VSSGFLNPPV EMGEIDSDDA LLIGVSRPAA FQLPLDPMAP CAFFAGGSGI APFRSFWQAR
LAQSGLSGGK NSLYLGVQSR EKFCFEEELR QYVNADFMEV HLAFSRDSRG LAYEGHDLVE
KHIPPRYIDT LIVEQGAQIC DLVMSKKQGG LGGYLYVCGS VSVFDSVMQG IRKAIYTYRT
ATESGVDTIV NKAFAERRFM LDVFMTPKPL PCTLPTIPLS QLALHTGHRP GSRMWIGVHG
SVYDVTDFCP MHPGGTLIIK SNAGVDCSKS FDNLAHTNNP EVSSLLTKYF VGHLTPKPDY
GSDEISALHD LWSAYLRTTV ETLVAHQFEM YEIMGASLET NSSHDPAGSN NIWLRESLPN
IIAVRTFYGY QSRLLQGGFA ALFGPKLQEL VLKLSFGVAS ANGPAADTKL PDVLGTVARA
KTSGDAATCT KEVALVGQFV CDADASLRFQ ERGVFAYAAR SVELDIALLE DLRQEACNGM
DAFDSIANSI KESSDPDVEN ARLTALSTFL LQVLERMARH LEVFYAQLAR SSVYQPQLEK
NPARTRWALV RRRIRDGSLF VLATKAELSS NLLDPAAGQN QQPYYMSRAN PNQNIDFDRV
MAQVQASLRQ DVSAMNTSHL QPHQQHPQQP LTLNAVHQAR GRVDTGDVSV VASRENADAL
RAMSSFVEKN SRAIRRLSKM PAAMPSGMNF EDIQRAALLE MAQSGVGGQS GLLSPPEMPG
DMHNHHHQEQ GLHVRKGGNG NRILPTPPSS RGSSRSPTRF NQPFAVGGKP TAEMLLAKLN
RPRGASLTRT PNASQPGSPA PFPVLRGSHS PPPSHHGSQH PVDAQTALSS MMSRLNTRPR
SGSAAMISST GGMHSPAHPA AGGGLARTRS LMSLGSSGSQ ARERGHVSRP SGGSLRALKL
RSVMEQSEER VAPTF
//
