CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002644
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 8-oxo-dGTP diphosphatase 
Protein Synonyms/Alias
 8-oxo-dGTPase; 7,8-dihydro-8-oxoguanine-triphosphatase; Mutator protein MutT; dGTP pyrophosphohydrolase 
Gene Name
 mutT 
Gene Synonyms/Alias
 b0099; JW0097 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
32ADAHMANKLEFPGGKacetylation[1]
39KLEFPGGKIEMGETPacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 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. 
Sequence Annotation
 DOMAIN 1 129 Nudix hydrolase.
 REGION 6 8 Substrate binding.
 REGION 34 38 Substrate binding.
 MOTIF 38 59 Nudix box.
 METAL 38 38 Magnesium; via carbonyl oxygen.
 METAL 53 53 Magnesium.
 METAL 56 56 Magnesium.
 METAL 57 57 Magnesium.
 BINDING 23 23 Substrate.
 BINDING 28 28 Substrate.
 BINDING 119 119 Substrate.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium; Metal-binding; Mutator protein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 129 AA 
Protein Sequence
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV VRELQEEVGI 60
TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ PGEWMSLVGL NADDFPPANE 120
PVIAKLKRL 129 
Gene Ontology
 GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0030145; F:manganese ion binding; IDA:EcoCyc.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR003561; Mutator_MutT.
 IPR020476; Nudix_hydrolase.
 IPR020084; NUDIX_hydrolase_CS.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF00293; NUDIX 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS
 PR01401; MUTATORMUTT.
 PR00502; NUDIXFAMILY.