ID A0A423X8R4_9PEZI Unreviewed; 336 AA.
AC A0A423X8R4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=VMCG_00594 {ECO:0000313|EMBL:ROW12213.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW12213.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW12213.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW12213.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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}.
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:ROW12213.1}.
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DR EMBL; LKEA01000001; ROW12213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X8R4; -.
DR STRING; 356882.A0A423X8R4; -.
DR Proteomes; UP000283895; 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:UP000283895}.
FT DOMAIN 188..298
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 336 AA; 37067 MW; 94360B505A5CBAB6 CRC64;
MEKAAVDEQG LMIPLIDLSR FLNGDAAQRK ETADAILNGF QNAGFIYLKG LPITPSTRKH
VFDTSAKFFN GLSKDEKMAL GWTTPEANRG YSAPGREKVT QLTDITEVAK LKAGNPDIKE
SFEIGRDSDP AWPNQWPVEE PGTAVDGFKK TMLDFFDQCK TIHVEVMRAV AVGMGLDEDY
FDGFTDAGDN TLRLLHYPAV KSEVFKINPG QVRAGSHSDY GSITLLFQDS AGGLQVRSPN
GTFVDAAPIE DTCVVNAGDL LARWSNETIK STVHRVVEPR RKADEHPARY SIAYFCNPNF
KSHIEAIPGT YSTEADKKYE GINSGQYLVQ RLAATY
//