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Description:
Uracil-DNA glycosylase (EC 3.2.2.-) (UDG).
Molecular weight: 25562
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 )
Important dates:
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
07-MAR-2006, entry version 65.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein UNG_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J03725 | AAA24743.1 | - |
| EMBL | D13169 | BAA02448.1 | - |
| EMBL | D64044 | BAA10923.1 | - |
| EMBL | U00096 | AAC75633.1 | - |
| EMBL | D90886 | BAA16466.1 | - |
| PIR | A28175 | DGECU. | |
| PDB | 1EUG | X-ray | A=1-228. |
| PDB | 1EUI | X-ray | A/B=1-228. |
| PDB | 1FLZ | X-ray | A=1-228. |
| PDB | 1LQG | X-ray | A/B=1-228. |
| PDB | 1LQJ | X-ray | A/B/C/D=1-228. |
| PDB | 1LQM | X-ray | A/C/E/G=1-228. |
| PDB | 1UUG | X-ray | A/C=1-228. |
| PDB | 2EUG | X-ray | A=1-228. |
| PDB | 2UUG | X-ray | A/B=1-228. |
| PDB | 3EUG | X-ray | A=1-228. |
| PDB | 4EUG | X-ray | A=1-228. |
| PDB | 5EUG | X-ray | A=1-228. |
| GenomeReviews | U00096_GR | b2580.1 | |
| EchoBASE | EB1051 | -.1 | |
| EcoGene | EG11058 | ung. | |
| BioCyc | EcoCyc:EG11058-MONOMER | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00148 | - | 1. |
| InterPro | IPR003249 | U_glycsylse_notp. | |
| InterPro | IPR002043 | UDNA_glycsylse. | |
| InterPro | IPR005122 | UDNA_glycsylseSF. | |
| PANTHER | PTHR11264 | U_glycsylse_notp.1 | 1. |
| Pfam | PF03167 | UDG | 1. |
| ProDom | PD001589 | U_glycsylse_notp | 1. |
| TIGRFAMs | TIGR00628 | ung | 1. |
| PROSITE | PS00130 | U_DNA_GLYCOSYLASE | 1. |
Keywords:
3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Glycosidase; Hydrolase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-31.
RX MEDLINE=88227981; PubMed=2836397;
RA Varshney U., Hutcheon T., de Sande J.H.;
RT "Sequence analysis, expression, and conservation of Escherichia coli
RT uracil DNA glycosylase and its gene (ung).";
RL J. Biol. Chem. 263:7776-7784(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in
RT Escherichia coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York
RL (1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [6]
RP STRUCTURE BY NMR.
RX MEDLINE=97407932; PubMed=9261156; DOI=10.1074/jbc.272.34.21408;
RA Lundquist A.J., Beger R.D., Bennett S.E., Bolton P.H., Mosbaugh D.W.;
RT "Site-directed mutagenesis and characterization of uracil-DNA
RT glycosylase inhibitor protein. Role of specific carboxylic amino acids
RT in complex formation with Escherichia coli uracil-DNA glycosylase.";
RL J. Biol. Chem. 272:21408-21419(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX MEDLINE=98451580; PubMed=9776748; DOI=10.1093/nar/26.21.4880;
RA Ravishankar R., Sagar M.B., Roy S., Purnapatre K., Handa P.,
RA Varshney U., Vijayan M.;
RT "X-ray analysis of a complex of Escherichia coli uracil DNA
RT glycosylase (EcUDG) with a proteinaceous inhibitor. The structure
RT elucidation of a prokaryotic UDG.";
RL Nucleic Acids Res. 26:4880-4887(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX MEDLINE=99182421; PubMed=10080896; DOI=10.1006/jmbi.1999.2605;
RA Putnam C.D., Shroyer M.J.N., Lundquist A.J., Mol C.D., Arvai A.S.,
RA Mosbaugh D.W., Tainer J.A.;
RT "Protein mimicry of DNA from crystal structures of the uracil-DNA
RT glycosylase inhibitor protein and its complex with Escherichia coli
RT uracil-DNA glycosylase.";
RL J. Mol. Biol. 287:331-346(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX MEDLINE=99188668; PubMed=10090282;
RX DOI=10.1002/(SICI)1097-0134(19990401)35:1<13::AID-PROT2>3.3.CO;2-U;
RA Xiao G., Tordova M., Jagadeesh J., Drohat A.C., Stivers J.T.,
RA Gilliland G.L.;
RT "Crystal structure of Escherichia coli uracil DNA glycosylase and its
RT complexes with uracil and glycerol: structure and glycosylase
RT mechanism revisited.";
RL Proteins 35:13-24(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX MEDLINE=20480086; PubMed=11027138; DOI=10.1021/bi001532v;
RA Werner R.M., Jiang Y.L., Gordley R.G., Jagadeesh G.J., Ladner J.E.,
RA Xiao G., Tordova M., Gilliland G.L., Stivers J.T.;
RT "Stressing-out DNA? The contribution of serine-phosphodiester
RT interactions in catalysis by uracil DNA glycosylase.";
RL Biochemistry 39:12585-12594(2000).
Feature:
INIT_MET 0 0
CHAIN 1 228 Uracil-DNA glycosylase.
/FTId=PRO_0000176091.
ACT_SITE 63 63 Proton acceptor.
HELIX 6 10
TURN 11 12
HELIX 13 15
STRAND 16 16
HELIX 17 30
TURN 31 33
STRAND 34 34
STRAND 36 38
HELIX 40 42
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HELIX 45 49
STRAND 50 50
HELIX 52 54
STRAND 57 63
STRAND 67 67
TURN 68 70
STRAND 72 74
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STRAND 82 82
HELIX 86 98
STRAND 99 99
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STRAND 106 106
HELIX 111 114
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STRAND 118 124
STRAND 127 128
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STRAND 131 131
TURN 132 137
STRAND 138 139
HELIX 140 154
STRAND 156 157
STRAND 159 164
HELIX 165 170
TURN 171 173
STRAND 174 174
TURN 176 178
STRAND 179 184
STRAND 187 188
TURN 189 191
HELIX 192 196
TURN 197 198
HELIX 201 211
TURN 212 213
STRAND 220 220
Comments:
-!- FUNCTION: Excises uracil residues from the DNA which can arise as
a result of misincorporation of dUMP residues by DNA polymerase or
due to deamination of cytosine.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P10484:hsdM; NbExp=1; IntAct=EBI-559403, EBI-552119;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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Sequence length: 228
ANELTWHDVL AEEKQQPYFL NTLQTVASER QSGVTIYPPQ KDVFNAFRFT ELGDVKVVIL
GQDPYHGPGQ AHGLAFSVRP GIAIPPSLLN MYKELENTIP GFTRPNHGYL ESWARQGVLL
LNTVLTVRAG QAHSHASLGW ETFTDKVISL INQHREGVVF LLWGSHAQKK GAIIDKQRHH
VLKAPHPSPL SAHRGFFGCN HFVLANQWLE QRGETPIDWM PVLPAESE