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Database: UniProt
Entry: A0A433D5W4_9FUNG
LinkDB: A0A433D5W4_9FUNG
Original site: A0A433D5W4_9FUNG 
ID   A0A433D5W4_9FUNG        Unreviewed;       360 AA.
AC   A0A433D5W4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=BC936DRAFT_147198 {ECO:0000313|EMBL:RUP46221.1};
OS   Jimgerdemannia flammicorona.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Endogonomycetes; Endogonales; Endogonaceae; Jimgerdemannia.
OX   NCBI_TaxID=994334 {ECO:0000313|EMBL:RUP46221.1, ECO:0000313|Proteomes:UP000268093};
RN   [1] {ECO:0000313|EMBL:RUP46221.1, ECO:0000313|Proteomes:UP000268093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMNB39 {ECO:0000313|EMBL:RUP46221.1,
RC   ECO:0000313|Proteomes:UP000268093};
RX   PubMed=30485448;
RA   Chang Y., Desiro A., Na H., Sandor L., Lipzen A., Clum A., Barry K.,
RA   Grigoriev I.V., Martin F.M., Stajich J.E., Smith M.E., Bonito G.,
RA   Spatafora J.W.;
RT   "Phylogenomics of Endogonaceae and evolution of mycorrhizas within
RT   Mucoromycota.";
RL   New Phytol. 0:0-0(2018).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {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:RUP46221.1}.
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DR   EMBL; RBNI01006138; RUP46220.1; -; Genomic_DNA.
DR   EMBL; RBNI01006138; RUP46221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433D5W4; -.
DR   Proteomes; UP000268093; 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; IPR026992; DIOX_N.
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:SF34; IRON/ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
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:UP000268093}.
FT   DOMAIN          186..289
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   360 AA;  40719 MW;  F369A237C32AE832 CRC64;
     MTIDSNAREP LSLPILDYSL LQSNDPDAQS GFISELRSAL LDSGFFYLTN HGIPLQELDS
     LFDVLKRFFT LPLEIKEEIA MEKSPHFRGY TRLGEEITDF KADNREELDY APERASLRPL
     PATSPIYQNL HGPNQWPDEA LVPGFRDGVL RFQARANDVA LAIMSAIARS LELSPRFFEE
     AFGEKSHNRL KLVRYPAAGE TGVQGHGLGV GPHKDGGYLT MLFQDAVGGL QIQTRMGSWL
     SATPIRGTAV INIGQQLERL TKRVYVSTTH RVLTHSHSER FSVPFFLCPH LDAVIPEIDV
     PAWILDRARE HHEWTSDVPT RELLQREVYG ENAWRGITRS HVGVLCKHYP EEAKRRGYVH
//
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