ID K8A2E9_9ENTR Unreviewed; 282 AA.
AC K8A2E9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN ORFNames=BN137_2807 {ECO:0000313|EMBL:CCJ73430.1};
OS Cronobacter condimenti 1330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1073999 {ECO:0000313|EMBL:CCJ73430.1, ECO:0000313|Proteomes:UP000009340};
RN [1] {ECO:0000313|EMBL:CCJ73430.1, ECO:0000313|Proteomes:UP000009340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330 {ECO:0000313|EMBL:CCJ73430.1,
RC ECO:0000313|Proteomes:UP000009340};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCJ73430.1}.
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DR EMBL; CAKW01000102; CCJ73430.1; -; Genomic_DNA.
DR RefSeq; WP_007676025.1; NZ_CP012264.1.
DR AlphaFoldDB; K8A2E9; -.
DR STRING; 1073999.AFK62_12685; -.
DR KEGG; ccon:AFK62_12685; -.
DR PATRIC; fig|1073999.7.peg.2661; -.
DR eggNOG; COG0122; Bacteria.
DR OrthoDB; 9811249at2; -.
DR Proteomes; UP000009340; Unassembled WGS sequence.
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:CCJ73430.1};
KW Hydrolase {ECO:0000313|EMBL:CCJ73430.1}.
FT DOMAIN 1..112
FT /note="DNA-3-methyladenine glycosylase AlkA N-terminal"
FT /evidence="ECO:0000259|SMART:SM01009"
FT DOMAIN 122..275
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 282 AA; 31469 MW; CDB60B30A3B68E2A CRC64;
MFTLRYQPPY DWPWMLRFLA DRAVVGIEEV SDSQYRRTLS VGSHHGWLSV TPHPESATLT
LTLSDGLLPV AEEVQARVAR LFDLHFDPAP MLETLGPLAA ARPGLRLPGS VDVFEQGVRA
ILGQLVSVAM AAKLTGKVVQ AVGTPLEDGS GWRFPTPEAM ARTEPQRLKA LGMPLMRAGA
LIQLAHEHLA GRFPLRCPQD VAAGVKALTQ LPGIGPWTAN YFAMRGWQAP DIFLPDDYLI
KQRFAPMTPA QIRRFAERWQ PWRTYALLHV WYASDWQTPV SE
//
