ALKB_CAUVN
ID ALKB_CAUVN Reviewed; 220 AA.
AC B8GWW6; O05725;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=CCNA_00009;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9150207; DOI=10.1128/jb.179.10.3139-3145.1997;
RA Colombi D., Gomes S.L.;
RT "An alkB gene homolog is differentially transcribed during the Caulobacter
RT crescentus cell cycle.";
RL J. Bacteriol. 179:3139-3145(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45302.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ACL93476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U73681; AAC45302.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP001340; ACL93476.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_002515384.1; NC_011916.1.
DR AlphaFoldDB; B8GWW6; -.
DR SMR; B8GWW6; -.
DR EnsemblBacteria; ACL93476; ACL93476; CCNA_00009.
DR GeneID; 7333150; -.
DR KEGG; ccs:CCNA_00009; -.
DR PATRIC; fig|565050.3.peg.9; -.
DR HOGENOM; CLU_039677_1_0_5; -.
DR OMA; NCGPLGW; -.
DR OrthoDB; 1391445at2; -.
DR PhylomeDB; B8GWW6; -.
DR Proteomes; UP000001364; 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_0000378276"
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"
FT CONFLICT 127..128
FT /note="RD -> AT (in Ref. 1; AAC45302)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="V -> L (in Ref. 1; AAC45302)"
FT /evidence="ECO:0000305"
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
