Reviewed, UniProtKB/Swiss-Prot P05100 (3MG1_ECOLI)

Names and origin

Protein names

Recommended name:
    DNA-3-methyladenine glycosylase 1
    EC=3.2.2.20
Alternative name(s):
    DNA-3-methyladenine glycosylase I
    3-methyladenine-DNA glycosylase I, constitutive
      Short name=TAG I
    DNA-3-methyladenine glycosidase I

Gene names

Name:	tag
Ordered Locus Names:	b3549, JW3518

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	base-excision repair Inferred from electronic annotation. Source: InterPro
Molecular function	DNA-3-methyladenine glycosylase I activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aceE	P0AFG8	1	EBI-558722,EBI-542683

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 187

187

DNA-3-methyladenine glycosylase 1

PRO_0000194877

Secondary structure

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187

Helix Strand Turn

Details...

Helix

11 – 19

9

Beta 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

Beta strand

171 – 173

3

Beta strand

177 – 181

5

Sequences

	Sequence		Length	Mass (Da)
	P05100-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 5A305B5CA66A48FE	FASTA	187	21,100
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and structure of 3-methyladenine-DNA glycosylase I of Escherichia coli." Sakumi K., Nakabeppu Y., Yamamoto Y., Kawabata S., Iwanaga S., Sekiguchi M. J. Biol. Chem. 261:15761-15766(1986) [PubMed: 3536912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29.
[2]	"Nucleotide sequence of the tag gene from Escherichia coli." Steinum A.-L., Seeberg E. Nucleic Acids Res. 14:3763-3772(1986) [PubMed: 3520491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02606 Genomic DNA. Translation: AAA24658.1.
X03845 Genomic DNA. Translation: CAA27472.1.
U00039 Genomic DNA. Translation: AAB18526.1.
U00096 Genomic DNA. Translation: AAC76573.1.
AP009048 Genomic DNA. Translation: BAE77746.1.

PIR

DGECM1. A24604.

RefSeq

AP_004245.1.
NP_418005.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LMZ	NMR	-	A	1-187	[»]
1NKU	NMR	-	A	1-187	[»]
1P7M	NMR	-	A	1-187	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10950N.

IntAct

P05100. 4 interactions.

2-D gel databases

ECO2DBASE

H021.1. 6TH EDITION.

Genome annotation databases

GeneID

947137.

GenomeReviews

Gene locus JW3518 in contig AP009048_GR.
Gene locus b3549 in contig U00096_GR.

KEGG

ecj:JW3518.
eco:b3549.

Organism-specific databases

EchoBASE

EB0979.

EcoGene

EG10986. tag.

CMR

Search...

Phylogenomic databases

HOGENOM

P05100.

OMA

P05100. AYHDQEW.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10986-MON.

Family and domain databases

InterPro

IPR005019. Adenine_glyco.
IPR004597. Tag.
[Graphical view]

Pfam

PF03352. Adenine_glyco. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00624. tag. 1 hit.

ProtoNet

Search...

Entry information

Entry name

3MG1_ECOLI

Accession

Primary (citable) accession number: P05100
Secondary accession number(s): Q2M7L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)