uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  13 VDIVSEDNEVIAQSSRAQMRAERLRHRATYIVVHDGMGKILVQRRTDIKDFMPGMLDATAGGVVQAGEALLESARREAEE 92
Cdd:cd04697    1 VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742382425  93 ELGIAGVPFAEHGQFYFEDEHCRVWGGLFSCVSHGPFALQESEISEVCWMEPEEIT--ARCDEFTPDTLKALSLWLS 167
Cdd:cd04697   81 ELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILqaARGEEFTPDGRVALERYLA 157

NUDIX domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425   36 LRHRATYIVVHDGMGKILVQRRTDIKdfmPGMLDATAGGVVQAGEALLESARREAEEELGI--------AGVPFAEHGQF 107
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKP---FPGWWSLPGGKVEPGETPEEAARRELEEETGLepellellGSLHYLAPFDG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 742382425  108 YFEDEHcrVWGGLFSCVSHGPFALQ-ESEISEVCWMEPEEI 147
Cdd:pfam00293  78 RFPDEH--EILYVFLAEVEGELEPDpDGEVEEVRWVPLEEL 116

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  13 VDIVSEDNEVIAQSSRAQMRAERLRHRATYIVVHDGMGKILVQRRTDIKDFMPGMLDATAGGVVQAGEALLESARREAEE 92
Cdd:cd04697    1 VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742382425  93 ELGIAGVPFAEHGQFYFEDEHCRVWGGLFSCVSHGPFALQESEISEVCWMEPEEIT--ARCDEFTPDTLKALSLWLS 167
Cdd:cd04697   81 ELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILqaARGEEFTPDGRVALERYLA 157

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  13 VDIVSEDNEVIAQSSRAQMRAERLRHRATYI-VVHDGMGKILVQRRTDIKDFMPGMLDATAGGVVQAGEALLESARREAE 91
Cdd:cd04692    1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVwLVNPEEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742382425  92 EELGIAgVPFAE-----------HGQFYFEDEHCRVwgglFSCVSHGP---FALQESEISEVCWMEP 144
Cdd:cd04692   81 EELGLT-VSPEDliflgvireevIGGDFIDNEFVHV----YLYETDRPleeFKLQPEEVAGVVFVDL 142

Nudix hydrolase homolog

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  38 HRATYIVVH-DGMGKILVQRRTDIKDFMPGMLDATAGGVVQAGEALLESARREAEEELGIAGVPFAEHGQFYFEDEhCRV 116
Cdd:PLN02791  32 HRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLSAQRELEEELGIILPKDAFELLFVFLQE-CVI 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 742382425 117 WGG-----------LFSCVSHGP---FALQESEISEVCWMEPEE 146
Cdd:PLN02791 111 NDGkfinneyndvyLVTTLDPIPleaFTLQESEVSAVKYMSIEE 154

isopentenyl-diphosphate Delta-isomerase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425   8 AGMEWVDIVSEDNEVIAQSSRAQM-RAERLRHRATYIVVHDGMGKILVQRRTDIKDFMPGMLDATAGGVVQAGEALLESA 86
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAhTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  87 RREAEEELGIAGVPFA-EHGQFYF---------EDEHCRVWGGLFScvshGPFALQESEISEVCWMEPEEITARCDEftp 156
Cdd:PRK03759  83 IRRCREELGVEITDLElVLPDFRYratdpngivENEVCPVFAARVT----SALQPNPDEVMDYQWVDPADLLRAVDA--- 155

                        170       180
                 ....*....|....*....|..
gi 742382425 157 dTLKALSLWLSRNAGQESSKER 178
Cdd:PRK03759 156 -TPWAFSPWMVLQAANLEAREL 176

NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742382425  39 RATYIVVHDGMGKILVQRRTDikDFMPGMLDaTAGGVVQAGEALLESARREAEEELGIAGVPFAEHGQFYFE--DEHCRV 116
Cdd:cd02883    1 VAVGAVVFDDEGRVLLVRRSD--GPGPGGWE-LPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPdpDEGRHV 77

                         90       100
                 ....*....|....*....|....*...
gi 742382425 117 WGGLFSCVSHGPFA--LQESEISEVCWM 142
Cdd:cd02883   78 VVLVFLARVVGGEPppLDDEEISEVRWV 105