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Description:
A/G-specific adenine glycosylase (EC 3.2.2.-).
Molecular weight: 39149
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-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
07-MAR-2006, entry version 64.
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 MUTY_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X52391 | CAA36624.1 | - |
| EMBL | M59471 | AAA72957.1 | - |
| EMBL | U28377 | AAA69128.1 | - |
| EMBL | U00096 | AAC75998.1 | - |
| PIR | B38535 | B38535. | |
| PDB | 1KG2 | X-ray | A=1-225. |
| PDB | 1KG3 | X-ray | A=1-225. |
| PDB | 1KG4 | X-ray | A=1-225. |
| PDB | 1KG5 | X-ray | A=1-225. |
| PDB | 1KG6 | X-ray | A=1-225. |
| PDB | 1KG7 | X-ray | A=1-225. |
| PDB | 1KQJ | X-ray | A=1-225. |
| PDB | 1MUD | X-ray | A=1-225. |
| PDB | 1MUN | X-ray | @=1-225. |
| PDB | 1MUY | X-ray | A=1-225. |
| PDB | 1WEF | X-ray | A=1-225. |
| PDB | 1WEG | X-ray | A=1-225. |
| PDB | 1WEI | X-ray | A=1-225. |
| GenomeReviews | U00096_GR | b2961.1 | |
| EchoBASE | EB0622 | -.1 | |
| EcoGene | EG10627 | mutY. | |
| BioCyc | EcoCyc:EG10627-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 | IPR013003 | MutY. | |
| InterPro | IPR005760 | MutY_bac. | |
| PANTHER | PTHR10359:SF3 | MutY.1 | 1. |
| Pfam | PF00633 | HHH | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| SMART | SM00478 | ENDO3c | 1. |
| SMART | SM00525 | FES | 1. |
| TIGRFAMs | TIGR01084 | mutY | 1. |
| PROSITE | PS00764 | ENDONUCLEASE_III_1 | 1. |
| PROSITE | PS01155 | ENDONUCLEASE_III_2 | 1. |
Keywords:
3D-structure; 4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Metal-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=90326504; PubMed=2197596;
RA Michaels M.L., Pham L., Nghiem Y., Cruz C., Miller J.H.;
RT "MutY, an adenine glycosylase active on G-A mispairs, has homology to
RT endonuclease III.";
RL Nucleic Acids Res. 18:3841-3845(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=91161503; PubMed=2001994;
RA Tsai-Wu J.-J., Radicella J.P., Lu A.-L.;
RT "Nucleotide sequence of the Escherichia coli micA gene required for
RT A/G-specific mismatch repair: identity of micA and mutY.";
RL J. Bacteriol. 173:1902-1910(1991).
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 X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX MEDLINE=99061333; PubMed=9846876;
RA Guan Y., Manuel R.C., Arvai A.S., Parikh S.S., Mol C.D., Miller J.H.,
RA Lloyd S., Tainer J.A.;
RT "MutY catalytic core, mutant and bound adenine structures define
RT specificity for DNA repair enzyme superfamily.";
RL Nat. Struct. Biol. 5:1058-1064(1998).
Feature:
CHAIN 1 350 A/G-specific adenine glycosylase.
/FTId=PRO_0000102234.
METAL 192 192 Iron-sulfur (4Fe-4S).
METAL 199 199 Iron-sulfur (4Fe-4S).
METAL 202 202 Iron-sulfur (4Fe-4S).
METAL 208 208 Iron-sulfur (4Fe-4S).
HELIX 3 17
STRAND 22 22
HELIX 23 25
STRAND 26 27
HELIX 30 40
TURN 41 41
STRAND 42 43
HELIX 45 58
STRAND 60 61
HELIX 62 67
STRAND 68 68
HELIX 70 77
TURN 78 79
STRAND 80 80
TURN 83 83
HELIX 84 99
STRAND 100 100
TURN 101 102
STRAND 103 103
STRAND 107 107
HELIX 108 112
TURN 113 113
STRAND 114 114
TURN 115 116
HELIX 119 130
STRAND 133 133
HELIX 139 149
TURN 150 150
STRAND 153 153
TURN 155 156
STRAND 157 157
HELIX 158 171
STRAND 174 174
TURN 175 176
HELIX 177 190
TURN 191 191
STRAND 192 192
STRAND 194 196
HELIX 199 201
TURN 203 207
HELIX 209 213
TURN 214 214
HELIX 216 218
STRAND 219 220
Comments:
-!- FUNCTION: Adenine glycosylase active on G-A mispairs. MutY also
corrects error-prone DNA synthesis past go lesions which are due
to the oxidatively damaged form of guanine: 7,8-dihydro-8-
oxoguanine.
-!- 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.
-!- SIMILARITY: Belongs to the nth/mutY family.
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Sequence length: 350
MQASQFSAQV LDWYDKYGRK TLPWQIDKTP YKVWLSEVML QQTQVATVIP YFERFMARFP
TVTDLANAPL DEVLHLWTGL GYYARARNLH KAAQQVATLH GGKFPETFEE VAALPGVGRS
TAGAILSLSL GKHFPILDGN VKRVLARCYA VSGWPGKKEV ENKLWSLSEQ VTPAVGVERF
NQAMMDLGAM ICTRSKPKCS LCPLQNGCIA AANNSWALYP GKKPKQTLPE RTGYFLLLQH
EDEVLLAQRP PSGLWGGLYC FPQFADEESL RQWLAQRQIA ADNLTQLTAF RHTFSHFHLD
IVPMWLPVSS FTGCMDEGNA LWYNLAQPPS VGLAAPVERL LQQLRTGAPV