P37878 (3MGA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-3-methyladenine glycosylase
EC=3.2.2.21

Alternative name(s):
3-methyladenine-DNA glycosidase

Gene names

Name:	alkA
Ordered Locus Names:	BSU01800

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions. Ref.1
Catalytic activity	Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine. Ref.1
Induction	Up-regulated by methylated AdaA in response to the exposure to alkylating agents. Ref.1
Disruption phenotype	Disruption of this gene sensitizes cells to the alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine. Ref.1
Miscellaneous	Overproduction of this gene renders cells highly resistant to the alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine.
Sequence similarities	Belongs to the alkylbase DNA glycosidase AlkA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Molecular function	DNA-3-methyladenine glycosylase activity Inferred from electronic annotation. Source: EC DNA-3-methylguanine glycosylase activity Inferred from electronic annotation. Source: EC DNA-7-methyladenine glycosylase activity Inferred from electronic annotation. Source: EC DNA-7-methylguanine glycosylase activity Inferred from electronic annotation. Source: EC damaged DNA binding Inferred from electronic annotation. Source: InterPro oxidized purine base lesion DNA N-glycosylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	DNA-3-methyladenine glycosylase		PRO_0000194880
Sites
	Active site	258	1	Proton acceptor By similarity
	Site	238	1	Determinant for substrate specificity and/or activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37878 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 17BEEFC78457A591	FASTA	303	35,634
	10 20 30 40 50 60 MTWHEVNDVI VITLPEIFDM NANLGYLTRE KNECMYEIEN NIITKVIAIG EIRSLVQVSV 70 80 90 100 110 120 INNKQMIVQF LNDSRPVEQW KREEIVKYIH EWFDLDNDLT PFYEMAKADP LLKMPARKFY 130 140 150 160 170 180 GLRVIGIPDL FEALCWGVLG QQINLAFAYS LKKQFVEAFG DSIEWNGKKY WVFPPYERIA 190 200 210 220 230 240 RLTPTDLADI KMTVKKSEYI IGIARLMASG ELSREKLMKM NFKDAEKNLI KIRGIGPWTA 250 260 270 280 290 300 NYVLMRCLRF PTAFPIDDVG LIHSIKILRN MNRKPTKDEI LEISVPWKEW QSYATFYLWR VLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA glycosylase is adjacent to the ada operon." Morohoshi F., Hayashi K., Munakata N. J. Bacteriol. 175:6010-6017(1993) [PubMed: 8376346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ROLE IN RESISTANCE TO ALKYLATION DAMAGE, GENE NAME, INDUCTION, DISRUPTION PHENOTYPE. Strain: 168.
[2]	"Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome." Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D14465 Genomic DNA. Translation: BAA03361.1. AB006424 Genomic DNA. Translation: BAA33073.1. AL009126 Genomic DNA. Translation: CAB11956.1.
PIR	E69584.
RefSeq	NP_388061.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P37878.
SMR	P37878. Positions 9-302.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003321; EBBACP00000003321; EBBACG00000003314.
GeneID	938586.
GenomeReviews	Gene locus BSU01800 in contig AL009126_GR.
KEGG	bsu:BSU01800.
NMPDR	fig|224308.1.peg.180.
PATRIC	18971913. VBIBacSub10457_0185.
Organism-specific databases
GenoList	BSU01800. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002395.
HOGENOM	HBG341234.
OMA	DLFEALC.
PhylomeDB	P37878.
ProtClustDB	CLSK886592.
Enzyme and pathway databases
BioCyc	BSUB:BSU01800-MONOMER.
Family and domain databases
InterPro	IPR010316. AlkA_N. IPR000035. Alkylbase_DNA_glycsylse_CS. IPR011257. DNA_glycosylase. IPR003265. HhH-GPD_domain. IPR023170. HTH_base_excis_C. IPR012904. OGG_N. [Graphical view]
Gene3D	G3DSA:3.30.310.20. AlkA_N. 1 hit. G3DSA:1.10.340.30. DNA_glycosylase. 1 hit. G3DSA:1.10.1670.10. HTH_base_excis_C. 1 hit.
KO	K01247.
Pfam	PF00730. HhH-GPD. 1 hit. PF07934. OGG_N. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
PROSITE	PS00516. ALKYLBASE_DNA_GLYCOS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

3MGA_BACSU

Accession

Primary (citable) accession number: P37878

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program