ID Q121P1_POLSJ Unreviewed; 217 AA.
AC Q121P1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=DNA-N1-methyladenine dioxygenase {ECO:0000313|EMBL:ABE46751.1};
DE EC=1.14.11.- {ECO:0000313|EMBL:ABE46751.1};
GN OrderedLocusNames=Bpro_4875 {ECO:0000313|EMBL:ABE46751.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46751.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE46751.1; -; Genomic_DNA.
DR RefSeq; WP_011485736.1; NC_007948.1.
DR AlphaFoldDB; Q121P1; -.
DR STRING; 296591.Bpro_4875; -.
DR KEGG; pol:Bpro_4875; -.
DR eggNOG; COG3145; Bacteria.
DR HOGENOM; CLU_039677_1_1_4; -.
DR OrthoDB; 9796932at2; -.
DR Proteomes; UP000001983; 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, ECO:0000313|EMBL:ABE46751.1};
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 ECO:0000313|EMBL:ABE46751.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 117..217
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 124..126
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 208..214
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ SEQUENCE 217 AA; 23297 MW; FAF0CA088D95853C CRC64;
MTQDLFEEEP LAYVAPQVMA PGAVLLRGFA CDVEQALMHA VEQVTAAAPL RHLVTPGGYT
MSVAMSNCGA LGWVSDRTGY RYTGTDPLSG QPWPPMPDCF ARLARRAAAE AGFGGFRPDA
CLVNCYEPGA RLSLHQDKDE GDMSAPIVSV SLGLPAVFLF GTTRRKDRPA RYRLVHGDVA
VWGGPSRLAY HGVAPLAAGE HALLGRQRIN LTFRCAA
//
