ID A0A2A9FDR7_9PSEU Unreviewed; 213 AA.
AC A0A2A9FDR7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Alkylated DNA repair protein (DNA oxidative demethylase) {ECO:0000313|EMBL:PFG49083.1};
GN ORFNames=ATK36_4206 {ECO:0000313|EMBL:PFG49083.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG49083.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG49083.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG49083.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PFG49083.1}.
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DR EMBL; PDJK01000002; PFG49083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9FDR7; -.
DR Proteomes; UP000243542; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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};
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 Methyltransferase {ECO:0000313|EMBL:PFG49083.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000243542};
KW Transferase {ECO:0000313|EMBL:PFG49083.1}.
FT DOMAIN 108..210
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 69..71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 115..117
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 201..207
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ SEQUENCE 213 AA; 23510 MW; EB736F1BC02B8F5E CRC64;
MDPSDALLPR PRREIVPGAV HVPDWLDPAQ QRALVEACRG WRGYRATRLP GGGVMSVRTV
CLGWQWLPYR YSRTREDGSP VQPFPGWLAD LGRRALADAY GRPAADYHPD VALVNYYDDA
AKMGMHQDKD ERSPDPVVSL SLGDTCVFRF GNTEHRNRPY TDIELRSGDL FVFGGAARLA
FHGVPKTLPG TADPELGLTG RLNLTLRVSG LAA
//
