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Description:
Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site)lyase).
Molecular weight: 23562
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:
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
07-MAR-2006, entry version 7.
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 END3_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J02857 | AAA24227.1 | - |
| EMBL | D90806 | BAA15387.1 | - |
| EMBL | D90807 | BAA15394.1 | - |
| EMBL | D90808 | BAA15417.1 | - |
| EMBL | U00096 | AAC74705.1 | - |
| PIR | A32412 | A32412. | |
| PDB | 2ABK | X-ray | @=1-211. |
| GenomeReviews | U00096_GR | b1633.1 | |
| EchoBASE | EB0656 | -.1 | |
| EcoGene | EG10662 | nth. | |
| BioCyc | EcoCyc:EG10662-MONOMER | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR003265 | Endo_3c. | |
| InterPro | IPR004035 | EndoIII_FCL. | |
| InterPro | IPR004036 | EndoIII_HhH. | |
| InterPro | IPR003651 | FeS_bind. | |
| InterPro | IPR000445 | HhH. | |
| InterPro | IPR005759 | Nth. | |
| Pfam | PF00633 | HHH | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| SMART | SM00478 | ENDO3c | 1. |
| SMART | SM00525 | FES | 1. |
| TIGRFAMs | TIGR01083 | nth | 1. |
| PROSITE | PS00764 | ENDONUCLEASE_III_1 | 1. |
| PROSITE | PS01155 | ENDONUCLEASE_III_2 | 1. |
Keywords:
3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Multifunctional enzyme.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX MEDLINE=89352503; PubMed=2669955;
RA Asahara H., Wistort P.M., Bank J.F., Bakerian R.H., Cunningham R.P.;
RT "Purification and characterization of Escherichia coli endonuclease
RT III from the cloned nth gene.";
RL Biochemistry 28:4444-4449(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
RP MUTAGENESIS OF LYS-120.
RX MEDLINE=94379627; PubMed=8092678;
RA Cunningham R.P., Ahern H., Xing D., Thayer M.M., Tainer J.A.;
RT "Structure and function of Escherichia coli endonuclease III.";
RL Ann. N. Y. Acad. Sci. 726:215-222(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX MEDLINE=93030750; PubMed=1411536;
RA Kuo C.-F., McRee D., Fisher C.L., O'Handley S.F., Cunningham R.P.,
RA Tainer J.A.;
RT "Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease
RT III.";
RL Science 258:434-440(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX MEDLINE=95393988; PubMed=7664751;
RA Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A.;
RT "Novel DNA binding motifs in the DNA repair enzyme endonuclease III
RT crystal structure.";
RL EMBO J. 14:4108-4120(1995).
Feature:
CHAIN 1 211 Endonuclease III.
/FTId=PRO_0000102210.
ACT_SITE 112 112 Nucleophile; in the N-glycosylase
reaction (Probable).
METAL 187 187 Iron-sulfur (4Fe-4S).
METAL 194 194 Iron-sulfur (4Fe-4S).
METAL 197 197 Iron-sulfur (4Fe-4S).
METAL 203 203 Iron-sulfur (4Fe-4S).
MUTAGEN 120 120 K->Q: 10000-fold decrease in activity.
HELIX 3 16
HELIX 29 38
TURN 39 41
HELIX 44 54
TURN 55 57
HELIX 61 76
TURN 77 78
TURN 80 81
HELIX 82 99
TURN 100 102
HELIX 108 113
TURN 115 116
HELIX 119 130
HELIX 139 148
HELIX 156 166
HELIX 169 171
TURN 172 174
HELIX 175 185
TURN 186 186
HELIX 194 196
TURN 198 199
HELIX 200 202
TURN 206 207
Comments:
-!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
activity and a DNA N-glycosylase activity. Incises damaged DNA at
cytosines, thymines and guanines. Acts on a damaged strand, 5'
from the damaged site. Required for the repair of both oxidative
DNA damage and spontaneous mutagenic lesions.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- COFACTOR: Binds 1 4Fe-4S cluster which is not important for the
catalytic activity, but which is probably involved in the proper
positioning of the enzyme along the DNA strand.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the nth/mutY family.
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Sequence length: 211
MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT
PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK
TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI
LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I