UNG_VIBCH
ID UNG_VIBCH Reviewed; 226 AA.
AC Q9KPK8;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=VC_2359;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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}.
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DR EMBL; AE003852; AAF95502.1; -; Genomic_DNA.
DR PIR; C82086; C82086.
DR RefSeq; NP_231989.1; NC_002505.1.
DR RefSeq; WP_000004496.1; NZ_LT906614.1.
DR PDB; 2JHQ; X-ray; 1.50 A; A=1-226.
DR PDBsum; 2JHQ; -.
DR AlphaFoldDB; Q9KPK8; -.
DR SMR; Q9KPK8; -.
DR STRING; 243277.VC_2359; -.
DR DNASU; 2613028; -.
DR EnsemblBacteria; AAF95502; AAF95502; VC_2359.
DR GeneID; 57740969; -.
DR KEGG; vch:VC_2359; -.
DR PATRIC; fig|243277.26.peg.2246; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_0_6; -.
DR OMA; PDNGYLM; -.
DR BioCyc; VCHO:VC2359-MON; -.
DR BRENDA; 3.2.2.27; 6626.
DR EvolutionaryTrace; Q9KPK8; -.
DR Proteomes; UP000000584; Chromosome 1.
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; -; 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 PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176161"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:2JHQ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2JHQ"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2JHQ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:2JHQ"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2JHQ"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2JHQ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:2JHQ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2JHQ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2JHQ"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2JHQ"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:2JHQ"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:2JHQ"
SQ SEQUENCE 226 AA; 25446 MW; 8C972727FFCD4EA4 CRC64;
MSESLTWHDV IGNEKQQAYF QQTLQFVESQ RQAGKVIYPP AKDVFNAFRF TEFGDVKVVI
LGQDPYHGPN QAHGLCFSVL PGVKTPPSLV NIYKELAQDI PGFQIPPHGY LQSWAQQGVL
LLNTVLTVEQ GMAHSHANTG WETFTDRVID ALNQHRNGLI FLLWGSHAQK KGQMIDRQRH
HVLMAPHPSP LSAHRGFLGC RHFSKTNQLL QAQGIAPINW QPELES
