ID J7QPC1_METSZ Unreviewed; 207 AA.
AC J7QPC1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=2OG-Fe(II) oxygenase {ECO:0000313|EMBL:CCJ05760.1};
GN OrderedLocusNames=BN69_0309 {ECO:0000313|EMBL:CCJ05760.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ05760.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ05760.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ05760.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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};
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DR EMBL; HE956757; CCJ05760.1; -; Genomic_DNA.
DR RefSeq; WP_014889794.1; NC_018485.1.
DR AlphaFoldDB; J7QPC1; -.
DR STRING; 187303.BN69_0309; -.
DR KEGG; msc:BN69_0309; -.
DR PATRIC; fig|187303.17.peg.345; -.
DR eggNOG; COG3145; Bacteria.
DR HOGENOM; CLU_039677_1_0_5; -.
DR OrthoDB; 9796932at2; -.
DR Proteomes; UP000005263; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 101..207
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 68..70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 108..110
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 198..204
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ SEQUENCE 207 AA; 22627 MW; CEC15D54BF3EA5E0 CRC64;
MPEIAPGAFH YPSFLDAAAQ RALAEEIAQV IAAAPLYVST MPKTGAPMSV RMTNCGALGW
VSDKERGYRY EPRHPQTGRP WPAMPQKLLE LWSELAHYHK PPEACLVNVY DATARMGLHQ
DKDESDFAAP ILSLSFGADC RFRLGGTRRS DSAMALALSS GDALVLSGPA RMRYHGVDRI
LPTLNPLLPD ALAAFGVRVN LTLRRVT
//
