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UDGB_MYCTU
ID   UDGB_MYCTU              Reviewed;         268 AA.
AC   P9WM53; L0T7R5; P64785; Q11059;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Type-5 uracil-DNA glycosylase {ECO:0000305};
DE            EC=3.2.2.- {ECO:0000269|PubMed:17588829};
GN   Name=udgB {ECO:0000303|PubMed:17588829}; OrderedLocusNames=Rv1259;
GN   ORFNames=MTCY50.23c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   IRON-SULFUR CLUSTER.
RX   PubMed=17588829; DOI=10.1016/j.dnarep.2007.05.001;
RA   Srinath T., Bharti S.K., Varshney U.;
RT   "Substrate specificities and functional characterization of a thermo-
RT   tolerant uracil DNA glycosylase (UdgB) from Mycobacterium tuberculosis.";
RL   DNA Repair 6:1517-1528(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: DNA glycosylase with broad substrate specificity. Can remove
CC       uracil from double-stranded DNA containing either a U/G, U/A, U/C or
CC       U/T base pair. Can also excise ethenocytosine and hypoxanthine from
CC       double-stranded DNA. {ECO:0000269|PubMed:17588829}.
CC   -!- ACTIVITY REGULATION: Product inhibited by AP-site containing dsDNA but
CC       not by uracil. {ECO:0000269|PubMed:17588829}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermo-tolerant. {ECO:0000269|PubMed:17588829};
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       Type 5 (UDGb) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP44015.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL123456; CCP44015.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70753; C70753.
DR   RefSeq; NP_215775.1; NC_000962.3.
DR   AlphaFoldDB; P9WM53; -.
DR   SMR; P9WM53; -.
DR   STRING; 83332.Rv1259; -.
DR   PaxDb; P9WM53; -.
DR   GeneID; 887047; -.
DR   KEGG; mtu:Rv1259; -.
DR   PATRIC; fig|83332.12.peg.1410; -.
DR   TubercuList; Rv1259; -.
DR   eggNOG; COG1573; Bacteria.
DR   OMA; CVPPQNK; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0033958; F:DNA-deoxyinosine glycosylase activity; IDA:MTBBASE.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:MTBBASE.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:MTBBASE.
DR   GO; GO:0006284; P:base-excision repair; IDA:MTBBASE.
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..268
FT                   /note="Type-5 uracil-DNA glycosylase"
FT                   /id="PRO_0000103774"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         161
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT   BINDING         176
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJ65"
SQ   SEQUENCE   268 AA;  28500 MW;  6F2C31C9C561E7FD CRC64;
     MHPKTGRAFR SPVEPGSGWP GDPATPQTPV AADAAQVSAL AGGAGSICEL NALISVCRAC
     PRLVSWREEV AVVKRRAFAD QPYWGRPVPG WGSKRPRLLI LGLAPAAHGA NRTGRMFTGD
     RSGDQLYAAL HRAGLVNSPV SVDAADGLRA NRIRITAPVR CAPPGNSPTP AERLTCSPWL
     NAEWRLVSDH IRAIVALGGF AWQVALRLAG ASGTPKPRFG HGVVTELGAG VRLLGCYHPS
     QQNMFTGRLT PTMLDDIFRE AKKLAGIE
 
 
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