Protein Domain : IPR000086

Type:  Domain Name:  NUDIX hydrolase domain
Description:  The Nudix superfamily is widespread among eucaryotes, bacteria, archaea and viruses and consists mainly of pyrophosphohydrolases that act upon substrates of general structure NUcleoside DIphosphate linked to another moiety, X (NDP-X) to yield NMP plus P-X. Such substrates include (d)NTPs (both canonical and oxidised derivatives), nucleotide sugars and alcohols, dinucleoside polyphosphates (NpnN), dinucleotide coenzymes and capped RNAs. However, phosphohydrolase activity, including activity towards NDPs themselves, and non-nucleotide substrates such as diphosphoinositol polyphosphates (DIPs), 5-phosphoribosyl 1-pyrophosphate (PRPP), thiamine pyrophosphate (TPP) and dihydroneopterin triphosphate (DHNTP) have also been described. Some superfamily members, such as Escherichia coli mutT, have the ability to degrade potentially mutagenic, oxidised nucleotides while others control the levels of metabolic intermediates and signalling compounds. In procaryotes and simple eucaryotes, the number of Nudix genes varies from 0 to over 30, reflecting the metabolic complexity and adaptability of the organism. Nudix hydrolases are typically small proteins, larger ones having additional domains with interactive or other catalytic functions []. The Nudix domain formed by two beta-sheets packed between alpha-helices [, ]. It can accomodate sequences of different lengths in the connecting loops and in the amtiparallel beta-sheet. Catalysis depends on the conserved 23-amino acid Nudix motif (Nudix box), G-x(5)-E-x(5)-[UA]-x-R-E-x(2)-E-E-x-G-U, where U is an aliphatic, hydrophobic residue. This sequence is located in a loop-helix-loop structural motif and the Glu residues in the core of the motif, R-E-x(2)-E-E, play an important role in binding essential divalent cations []. The substrate specificity is determined by other residues outside the Nudix box. For example, CoA pyrophosphatases share the NuCoA motif L-L-T-x-R-[SA]-x(3)-R-x(3)-G-x(3)-F-P-G-G that is located N-terminal of the Nudix box and is involved in CoA recognition []. Short Name:  NUDIX_hydrolase_dom
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1 Child Features

DB identifier Type Name
IPR020476 Domain NUDIX hydrolase

2 Contains

DB identifier Type Name
IPR020084 Conserved_site NUDIX hydrolase, conserved site
IPR000059 Conserved_site NUDIX hydrolase, NudL, conserved site

2 Cross Referencess

Identifier
PF00293
PS51462

10 Found Ins

DB identifier Type Name
IPR003563 Family 7,8-dihydro-8-oxoguanine triphosphatase
IPR003293 Family Nudix hydrolase 6-like
IPR003561 Family Mutator MutT
IPR004385 Family Nucleoside diphosphate pyrophosphatase
IPR014078 Family Nucleoside triphosphatase YtkD
IPR003562 Family Mutator MutX protein
IPR003564 Family Dihydroneopterin triphosphate diphosphatase
IPR003565 Family Bis(5'-nucleosyl)-tetraphosphatase
IPR003300 Family Viral protein D9
IPR003301 Family Vaccinia virus D10, decapping enzyme

1 GO Annotation

GO Term Gene Name
GO:0016787 IPR000086

1 Ontology Annotations

GO Term Gene Name
GO:0016787 IPR000086

1 Parent Features

DB identifier Type Name
IPR015797 Domain NUDIX hydrolase domain-like

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
410980 D8RHM1 PAC:15409597 Selaginella moellendorffii 169  
5768 D8RKB0 PAC:15421022 Selaginella moellendorffii 128  
67467 D8QV61 PAC:15411528 Selaginella moellendorffii 175  
99897 D8RRE0 PAC:15419749 Selaginella moellendorffii 181  
150295 D8RVF9 PAC:15412576 Selaginella moellendorffii 259  
103175 D8RW55 PAC:15406770 Selaginella moellendorffii 202  
80228 D8QX43 PAC:15403710 Selaginella moellendorffii 198  
151789 D8S1P9 PAC:15419257 Selaginella moellendorffii 234  
176548 D8S3E0 PAC:15402001 Selaginella moellendorffii 355  
54771 D8S2U2 PAC:15420157 Selaginella moellendorffii 254  
438877 D8R034 PAC:15401957 Selaginella moellendorffii 325  
85508 D8R632 PAC:15420652 Selaginella moellendorffii 165  
139849 D8QMV6 PAC:15406548 Selaginella moellendorffii 237  
85946 D8R5K2 PAC:15401455 Selaginella moellendorffii 291  
163872 D8QQL9 PAC:15410777 Selaginella moellendorffii 279  
183198 D8SVX5 PAC:15419816 Selaginella moellendorffii 752  
73964 D8QNW5 PAC:15410860 Selaginella moellendorffii 180  
evm.model.supercontig_104.36 PAC:16405041 Carica papaya 242  
evm.model.supercontig_107.45 PAC:16405349 Carica papaya 206  
evm.model.supercontig_1105.3 PAC:16405823 Carica papaya 234  
evm.model.supercontig_116.67 PAC:16406326 Carica papaya 189  
evm.model.supercontig_12.144 PAC:16406686 Carica papaya 282  
evm.model.supercontig_136.34 PAC:16408324 Carica papaya 277  
evm.model.supercontig_2.207 PAC:16412572 Carica papaya 183  
evm.model.supercontig_2126.1 PAC:16413693 Carica papaya 226  
evm.model.supercontig_23.139 PAC:16414187 Carica papaya 382  
evm.model.supercontig_27.231 PAC:16415614 Carica papaya 263  
evm.model.supercontig_29.48 PAC:16416256 Carica papaya 273  
evm.model.supercontig_3.367 PAC:16416665 Carica papaya 198  
evm.model.supercontig_371.3 PAC:16418791 Carica papaya 224  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8810257
            16378245
            17698004
            19340986