ID A0A136IL58_9PEZI Unreviewed; 364 AA.
AC A0A136IL58;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Naringenin,2-oxoglutarate 3-dioxygenase {ECO:0000313|EMBL:KXJ85711.1};
GN ORFNames=Micbo1qcDRAFT_127540 {ECO:0000313|EMBL:KXJ85711.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ85711.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) 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; KQ964276; KXJ85711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IL58; -.
DR STRING; 196109.A0A136IL58; -.
DR InParanoid; A0A136IL58; -.
DR OrthoDB; 2908779at2759; -.
DR Proteomes; UP000070501; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF62; 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 Dioxygenase {ECO:0000313|EMBL:KXJ85711.1};
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:UP000070501}.
FT DOMAIN 214..321
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 123..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 41455 MW; B9C1A79EE2A7D5DD CRC64;
MTETAAPAAD SYKLELMSAY GPVFRDVLRT PARDCTSAEV PIIDLSDISG TEAQRRALAE
TIRDAAENTG FFYIKNHGIP KDTIDATFKQ AQAFFTQPES LKERASADNS KFFNGWSRKH
ASKISPTEKR DNREGFSFRY DPRHDPETKD PAAVPEDVKQ WLKVEEFVWE GTSHLPDFRK
DLVAYWQECI TLARRMIKLF AMALDAPEDY FDDLVTYPGS DSVFNYYPKN EGSTEGIVDI
GLGAHTDLQC FTFLWQDSVG GLQVLTKEGQ WVKVPPLADT FVVNIGDFMN RLSNDRFKST
VHRVYNHAPV DRYSMPFFFG LNHNEKCAVL PSCTSEKNPA KYEPISCGEW CRLRFEKTFD
VPKQ
//
