ID   UDGB_PYRAE              Reviewed;         226 AA.
AC   Q8ZXE0;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Type-5 uracil-DNA glycosylase {ECO:0000305};
DE            EC=3.2.2.- {ECO:0000269|PubMed:12065430};
DE   AltName: Full=Pa-UDGb {ECO:0000303|PubMed:12065430};
GN   OrderedLocusNames=PAE1327 {ECO:0000312|EMBL:AAL63408.1};
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF ALA-68.
RX   PubMed=12065430; DOI=10.1093/emboj/cdf309;
RA   Sartori A.A., Fitz-Gibbon S., Yang H., Miller J.H., Jiricny J.;
RT   "A novel uracil-DNA glycosylase with broad substrate specificity and an
RT   unusual active site.";
RL   EMBO J. 21:3182-3191(2002).
CC   -!- FUNCTION: DNA glycosylase with broad substrate specificity. Can remove
CC       uracil from double-stranded DNA containing either a U/G or U/A base
CC       pair. Can also process hydroxymethyluracil (mispaired with guanine or
CC       adenine), hypoxanthine and fluorouracil. Exhibits a clear preference
CC       for double-stranded DNA substrates, but can also process uracil in
CC       single-stranded DNA, with lower efficiency.
CC       {ECO:0000269|PubMed:12065430}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:12065430};
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       Type 5 (UDGb) family. {ECO:0000305}.
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DR   EMBL; AE009441; AAL63408.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZXE0; -.
DR   SMR; Q8ZXE0; -.
DR   STRING; 178306.PAE1327; -.
DR   EnsemblBacteria; AAL63408; AAL63408; PAE1327.
DR   KEGG; pai:PAE1327; -.
DR   PATRIC; fig|178306.9.peg.981; -.
DR   eggNOG; arCOG00905; Archaea.
DR   HOGENOM; CLU_083279_0_0_2; -.
DR   InParanoid; Q8ZXE0; -.
DR   OMA; CVPPQNK; -.
DR   BRENDA; 3.2.2.27; 5239.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0097506; F:deaminated base DNA N-glycosylase activity; IDA:UniProtKB.
DR   GO; GO:0033958; F:DNA-deoxyinosine glycosylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR   CDD; cd10031; UDG-F5_TTUDGB_like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   InterPro; IPR044147; UdgB-like.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; DNA damage; DNA repair; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Type-5 uracil-DNA glycosylase"
FT                   /id="PRO_0000439188"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         125
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         140
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   MUTAGEN         68
FT                   /note="A->D: 10-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:12065430"
SQ   SEQUENCE   226 AA;  24915 MW;  751755F4E2AB7627 CRC64;
     MDLARVHTPR GWYDDFVNRL VNCARCPRLV SYRSTVKPLR RYESWSYWGR PVPPWGDLNA
     RVMVVGLAPA AHGGNRTGRM FTGDASAQNL FKALFLLGLS NKPYSVSRDD GVEVRCVYIT
     SAVKCAPPKN RPTAEEVYNC SSWLREELEA VRPRAVVALG ELAWRAVLKI LGATTAAFKH
     GEVVNAAGVR VYASYHPSPL NVNTGRLTVE TLAEVLRRAA ADAGCL