Mutator mutT protein - Escherichia coli (strain K12)

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P08337 (MUTT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mutator mutT protein

Alternative name(s):
7,8-dihydro-8-oxoguanine-triphosphatase
8-oxo-dGTPase
EC=3.6.1.-
dGTP pyrophosphohydrolase

Gene names

Name:	mutT
Ordered Locus Names:	b0099, JW0097

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate. Ref.9
Catalytic activity	8-oxo-dGTP + H₂O = 8-oxo-dGMP + diphosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Monomer.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase Mutator protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity Inferred from direct assay Ref.7. Source: EcoCyc magnesium ion binding Inferred from direct assay. Source: EcoCyc manganese ion binding Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 129

129

Mutator mutT protein

PRO_0000056943

Regions

Domain

1 – 129

129

Nudix hydrolase

Region

6 – 8

Substrate binding

Region

34 – 38

Substrate binding

Motif

38 – 59

Nudix box

Sites

Metal binding

Magnesium; via carbonyl oxygen

Metal binding

Magnesium

Metal binding

Magnesium

Metal binding

Magnesium

Binding site

Substrate

Binding site

Substrate

Binding site

119

Substrate

Secondary structure

129

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08337 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 626287828DCEA53E
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FASTA

129

14,927

        10         20         30         40         50         60 
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV VRELQEEVGI 

        70         80         90        100        110        120 
TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ PGEWMSLVGL NADDFPPANE 


PVIAKLKRL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of the mutT mutator of Escherichia coli that causes A:T to C:G transversion." Akiyama M., Horiuchi T., Sekiguchi M. Mol. Gen. Genet. 206:9-16(1987) [PubMed: 3033442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"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.
[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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli." Schmidt M., Rollo E., Grodberg J., Oliver D. J. Bacteriol. 170:3404-3414(1988) [PubMed: 2841285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75. Strain: K12.
[6]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-129. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase." Bhatnagar S.K., Bessman M.J. J. Biol. Chem. 263:8953-8957(1988) [PubMed: 3288626] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: K12.
[8]	"Characterization of the mutT nucleoside triphosphatase of Escherichia coli." Bhatnagar S.K., Bullions L.C., Bessman M.J. J. Biol. Chem. 266:9050-9054(1991) [PubMed: 1851162] [Abstract] Cited for: CHARACTERIZATION.
[9]	"MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis." Maki H., Sekiguchi M. Nature 355:273-275(1992) [PubMed: 1309939] [Abstract] Cited for: FUNCTION.
[10]	"Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase." Abeygunawardana C., Weber D.J., Gittis A.G., Frick D.N., Lin J., Miller A.F., Bessman M.J., Mildvan A.S. Biochemistry 34:14997-15005(1995) [PubMed: 7578113] [Abstract] Cited for: STRUCTURE BY NMR.
[11]	"Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action." Lin J., Abeygunawardana C., Frick D.N., Bessman M.J., Mildvan A.S. Biochemistry 36:1199-1211(1997) [PubMed: 9063868] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH MAGNESIUM IONS AND AMPCPP.
[12]	"Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base." Nakamura T., Meshitsuka S., Kitagawa S., Abe N., Yamada J., Ishino T., Nakano H., Tsuzuki T., Doi T., Kobayashi Y., Fujii S., Sekiguchi M., Yamagata Y. J. Biol. Chem. 285:444-452(2010) [PubMed: 19864691] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH 8-OXO-GMP MANGANESE IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04831 Genomic DNA. Translation: CAA28523.1.
M20791 Genomic DNA. Translation: AAA24620.1.
X55034 Genomic DNA. Translation: CAA38876.1.
U00096 Genomic DNA. Translation: AAC73210.1.
AP009048 Genomic DNA. Translation: BAB96667.1.

PIR

MVECMT. A27890.

RefSeq

NP_414641.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MUT	NMR	-	A	1-129	[»]
1PPX	NMR	-	A	1-129	[»]
1PUN	NMR	-	A	1-129	[»]
1PUQ	NMR	-	A	1-129	[»]
1PUS	NMR	-	A	1-129	[»]
1TUM	NMR	-	A	1-129	[»]
3A6S	X-ray	1.80	A/B	1-129	[»]
3A6T	X-ray	1.96	A	1-129	[»]
3A6U	X-ray	2.56	A	1-129	[»]
3A6V	X-ray	2.00	A/B	1-129	[»]

ProteinModelPortal

P08337.

SMR

P08337. Positions 3-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10288N.

IntAct

P08337. 2 interactions.

MINT

MINT-1239561.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004172; EBESCP00000004172; EBESCG00000003408.
EBESCT00000014384; EBESCP00000013675; EBESCG00000013445.

GeneID

944824.

GenomeReviews

Gene locus JW0097 in contig AP009048_GR.
Gene locus b0099 in contig U00096_GR.

KEGG

ecj:JW0097.
eco:b0099.

PATRIC

32115303. VBIEscCol129921_0103.

Organism-specific databases

EchoBASE

EB0621.

EcoGene

EG10626. mutT.

Phylogenomic databases

eggNOG

COG0494.

GeneTree

EBGT00050000009041.

HOGENOM

HBG741910.

OMA

KLEYQFP.

PhylomeDB

P08337.

ProtClustDB

PRK10776.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10626-MONOMER.
MetaCyc:EG10626-MONOMER.

Gene expression databases

Genevestigator

P08337.

Family and domain databases

InterPro

IPR003561. Mutator_MutT.
IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

K03574.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PRINTS

PR01401. MUTATORMUTT.
PR00502. NUDIXFAMILY.

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

TIGRFAMs

TIGR00586. Mutt. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MUTT_ECOLI

Accession

Primary (citable) accession number: P08337

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents