GenomeNet

Database: UniProt/SWISS-PROT
Entry: UNG_PSEAE
LinkDB: UNG_PSEAE
Original site: UNG_PSEAE 
ID   UNG_PSEAE               Reviewed;         231 AA.
AC   Q9I5H9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=PA0750;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00148};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG04139.1; -; Genomic_DNA.
DR   PIR; C83551; C83551.
DR   RefSeq; NP_249441.1; NC_002516.2.
DR   RefSeq; WP_003106436.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; Q9I5H9; -.
DR   SMR; Q9I5H9; -.
DR   STRING; 208964.PA0750; -.
DR   PaxDb; 208964-PA0750; -.
DR   DNASU; 881872; -.
DR   GeneID; 77222682; -.
DR   GeneID; 881872; -.
DR   KEGG; pae:PA0750; -.
DR   PATRIC; fig|208964.12.peg.779; -.
DR   PseudoCAP; PA0750; -.
DR   HOGENOM; CLU_032162_3_1_6; -.
DR   InParanoid; Q9I5H9; -.
DR   OrthoDB; 9804372at2; -.
DR   PhylomeDB; Q9I5H9; -.
DR   BioCyc; PAER208964:G1FZ6-763-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR002043; UDG_fam1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   NCBIfam; TIGR00628; ung; 1.
DR   PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SMART; SM00987; UreE_C; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..231
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176127"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   231 AA;  26010 MW;  53F2B36FF0D883A7 CRC64;
     MTDNDDRIKL EASWKEALRE EFDKPYMKQL GEFLRQEKAA GKVIFPPGPL IFNALNTTPL
     ENVKVVIIGQ DPYHGPGQAH GLCFSVQPGV PTPPSLQNIY KELNRDLNIP IPNNGYLQRW
     AEQGVLLLNT SLTVEQAKAG SHANAGWQPF TDRVIEVVNE RCERLVFLLW GSHAQSKQKL
     IDPQRHLILK SAHPSPLSAY RGFLGNGHFS RTNKFLEQNG KTPIDWSLPD L
//
DBGET integrated database retrieval system