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Database: UniProt
Entry: A0A395S8L8_FUSSP
LinkDB: A0A395S8L8_FUSSP
Original site: A0A395S8L8_FUSSP 
ID   A0A395S8L8_FUSSP        Unreviewed;       332 AA.
AC   A0A395S8L8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=2og-fe oxygenase family {ECO:0000313|EMBL:RGP68670.1};
GN   ORFNames=FSPOR_5140 {ECO:0000313|EMBL:RGP68670.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP68670.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP68670.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP68670.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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:RGP68670.1}.
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DR   EMBL; PXOF01000067; RGP68670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395S8L8; -.
DR   STRING; 5514.A0A395S8L8; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF35; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G11160)-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT   DOMAIN          176..280
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   332 AA;  37584 MW;  6E9934D93A7DD61F CRC64;
     MTISSRPAEY ANVRTADLKT ITFDKLFDKD EGELKRLIQS CEEDGFFYLD LKSAASQKFW
     VDLHNIDRTT KEWFKQPIEK KLQTPTVSLA HGFKAVGNQS GSIESKKDGF EALKIGKSEL
     DGRWALPDVV TDNLPLFDQF TAACHFISKL LLDCLSDGLE LKGDARFETH HRDDCRSKST
     LYFLHYPPGA QDPNKVGQNM HTDIGSLTIL YAPQWGLQVF SPADGAWTYV EPREGHAIVN
     VGDTLRFLSG KRFKSALHRV LPLGGIQVED RYSISYFLRA SDSTEFKDSD EDESSAKQWY
     TKKYAMYEMP HVIQKQQTTL SGGMAQELQA SF
//
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