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Database: UniProt
Entry: A0A1V6YCT1_PENNA
LinkDB: A0A1V6YCT1_PENNA
Original site: A0A1V6YCT1_PENNA 
ID   A0A1V6YCT1_PENNA        Unreviewed;       340 AA.
AC   A0A1V6YCT1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=PENNAL_c0024G00048 {ECO:0000313|EMBL:OQE85309.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE85309.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
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:OQE85309.1}.
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DR   EMBL; MOOB01000024; OQE85309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6YCT1; -.
DR   STRING; 60175.A0A1V6YCT1; -.
DR   OMA; EQFGFFQ; -.
DR   OrthoDB; 1380829at2759; -.
DR   Proteomes; UP000191691; 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:SF272; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 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:UP000191691}.
FT   DOMAIN          176..286
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   340 AA;  38534 MW;  3838DA64A400846E CRC64;
     MNPNEPPIID FAPFYANDST KEDLIHQIRR ACEQFGFFQL INHAIPTEQQ TAVLQHSSEF
     FNLPLETKEK YNQATGGFNR GYERLRPQNF EKRTKGDLKE GFYLGQDLPL DDAYVVQRRF
     GQGPNKYPSE VPDPKGFRRV MDEYHDAMIE LAVAIMQVIA HTLGLNEDFF GDFCDHPVSI
     LRLLHYPSQE ADASDLERGT KAGLGIGAHT DFGAITMLLQ DDTGGLQVWN NLSSEWVDVT
     PVPGAYVVNL GNMMMRWTNN RYLSNLHRVI NTSGKERYSI PFFFSGNPNH TIRCLPGCED
     EESARYPPIT VHEWMAGRYA DTYGTSDGKA IGDMRQEPGL
//
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