ID   A0A318ZHQ5_9EURO        Unreviewed;       362 AA.
AC   A0A318ZHQ5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:PYH44103.1};
GN   ORFNames=BP01DRAFT_374960 {ECO:0000313|EMBL:PYH44103.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH44103.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH44103.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH44103.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-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; KZ821239; PYH44103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318ZHQ5; -.
DR   STRING; 1450539.A0A318ZHQ5; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000248349; 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:UP000248349}.
FT   DOMAIN          187..305
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   362 AA;  39537 MW;  DF6FCA4A16DF781F CRC64;
     MPTDKYFAQA PPFPTSPDFP IVSLPTISLA KLKAHDPTES TQLFRASREW GFFMLDLRAD
     EQGASLLHQA EKMFDLDAEL FSLDQATLDE YAYDAPRDLT GYKKAGLLRT DTGGYDHMHL
     YSINQDDMLG NRAARTNAPP IEAHRGDLQA FIRESSAALA VILATLDREL GLEAGTLAKL
     SPLDEESETS VRLLWSPPAP AVATTPPPAA ETQRVITLGG HTDIGTLTLL FHVLGGLQIL
     PAGVENTAQQ WRYVRPVPGC ALVNLGDTLV EWTGELLRSS LHRVVTAPGE QATVARRSVA
     YLVRPSKKAS MRRLQGGKIP AVAEGEEEET RPVNEWAAWR SKQIMLGTLK PQTRGGARAV
     VV
//