ID   A0A5N7BHL5_9EURO        Unreviewed;       327 AA.
AC   A0A5N7BHL5;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=BDV26DRAFT_255702 {ECO:0000313|EMBL:KAE8381283.1};
OS   Aspergillus bertholletiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1226010 {ECO:0000313|EMBL:KAE8381283.1, ECO:0000313|Proteomes:UP000326198};
RN   [1] {ECO:0000313|EMBL:KAE8381283.1, ECO:0000313|Proteomes:UP000326198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29228 {ECO:0000313|EMBL:KAE8381283.1,
RC   ECO:0000313|Proteomes:UP000326198};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; ML736172; KAE8381283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N7BHL5; -.
DR   Proteomes; UP000326198; 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   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
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:SF27; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 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:UP000326198}.
FT   DOMAIN          167..283
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   327 AA;  37424 MW;  62FC41851FCDF356 CRC64;
     MPTKYIDRSI PRISLADFDQ RIDEITADLV HAAENVGFFT IVDHGISTDE IETMFATAER
     FFNLPDNVKA TVPWNPNNVG WEKKAQVRPS TGQPDTKESY QLQFGENMTK MWLDDVHLPG
     FRTTSLTFMH RVQGVSERLM RCFARGLGFP DDYFIKCHDV SRPNEQTTMR LLHYFALPRE
     PDGNTYHRAG AHADWDFLTL LFQKDGQSGL EICPGREAVT EFGIGDEWTR VEACTGEIVC
     NIGDLLMSWS DDRFKSTFHR VKAPSEPEDY YGDRYSIAYF NQPCKDALIQ GPKKKYPMLT
     GEQFNTQAMQ RNFAALQEKL KSMKASA
//