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Database: UniProt
Entry: A0A1V6U456_9EURO
LinkDB: A0A1V6U456_9EURO
Original site: A0A1V6U456_9EURO 
ID   A0A1V6U456_9EURO        Unreviewed;       363 AA.
AC   A0A1V6U456;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=PENFLA_c001G04604 {ECO:0000313|EMBL:OQE32653.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE32653.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE32653.1}.
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DR   EMBL; MLQL01000001; OQE32653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6U456; -.
DR   STRING; 254877.A0A1V6U456; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000191342; 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:SF35; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G11160)-RELATED; 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:UP000191342}.
FT   DOMAIN          193..298
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   363 AA;  40441 MW;  D5A64066F5082089 CRC64;
     MQSQTDQKNI PNNFPGLPPF PDDVSTAPLL RLSSEKLLAG DPTELERLFE ASTDIGFFYL
     DLSDSDQGLS LLGDADNLFQ VGERLFELSL EEKQQYDFSG QNSYFGYKAQ GAAVVDKQGN
     LDRNEFYNVS KDDILSVSDP LPAPEVLHKT RARLASFMRG SHAIVTLILD ILNDQLALPK
     DTLSNLHRQH AVSGDQVRFV KAPPQPVDDR RTALGQHTDF GSVTVLFNRL GGLQVLPPGA
     DAEWVYVRPL PGHAIVNLGD AMVKFTNGLF RSNIHRVVAP PGLQAESTRY SLVYFARPED
     SVMLHRLEGS DLIPVMEDGQ SEEEINSKDW IIRRALGRRV DRVNDVDFEK SAGTEQLSRR
     IKV
//
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