ALKB_SALTY
ID ALKB_SALTY Reviewed; 216 AA.
AC P37462;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase AlkB;
DE EC=1.14.11.33;
DE AltName: Full=Alkylated DNA repair protein AlkB;
DE AltName: Full=DNA oxidative demethylase AlkB;
GN Name=alkB; OrderedLocusNames=STM2264;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=1904855; DOI=10.1128/jb.173.12.3663-3672.1991;
RA Hakura A., Morimoto K., Sofuni T., Nohmi T.;
RT "Cloning and characterization of the Salmonella typhimurium ada gene, which
RT encodes O6-methylguanine-DNA methyltransferase.";
RL J. Bacteriol. 173:3663-3672(1991).
CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA containing 3-
CC methylcytosine or 1-methyladenine by oxidative demethylation. Has
CC highest activity towards 3-methylcytosine. Has lower activity towards
CC alkylated DNA containing ethenoadenine, and no detectable activity
CC towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and
CC single-stranded substrates. Requires molecular oxygen, alpha-
CC ketoglutarate and iron. Provides extensive resistance to alkylating
CC agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1
CC agents) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a
CC nucleobase within DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875,
CC ChEBI:CHEBI:64428; EC=1.14.11.33;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21166.1; -; Genomic_DNA.
DR EMBL; D90221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B39433; B39433.
DR RefSeq; NP_461207.1; NC_003197.2.
DR RefSeq; WP_000884990.1; NC_003197.2.
DR AlphaFoldDB; P37462; -.
DR SMR; P37462; -.
DR STRING; 99287.STM2264; -.
DR PaxDb; P37462; -.
DR EnsemblBacteria; AAL21166; AAL21166; STM2264.
DR GeneID; 1253786; -.
DR KEGG; stm:STM2264; -.
DR PATRIC; fig|99287.12.peg.2398; -.
DR HOGENOM; CLU_039677_1_1_6; -.
DR OMA; NCGPLGW; -.
DR PhylomeDB; P37462; -.
DR BioCyc; SENT99287:STM2264-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IBA:GO_Central.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; IBA:GO_Central.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0070989; P:oxidative demethylation; ISS:UniProtKB.
DR GO; GO:0035513; P:oxidative RNA demethylation; IBA:GO_Central.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IBA:GO_Central.
DR GO; GO:0042245; P:RNA repair; ISS:UniProtKB.
DR Gene3D; 2.60.120.590; -; 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; PTHR16557; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase; DNA damage; DNA repair; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..216
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB"
FT /id="PRO_0000066666"
FT DOMAIN 113..213
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120..122
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 204..210
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="A -> R (in Ref. 2; D90221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 23787 MW; 8F320C7B9CABFAB6 CRC64;
MLDLFADEAP WQEPLAPGAV VLRRFAFRAA QSLLDDIGFV ASQSPFRQMV TPGGYTMSVA
MTNCGALGWT TDRHGYCYAV RDPLTDKPWP ALPLSFASVC RQAAIAAGYA SFQPDACLIN
RYAPGAKLSL HQDKDEPDLR APIVSVSLGV PAVFQFGGLR RSDPIQRILL EHGDIVVWGG
ESRLFYHGIQ PLKAGFHPMT GEFRYNLTFR QAAEKE
