ID A0A0A2K2S3_PENEN Unreviewed; 360 AA.
AC A0A0A2K2S3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Oxoglutarate/iron-dependent dioxygenase {ECO:0000313|EMBL:KGO61958.1};
GN ORFNames=PEX2_014540 {ECO:0000313|EMBL:KGO61958.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61958.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61958.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61958.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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:KGO61958.1}.
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DR EMBL; JQFZ01000027; KGO61958.1; -; Genomic_DNA.
DR RefSeq; XP_016602624.1; XM_016738730.1.
DR AlphaFoldDB; A0A0A2K2S3; -.
DR STRING; 27334.A0A0A2K2S3; -.
DR GeneID; 27674149; -.
DR HOGENOM; CLU_029471_0_0_1; -.
DR OrthoDB; 47845at2759; -.
DR PhylomeDB; A0A0A2K2S3; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR004574; Alkb.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:KGO61958.1};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 221..348
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ SEQUENCE 360 AA; 40107 MW; CDB0BE2C3C55619B CRC64;
MAQIKGLSAY DRPPDPVRLC YKKYSKIALS KVDNDPGILD LQRIDPDQLP DGVTITQYMS
SQDLRLAFDD FIRGSHAATD EHAPLTEDIP VFAHKSISGL LMIPALFPPT IQIELLSRLF
HRDLPNPEHQ TNLHLHYDVT YPEESEETHM PKSFFADDPT RAFQPKDPHV HKPLTVQNLL
EKKLRWVTLG GQYDWTAKVY PSGTPPEFPP DIAKVLRAAF PATSAQAAIL NLYSAGDTLS
VHRDVSEECD VGLISVSFGC DGLFLASHDD GNGCEIIRLR SGDTVYMNGK SRFAWHGVPK
ILPSTCPKWL ADWPSSGESA PGMPPGPYEM WKGWMSSKRV NLNVRQMTAT QACEESVDQA
//
