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Protein

Adenine DNA glycosylase

Gene

mutY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (8-oxo-dGTP).

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Proton donor/acceptorBy similarity
Sitei138 – 1381Transition state stabilizerBy similarity
Metal bindingi192 – 1921Iron-sulfur (4Fe-4S)
Metal bindingi199 – 1991Iron-sulfur (4Fe-4S)
Metal bindingi202 – 2021Iron-sulfur (4Fe-4S)
Metal bindingi208 – 2081Iron-sulfur (4Fe-4S)

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10627-MONOMER.
ECOL316407:JW2928-MONOMER.
RETL1328306-WGS:GSTH-1019-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine DNA glycosylase (EC:3.2.2.-)
Alternative name(s):
A/G-specific adenine glycosylase
Gene namesi
Name:mutY
Synonyms:micA
Ordered Locus Names:b2961, JW2928
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10627. mutY.

Pathology & Biotechi

Chemistry

DrugBankiDB00173. Adenine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Adenine DNA glycosylasePRO_0000102234Add
BLAST

Proteomic databases

PaxDbiP17802.
PRIDEiP17802.

Interactioni

Protein-protein interaction databases

BioGridi4262359. 411 interactions.
851767. 3 interactions.
DIPiDIP-10289N.
IntActiP17802. 11 interactions.
MINTiMINT-1240449.
STRINGi511145.b2961.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1715Combined sources
Helixi23 – 253Combined sources
Helixi30 – 4011Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 5814Combined sources
Helixi62 – 676Combined sources
Helixi70 – 778Combined sources
Helixi84 – 9916Combined sources
Helixi108 – 1125Combined sources
Helixi119 – 13012Combined sources
Helixi139 – 14911Combined sources
Helixi158 – 17114Combined sources
Helixi177 – 19014Combined sources
Beta strandi194 – 1963Combined sources
Helixi199 – 2013Combined sources
Turni203 – 2075Combined sources
Helixi209 – 2135Combined sources
Helixi216 – 2183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KG2X-ray1.20A1-225[»]
1KG3X-ray1.55A1-225[»]
1KG4X-ray1.60A1-225[»]
1KG5X-ray1.35A1-225[»]
1KG6X-ray1.50A1-225[»]
1KG7X-ray1.50A1-225[»]
1KQJX-ray1.70A1-225[»]
1MUDX-ray1.80A1-225[»]
1MUNX-ray1.20A1-225[»]
1MUYX-ray1.40A1-225[»]
1WEFX-ray1.90A1-225[»]
1WEGX-ray1.80A1-225[»]
1WEIX-ray1.45A1-225[»]
ProteinModelPortaliP17802.
SMRiP17802. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17802.

