[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29. PubMed=3536912 [NCBI, ExPASy, EBI, Israel, Japan] Sakumi K., Nakabeppu Y., Yamamoto Y., Kawabata S., Iwanaga S., Sekiguchi M.; "Purification and structure of 3-methyladenine-DNA glycosylase I of Escherichia coli."; J. Biol. Chem. 261:15761-15766(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/14.9.3763; PubMed=3520491 [NCBI, ExPASy, EBI, Israel, Japan] Steinum A.-L., Seeberg E.; "Nucleotide sequence of the tag gene from Escherichia coli."; Nucleic Acids Res. 14:3763-3772(1986).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan] Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."; Nucleic Acids Res. 22:2576-2586(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine from the damaged DNA polymer formed by alkylation lesions.
CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3-methyladenine.
ENZYME REGULATION: Activity is controlled by product inhibition.
INTERACTION:
P0AFG8:aceE; NbExp=1; IntAct=EBI-558722, EBI-542683;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02606; AAA24658.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03845; CAA27472.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00039; AAB18526.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76573.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77746.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24604; DGECM1.

RefSeq

AP_004245.1; -.
NP_418005.1; -.

3D structure databases

PDB

1LMZ; NMR; -; A=1-187.	[ExPASy / RCSB / EBI]
1NKU; NMR; -; A=1-187.	[ExPASy / RCSB / EBI]
1P7M; NMR; -; A=1-187.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LMZ; -.
1NKU; -.
1P7M; -.

ModBase

P05100.

Protein-protein interaction databases

DIP

DIP:10950N; -.

IntAct

P05100; -.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10986-MON; -.

2D gel databases

ECO2DBASE

H021.1; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0979; -.

EcoGene

EG10986; tag.

Ontologies

GO:0008725;	Molecular function: DNA-3-methyladenine glycosylase I activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006284;	Biological process: base-excision repair (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005019; Adenine_glyco.
IPR004597; Tag.
Graphical view of domain structure.

Pfam

PF03352; Adenine_glyco; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00624; tag; 1.

ProtoNet

P05100.

Genome annotation databases

GeneID

947137; -.

GenomeReviews

U00096_GR; b3549.
AP009048_GR; JW3518.

KEGG

ecj:JW3518; -.
eco:b3549; -.

Phylogenomic databases

HOGENOM

P05100; -.

Other

LinkHub

P05100; -.

Genome annotation databases

CMR

P05100; b3549.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 187`	`187`	`DNA-3-methyladenine glycosylase 1.`	`PRO_0000194877`
`HELIX`	`11 19`	`9`
`STRAND`	`20 23`	`4`
`HELIX`	`28 41`	`14`
`HELIX`	`46 60`	`15`
`TURN`	`61 63`	`3`
`HELIX`	`65 69`	`5`
`HELIX`	`73 80`	`8`
`HELIX`	`89 107`	`19`
`HELIX`	`112 119`	`8`
`TURN`	`120 122`	`3`
`HELIX`	`132 134`	`3`
`HELIX`	`140 152`	`13`
`HELIX`	`159 169`	`11`
`STRAND`	`171 173`	`3`
`STRAND`	`177 181`	`5`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 21100 Da [This is the MW of the unprocessed precursor]

CRC64: 5A305B5CA66A48FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERCGWVSQD PLYIAYHDNE WGVPETDSKK LFEMICLEGQ QAGLSWITVL KKRENYRACF 

        70         80         90        100        110        120 
HQFDPVKVAA MQEEDVERLV QDAGIIRHRG KIQAIIGNAR AYLQMEQNGE PFVDFVWSFV 

       130        140        150        160        170        180 
NHQPQVTQAT TLSEIPTSTS ASDALSKALK KRGFKFVGTT ICYSFMQACG LVNDHVVGCC 


CYPGNKP

P05100 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools