ID UNG_ENT38 Reviewed; 229 AA.
AC A4WDE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 29-MAY-2013, entry version 43.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=Ent638_3065;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Enterobacter sp. 638.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC a result of misincorporation of dUMP residues by DNA polymerase or
CC due to deamination of cytosine (By similarity).
CC -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC double-stranded DNA and polynucleotides, releasing free uracil.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000653; ABP61729.1; -; Genomic_DNA.
DR RefSeq; YP_001177780.1; NC_009436.1.
DR ProteinModelPortal; A4WDE9; -.
DR SMR; A4WDE9; 1-229.
DR STRING; 399742.Ent638_3065; -.
DR EnsemblBacteria; ABP61729; ABP61729; Ent638_3065.
DR GeneID; 5112600; -.
DR KEGG; ent:Ent638_3065; -.
DR PATRIC; 20415811; VBIEntSp101211_3217.
DR eggNOG; COG0692; -.
DR HOGENOM; HOG000229528; -.
DR KO; K03648; -.
DR OMA; AGKEIYP; -.
DR ProtClustDB; PRK05254; -.
DR BioCyc; ESP399742:GJ0E-3129-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1; -.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR002043; Ura_DNA_glycsylse.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; UDNA_glycsylseSF; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase;
KW Hydrolase.
FT CHAIN 1 229 Uracil-DNA glycosylase.
FT /FTId=PRO_1000058128.
FT ACT_SITE 64 64 Proton acceptor (By similarity).
SQ SEQUENCE 229 AA; 25636 MW; 50BAE779E040C688 CRC64;
MTTSLTWHDV LADEKQQPYF VNTLNTVAAE RQSGQTIYPP QKDVFNAFRY TELNNVKVVI
LGQDPYHGPG QAHGLAFSVR PGIATPPSLL NMYKELEGSL PGFVRPAHGY LESWAHQGVL
LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINEHREGVV FLLWGAHAQK KGAIIDPKRH
HVLKAPHPSP LSAHRGFFGC NHFVLTNEWL EKRGEKPIDW MPVLPMESE
//
