ID A0A179A0I8_9EURO Unreviewed; 1576 AA.
AC A0A179A0I8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN ORFNames=AYL99_00717 {ECO:0000313|EMBL:OAP64745.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP64745.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP64745.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP64745.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAP64745.1}.
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DR EMBL; LVYI01000001; OAP64745.1; -; Genomic_DNA.
DR RefSeq; XP_018698112.1; XM_018832233.1.
DR STRING; 1367422.A0A179A0I8; -.
DR GeneID; 30004887; -.
DR OrthoDB; 2723058at2759; -.
DR Proteomes; UP000078343; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-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; 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; PS00191; CYTOCHROME_B5_1; 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 Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078343}.
FT DOMAIN 842..909
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1195..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 174587 MW; A33DC81E6A49A5E2 CRC64;
MPAVVARGKM RESILALPLV YGTEDVIPDQ ALWAAVVCLG ILASVYRYEE RNDGHEGISI
TAPPGTFRNL SGEADDEEEE TKGIPRNIAI PLRQICTRMG RILPHLTQYD VSVYNYKLRD
PTSINPYVAR CENMDLRWPV FNDRGEAMFL LCMAETHGCF TQGVEVITRC QERVMLKDKE
GLLRELIKLK AIVDRFVHVF QKISVNPNSG ENFANPVEWG QRYAKFSAPL SKRVPALSGL
ALPVFLLMDA FIGRSKYDSF LGREALHLRA WLPMNIRAFI AAIEYHYQVP AFVKKSGDPR
LMGVMEGILE AYLSERGWFG THRYKVYGFL EVVAKTGRSE TNGNAGSSDN VGRPWEEVHK
TLSESMRERL EPFRGKVTLQ PHELRGSFEE CRFKARILSR SFVDTDPLRS TAMVTFGLEG
TGITFQPGDR LAIMPVNSWT EMGKITAALG LDELLHKALP LSQNSDWIRF ARHLKSVSRT
GGEPSLTVHD ILRRGHLAPL TKEMVMAFHM ALRASSSSVL KVLGSEMWPV EGSIGDLLQV
ALAEVPSTIW DRAFNLSDLS WLPKLIPIEV PRTYSISNYS NELLPSTVDL TVARTESPLA
PILQSTNPGN RRCGVSSGCL NPDPSSSGEM FDDEEYLIGI SRPINFQLPS TMTGPIAMFA
GGSGIAPFRG FWQARAQTCV GRNILFLGVQ SRERFSYEHE LREYVQNGQL ELHTAFSRDR
NGLIYDPVSR DLVEKQMSPR YLDATIIEQG RTVCDLVISK SQGGLGGHLY ICGSVAMYET
IITGIRQAIY QNWASTKESA DSLLAKAFAE RRFMLDIFMT PRPISYATPR IPLSKLALNT
GHRKGSRMYI GVHGGVYDIT DFLPIHPGGT LIAQASAGLD ASKTFDDVAH TTNPEVMSLL
SKYFIGHLAA KPDFRSTEIS GIYDLWYEYL RSCVEALTTL HFEVNYIQQD ARTWFQGDLF
NMGGVRKFYQ FQSRLMQNGF STLFGAKLQE LHLKLTFALV NSGTPETRVP DVIGVITRAQ
ASAPAATAAK EIAQIGSFVC NNQQAQFQEN GILQYARAVT ELDVRFLEEI REDVCMGMDA
FDVIECIESG TDKHKLVSLS TYLLSVLERV AERLGTFYSR LSRESIYHPE LEKNPARTRW
NVLKRKIHDG SFFILAQASA FSGASHATKP FRSTRYADQD IVFAQVVSQA QQAIDAGQPH
VGRDSNRSPN TVSTRPVRLA DSHTARAAHR LDTPSSYEIH ESRNALQSIS TFMDSNMHSI
KRLSQLPSDL SFANIVAAYG TNSKRLPSVP SLEEHDEGRP GPAEHQRGGS QSSYISNWPL
PRTTTVKPGS RTLNNPLADH KPRLVRRPTN GSISSVNGLP HNPAPSAQSH ASFIGRPVLR
APDAPQNAAR PPPRPFLSNL TSRSRSQSRS RSDSENSLRH DGSVVTSART LEGPVTNLHT
KLMRRQLSNA SAQNNSVLEA EATSSGALAQ SQFWQSPKTS TMPILPQGAP PEGGNERLLQ
QRQQQNEMIM MGEARGTLAA PGRIPPFSGL RVLKLATATE MGTRQAAGRE GSGPPDLSPG
NAMGSIRATP LPLNVR
//
