ALKB_CAUVC
ID ALKB_CAUVC Reviewed; 220 AA.
AC P0CAT7; O05725;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase AlkB homolog;
DE EC=1.14.11.33;
DE AltName: Full=DNA oxidative demethylase AlkB;
GN Name=alkB; OrderedLocusNames=CC_0009;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK21997.1; -; Genomic_DNA.
DR PIR; A87250; A87250.
DR RefSeq; NP_418829.1; NC_002696.2.
DR AlphaFoldDB; P0CAT7; -.
DR SMR; P0CAT7; -.
DR STRING; 190650.CC_0009; -.
DR EnsemblBacteria; AAK21997; AAK21997; CC_0009.
DR KEGG; ccr:CC_0009; -.
DR PATRIC; fig|190650.5.peg.9; -.
DR eggNOG; COG3145; Bacteria.
DR HOGENOM; CLU_039677_1_0_5; -.
DR OMA; NCGPLGW; -.
DR BioCyc; CAULO:CC0009-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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..220
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB
FT homolog"
FT /id="PRO_0000066667"
FT DOMAIN 117..218
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124..126
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 209..215
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 23764 MW; 14DFA72565DCBD2F CRC64;
MAVVRRAVAA RGLQMIAKPL TVVPGFDVWP GLLDISAQRA LVEAVLAGAE QAPFSNYRTA
YGKPMSVAMT ALGSLGWTSD ARGYRYVDRH PETGRPWPDM PPALLDLWTV LGDPETPPDS
CLVNLYRDGA RMGLHQDRDE ADPRFPVLSI SLGDTAVFRI GGVNRKDPTR SLRLASGDVC
RLLGPARLAF HGVDRILPGS SSLVPGGGRI NLTLRRARTA