Family & Domainsi

Sequence similaritiesi

Belongs to the Nth/MutY family.Curated

Phylogenomic databases

eggNOGiENOG4105CEN. Bacteria.
COG1194. LUCA.
HOGENOMiHOG000028744.
InParanoidiP17802.
KOiK03575.
OMAiEADWLWY.
OrthoDBiEOG6RNQH0.
PhylomeDBiP17802.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQASQFSAQV LDWYDKYGRK TLPWQIDKTP YKVWLSEVML QQTQVATVIP
60 70 80 90 100
YFERFMARFP TVTDLANAPL DEVLHLWTGL GYYARARNLH KAAQQVATLH
110 120 130 140 150
GGKFPETFEE VAALPGVGRS TAGAILSLSL GKHFPILDGN VKRVLARCYA
160 170 180 190 200
VSGWPGKKEV ENKLWSLSEQ VTPAVGVERF NQAMMDLGAM ICTRSKPKCS
210 220 230 240 250
LCPLQNGCIA AANNSWALYP GKKPKQTLPE RTGYFLLLQH EDEVLLAQRP
260 270 280 290 300
PSGLWGGLYC FPQFADEESL RQWLAQRQIA ADNLTQLTAF RHTFSHFHLD
310 320 330 340 350
IVPMWLPVSS FTGCMDEGNA LWYNLAQPPS VGLAAPVERL LQQLRTGAPV
Length:350
Mass (Da):39,149
Last modified:August 1, 1990 - v1
Checksum:iC7D3657C03EBBF4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52391 Genomic DNA. Translation: CAA36624.1.
M59471 Genomic DNA. Translation: AAA72957.1.
U28377 Genomic DNA. Translation: AAA69128.1.
U00096 Genomic DNA. Translation: AAC75998.1.
AP009048 Genomic DNA. Translation: BAE77024.1.
PIRiB38535.
RefSeqiNP_417436.1. NC_000913.3.
WP_001321419.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75998; AAC75998; b2961.
BAE77024; BAE77024; BAE77024.
GeneIDi947447.
KEGGiecj:JW2928.
eco:b2961.
PATRICi32121336. VBIEscCol129921_3056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52391 Genomic DNA. Translation: CAA36624.1.
M59471 Genomic DNA. Translation: AAA72957.1.
U28377 Genomic DNA. Translation: AAA69128.1.
U00096 Genomic DNA. Translation: AAC75998.1.
AP009048 Genomic DNA. Translation: BAE77024.1.
PIRiB38535.
RefSeqiNP_417436.1. NC_000913.3.
WP_001321419.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KG2X-ray1.20A1-225[»]
1KG3X-ray1.55A1-225[»]
1KG4X-ray1.60A1-225[»]
1KG5X-ray1.35A1-225[»]
1KG6X-ray1.50A1-225[»]
1KG7X-ray1.50A1-225[»]
1KQJX-ray1.70A1-225[»]
1MUDX-ray1.80A1-225[»]
1MUNX-ray1.20A1-225[»]
1MUYX-ray1.40A1-225[»]
1WEFX-ray1.90A1-225[»]
1WEGX-ray1.80A1-225[»]
1WEIX-ray1.45A1-225[»]
ProteinModelPortaliP17802.
SMRiP17802. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262359. 411 interactions.
851767. 3 interactions.
DIPiDIP-10289N.
IntActiP17802. 11 interactions.
MINTiMINT-1240449.
STRINGi511145.b2961.

Chemistry

DrugBankiDB00173. Adenine.

Proteomic databases

PaxDbiP17802.
PRIDEiP17802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75998; AAC75998; b2961.
BAE77024; BAE77024; BAE77024.
GeneIDi947447.
KEGGiecj:JW2928.
eco:b2961.
PATRICi32121336. VBIEscCol129921_3056.

Organism-specific databases

EchoBASEiEB0622.
EcoGeneiEG10627. mutY.

Phylogenomic databases

eggNOGiENOG4105CEN. Bacteria.
COG1194. LUCA.
HOGENOMiHOG000028744.
InParanoidiP17802.
KOiK03575.
OMAiEADWLWY.
OrthoDBiEOG6RNQH0.
PhylomeDBiP17802.

Enzyme and pathway databases

BioCyciEcoCyc:EG10627-MONOMER.
ECOL316407:JW2928-MONOMER.
RETL1328306-WGS:GSTH-1019-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP17802.
PROiP17802.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III."
    Michaels M.L., Pham L., Nghiem Y., Cruz C., Miller J.H.
    Nucleic Acids Res. 18:3841-3845(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the Escherichia coli micA gene required for A/G-specific mismatch repair: identity of micA and mutY."
    Tsai-Wu J.-J., Radicella J.P., Lu A.-L.
    J. Bacteriol. 173:1902-1910(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily."
    Guan Y., Manuel R.C., Arvai A.S., Parikh S.S., Mol C.D., Miller J.H., Lloyd S., Tainer J.A.
    Nat. Struct. Biol. 5:1058-1064(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

Entry informationi

Entry nameiMUTY_ECOLI
AccessioniPrimary (citable) accession number: P17802
Secondary accession number(s): Q2M9N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 11, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.