ID W3XH60_PESFW Unreviewed; 335 AA.
AC W3XH60;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=PFICI_02591 {ECO:0000313|EMBL:ETS84566.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS84566.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI912110; ETS84566.1; -; Genomic_DNA.
DR RefSeq; XP_007829363.1; XM_007831172.1.
DR AlphaFoldDB; W3XH60; -.
DR GeneID; 19267604; -.
DR KEGG; pfy:PFICI_02591; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_1_1; -.
DR InParanoid; W3XH60; -.
DR OMA; VDNIWVA; -.
DR OrthoDB; 1332763at2759; -.
DR Proteomes; UP000030651; 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: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:UP000030651}.
FT DOMAIN 175..296
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 335 AA; 37258 MW; 111080617FDFE854 CRC64;
MAAQVDADTV NMALFYGTPE EKQSFCDTLV TLLKQKGCIK IQNHRIPADM IHKCFAMTRQ
FFNLSLEDKM KAKHPPQANP NRGYSYVGQE NIAAISGFGK GDGYGPGTTK DVKETYDMGA
ANDPLVDNVW VPEECLPGFR SFMESFYDEA FKAELDIISA ISLALGVSEE HMRTLHNRAE
NEFRLLHYPA IPASTLADGT STRIAEHTDF GTITLLFQDS TGGLQVENQD QYGTFHDVIS
SAPTDIIINI GDSLQRLTND TFRAACHRVT YPPSVQAGDG DKVIPERYSI AYFGKPNRAA
SLLPLKEFVS EARPCKYEDV TAWDFNNKRI VSLFS
//