ID G7UVQ0_PSEUP Unreviewed; 195 AA.
AC G7UVQ0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=2OG-Fe(II) oxygenase {ECO:0000313|EMBL:AER55167.1};
GN OrderedLocusNames=DSC_02570 {ECO:0000313|EMBL:AER55167.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55167.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER55167.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER55167.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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DR EMBL; CP003093; AER55167.1; -; Genomic_DNA.
DR AlphaFoldDB; G7UVQ0; -.
DR STRING; 1045855.DSC_02570; -.
DR KEGG; psd:DSC_02570; -.
DR eggNOG; COG3145; Bacteria.
DR HOGENOM; CLU_048788_5_2_6; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032852; ALKBH2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31573; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2; 1.
DR PANTHER; PTHR31573:SF1; DNA OXIDATIVE DEMETHYLASE ALKBH2; 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 Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT DOMAIN 93..191
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 43..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 63..65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 100
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 102
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 112
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 170
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 182
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 186
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 188
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 195 AA; 21888 MW; 293BA1A79291957F CRC64;
MDTNLDQTGL VRFADWMAAP AAEALNAALS QAISWETHRL RLFGRWVHAP RLSCWIGDPG
AVYRYSGRTF APQPWPHALL PLRQRLREEL GVDFNSVLAN LYRDGRDAMG WHSDDEPELG
PEPVIASLSL GAARRFVLRR RDDHAVKQAL VLEPGSLLVM RGASQRDWQH ALPRTARPGG
PRINLTFRRI VDAGV
//
