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Database: UniProt
Entry: A0A2H3FW53_FUSOX
LinkDB: A0A2H3FW53_FUSOX
Original site: A0A2H3FW53_FUSOX 
ID   A0A2H3FW53_FUSOX        Unreviewed;      1686 AA.
AC   A0A2H3FW53;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=indoleamine 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00034333};
DE            EC=1.13.11.52 {ECO:0000256|ARBA:ARBA00034333};
GN   ORFNames=AU210_014919 {ECO:0000313|EMBL:PCD23397.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD23397.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD23397.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD23397.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA   Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD23397.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD23397.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT   multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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:PCD23397.1}.
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DR   EMBL; MABQ02000011; PCD23397.1; -; Genomic_DNA.
DR   STRING; 327505.A0A2H3FW53; -.
DR   OrthoDB; 2723058at2759; -.
DR   Proteomes; UP000219602; Chromosome 13.
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:UP000219602}.
FT   DOMAIN          984..1065
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1456..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1554..1597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1637..1659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1558..1597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1637..1651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1686 AA;  185947 MW;  528B9EAF07EF261D CRC64;
     MSISSCPVSG SAGGECPVSG SSRSAQTRRG CAFSAATQPG DLHAAFDIPR GIDTEEWLRA
     RERKTINELL YADYPSREEV DSVKSQQELD AMNASDHDLL AIALGAPARQ VLQRAQEIGP
     QTGWRDGYLS VEHGFCPPDY EEPIAALARS PGRIWSDLCE RMPGCCARGR VREAVAALPL
     VEGTEENIPD EALWGAVVAL GMLCSIYRFE DKHDGKDGLA ITDGATTKPQ CPMGDDLCEE
     LEGIPLCIAL PYYQVSRRMG RTLPHLSFPD QASYNLKIRD VKSNTPYLAR FDNTDLRWPM
     FGERAEVAFL KGCADTSASF QHGPDAIAAC QEHVMTGNIE GLLHEMIRLK EILERMPNAF
     HSISPNPNAG DNYVSADKWV RWGLFSSPLS KRVPAASGLQ FPPYLVMDAF LGRKTHASFL
     GVEALHLRAW LPSNHRAFIA AIQYHYSIPE FVQRSGDPRL MGVLEGIVEA YAGERGFMGV
     HRYKVFGILE VAAKTGRTAT NGLSGAADAT RPWEETHRQF SDAMKERLEP FRGKLAMEPH
     SMRGTFEECR YMAKIASCSS IDQDASRSTA MITLDIRDTG ITFAPGDRVA VMPLNSWEEC
     AKMVAALGLD QHLREPVDTT GTWSRFEHHL STVTRTAHRQ LTVIDILRRG HLAPITKELT
     VKVHELLHAS SNTVLQVLAT EEWPVRGSLG DLLQKAVLDT PSHIWNRAFN LEDLSWLSEL
     VQLEVPRTYS ISSHSDELLP STVDLTISRA EYELSPIFSQ GQTVTRAGVA SGFFNPRPLS
     AENSLLYEVL IGVSRPVAFQ LPIDKMVPCA FFAGGSGIAP FRSFWQHRLA TSGLSGGRNL
     LYLGVQSREK FCYEAELREL VNMGFMEVHL AFSRDRHGLA YDGVARDLVE KPTPPRYIDS
     LIVEQGNMIC DMVMSKKQGG LGGHLYVCGS VSVFDSVMSG IRKAMYNYRT ATMETVDLII
     NKAFAERRFM LDVFMSPKAL PCNLPTISLS SLALHTGHRQ ESRMWIAVHG SVYDITDFCP
     MHPGGTLIIK SNAGVDCTKS FDNLAHTNNP EVSSLLTRYF IGHLAPKPDY RDSDVSTLHD
     LWASYLRVTV ETLVAHQFEM NDIMGESIDS PSAYDPNGIS NIWLREGLPN TIAIRTFYDY
     QNRLLQGGFS ALFGSKLEEL VLRLSFNFAN SGGPGVASKL PDILGTIARA KSGSDAVRSA
     KEISALGDFV CDPSSELRFQ ERGVLDFTAK CVQLDIELLE DLRQEACNGM DAFESIATVL
     DSFDGSNSDS TPVAALSSFL LQTLERMAHR LAMFYTQLAR LSVYQPELEH NPARTRWAFV
     RRCIRDGTFF VMTRSRNDGQ SMDGQSESYY INAKSLEKTT FDNILSQIKH VITSSTAESQ
     TTIVQPSTVN DVHHERATTL AKDGSVASSA SRLNVGAVES MGSFMKKNEK AIRRLSSMPS
     QLQLDDLQRA IALNDKPSPQ ASESTDASKE NPGRFKPLEL KTSLKIDPNA LLACKDQMLT
     ARMRIMAGYE MMSCSASRLS APAKCTSISS ITFEEADELV VTNPQPLMEC LKSIPDDESV
     PSSASCTTAQ SRRSSFSGSS VTGSIAESVI QTPPSRPYET SMALKLKLEG LNRRSRGESV
     SSRQSFISAS SAMDLRRNRS LSSTRNASKR MSIDPGHTRE QSAGRLLAFK LGALAGERRS
     FIPPTW
//
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