UDGA_PYRAE
ID UDGA_PYRAE Reviewed; 196 AA.
AC Q8ZYS2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000305};
DE EC=3.2.2.27 {ECO:0000269|PubMed:11399761};
DE AltName: Full=Pa-UDG {ECO:0000303|PubMed:11399761};
DE AltName: Full=Pa-UDGa {ECO:0000312|EMBL:AAL62921.1};
GN Name=paudg {ECO:0000303|PubMed:11399761};
GN OrderedLocusNames=PAE0651 {ECO:0000312|EMBL:AAL62921.1};
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11399761; DOI=10.1074/jbc.m102985200;
RA Sartori A.A., Schaer P., Fitz-Gibbon S., Miller J.H., Jiricny J.;
RT "Biochemical characterization of uracil processing activities in the
RT hyperthermophilic archaeon Pyrobaculum aerophilum.";
RL J. Biol. Chem. 276:29979-29986(2001).
RN [3]
RP IRON-SULFUR CLUSTER.
RX PubMed=11877410; DOI=10.1074/jbc.m200668200;
RA Hinks J.A., Evans M.C., De Miguel Y., Sartori A.A., Jiricny J., Pearl L.H.;
RT "An iron-sulfur cluster in the family 4 uracil-DNA glycosylases.";
RL J. Biol. Chem. 277:16936-16940(2002).
CC -!- FUNCTION: Removes uracil bases that are present in DNA as a result of
CC either deamination of cytosine or misincorporation of dUMP instead of
CC dTMP. Can remove uracil from double-stranded DNA containing either a
CC U/G or U/A base pair as well as from single-stranded DNA.
CC {ECO:0000269|PubMed:11399761}.
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:0000269|PubMed:11399761};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. {ECO:0000269|PubMed:11399761};
CC -!- MISCELLANEOUS: The 4Fe-4S cluster may have a structural rather than a
CC catalytic role. {ECO:0000269|PubMed:11877410}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC Type 4 (UDGa) family. {ECO:0000305}.
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DR EMBL; AE009441; AAL62921.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZYS2; -.
DR SMR; Q8ZYS2; -.
DR STRING; 178306.PAE0651; -.
DR EnsemblBacteria; AAL62921; AAL62921; PAE0651.
DR KEGG; pai:PAE0651; -.
DR PATRIC; fig|178306.9.peg.467; -.
DR eggNOG; arCOG00905; Archaea.
DR HOGENOM; CLU_044815_1_3_2; -.
DR InParanoid; Q8ZYS2; -.
DR OMA; RPWLIAE; -.
DR BRENDA; 3.2.2.27; 5239.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR005273; Ura-DNA_glyco_family4.
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.
DR TIGRFAMs; TIGR00758; UDG_fam4; 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..196
FT /note="Type-4 uracil-DNA glycosylase"
FT /id="PRO_0000439184"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5,
FT ECO:0000305|PubMed:11877410"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5,
FT ECO:0000305|PubMed:11877410"
FT BINDING 40..42
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 54
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 80
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5,
FT ECO:0000305|PubMed:11877410"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5,
FT ECO:0000305|PubMed:11877410"
FT BINDING 162
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
SQ SEQUENCE 196 AA; 21563 MW; 4AA8B9824738D362 CRC64;
MDLQKLHELI KNCDKCPLHK YRKNAVPGEG EMKLGVMIVG EAPGASEDEA GRPFVGAAGQ
LLTEALSRLG VRRGDVFITN VVKCRPPNNR TPNREEVEAC LPYLIQQIGI LKPRRIIALG
LISAKALMEL MGRRAEKLGD VKGKCYQGRI AGVQVELCIT YHPAAVLRKP ALRGEFQKDL
AMFFGGGLDR FLDPSK
