ID D2TQM1_CITRI Unreviewed; 289 AA.
AC D2TQM1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN Name=alkA {ECO:0000313|EMBL:CBG88953.1};
GN OrderedLocusNames=ROD_22041 {ECO:0000313|EMBL:CBG88953.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG88953.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG88953.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG88953.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000086};
CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000256|ARBA:ARBA00010817}.
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DR EMBL; FN543502; CBG88953.1; -; Genomic_DNA.
DR RefSeq; WP_012906407.1; NC_013716.1.
DR AlphaFoldDB; D2TQM1; -.
DR STRING; 637910.ROD_22041; -.
DR KEGG; cro:ROD_22041; -.
DR eggNOG; COG0122; Bacteria.
DR HOGENOM; CLU_000445_72_3_6; -.
DR OrthoDB; 9811249at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.30.310.20; DNA-3-methyladenine glycosylase AlkA, N-terminal domain; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR InterPro; IPR010316; AlkA_N.
DR InterPro; IPR037046; AlkA_N_sf.
DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR PANTHER; PTHR43003; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR PANTHER; PTHR43003:SF13; DNA-3-METHYLADENINE GLYCOSYLASE 2; 1.
DR Pfam; PF06029; AlkA_N; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM01009; AlkA_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000313|EMBL:CBG88953.1};
KW Hydrolase {ECO:0000313|EMBL:CBG88953.1}.
FT DOMAIN 1..112
FT /note="DNA-3-methyladenine glycosylase AlkA N-terminal"
FT /evidence="ECO:0000259|SMART:SM01009"
FT DOMAIN 130..276
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 289 AA; 31987 MW; A42B4F53B3314A6D CRC64;
MFTLSWQPPY DWSWMLGFLA ARAVSGIETV DEMRYTRSLA SGKQRGLITM VPDERTHTLR
VSLTPGLLPV AGICLEKIER LFDLRCEPAL ITDALGELGA ARPGLRLPGS VDTFEQGVRA
ILGQLVSVAM AAKLTAKVVQ RYGEPLAEAP GYLCFPTPEK IASADPQELK ALGMPLRRAG
ALIYLARAAL DGTFTAHAPA DIESGVRALL AFPGIGRWTA NYFALRGWQA KDIFLPDDYL
IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTDGWQPS VDGEVAGIQ
//
