ID   A0A0F7RXW8_9BASI        Unreviewed;       793 AA.
AC   A0A0F7RXW8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Dioxygenase Ssp1 {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   Name=SSCI31680.1 {ECO:0000313|EMBL:CDR99934.1};
OS   Sporisorium scitamineum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=49012 {ECO:0000313|EMBL:CDR99934.1, ECO:0000313|Proteomes:UP000242770};
RN   [1] {ECO:0000313|Proteomes:UP000242770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Berkman P.J.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCFA01001743; CDR99934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7RXW8; -.
DR   STRING; 49012.A0A0F7RXW8; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000242770; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964}.
FT   BINDING         387
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   NON_TER         793
FT                   /evidence="ECO:0000313|EMBL:CDR99934.1"
SQ   SEQUENCE   793 AA;  88302 MW;  636ED5FDC4EFAC50 CRC64;
     MTTEKMEQVK TFVQDKVNQT TDAAGLSATE TRKKAQGVLK KAQQKTSAAT TTSIESLQML
     LDQLNRSRIV NDVKLLGQAP NLLVRGLTGG GLDDRKLLLE QLITLLASMP VSSNISRTLS
     DALISIIWGD LPHPAVSFMG HEHRFRRPDG SDNNVMNPKL GASNQPYSRN VQRLHPQPVN
     LPDPGTVYDL LLARDGLEPH PTGISSLLFN FANIIIHDIF STTRVPGAHS AYNEHSSYLD
     LQVVYGANLE EQKRVRTGTL GLLKPDVIGD WRLAMMPPAT AALGVLFSRN HNYIAKRLYE
     VNENKRFDDL EGEALDEELF GIARLVNCGH FLHIILRDYI PVILNTNDSE WYVDPLNVIK
     NIGGPSSLER GIGNSVAAEF SILYRWHAAV SQNDEKWMNE FLEARFPGKS PEEVTPMEFV
     GAAASLKHDF LDTDPGQWNL HNWERDAQGK FDDSVIAQVV KDAVSDVAAA FRARGHPSWF
     RPIEILGMIT ARKDWALCTM NEFRHFLGLK TYNSFSEWNP DPKISKAAEM LYGDIDNLEL
     YPGLMAEEAK PSIPGSGLCP GYTISRGILS DAAALTRGDR FYTNDFSTSN LTSAGYEYCT
     TPQPGGHGLM GKLIMANLPG QFPYNSIYAL FPFRVPEKTV DMLKEKRVLE QYDTSYPVPA
     RCWYAIESYS ASKDILEDSR YFVALPPMSY DESLMTSALH SIPRFHDEVS DFFSVNTGLT
     MKDRSIPYAP SSRERIVDLI EVVNAVSAQF TAKLFALPTP GSHGLHLGMS PEELSTTLTK
     PLAYAMYGSF DFQ
//