coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949  28 QAAVLVPIT-RSDDPELVLTLRAAGLSTHGGEVAFPGGRRDPEDADLVRTALREAEEEIALPPGLVEVVGPLSTLVSRHG 106
Cdd:cd03426   2 RAAVLIPLVeGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEIGLPPESVEVLGRLDPLYTPSG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598949 107 IEVTPYVAFIPDFVEYQPNDGEIAAVFNVPLSFFRDDPREVTHRIDYFG--RSWYVPSYRFGEFKIWGLTAIMVVEL 181
Cdd:cd03426  82 FVVTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGprGTYRVPFYPYEGYVIWGLTARILSEL 158

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949  28 QAAVLVPIT-RSDDPELVLTLRAAGLSTHGGEVAFPGGRRDPEDADLVRTALREAEEEIALPPGLVEVVGPLSTLVSRHG 106
Cdd:cd03426   2 RAAVLIPLVeGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEIGLPPESVEVLGRLDPLYTPSG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598949 107 IEVTPYVAFIPDFVEYQPNDGEIAAVFNVPLSFFRDDPREVTHRIDYFG--RSWYVPSYRFGEFKIWGLTAIMVVEL 181
Cdd:cd03426  82 FVVTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGprGTYRVPFYPYEGYVIWGLTARILSEL 158

8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949  25 RFPQAAVLVPITrsDDPELVLTLRAAGlSTHGGEVAFPGGRRDPEDaDLVRTALREAEEEIALPPGLVEVVGPLSTlVSR 104
Cdd:COG0494  11 HYRPAVVVVLLD--DDGRVLLVRRYRY-GVGPGLWEFPGGKIEPGE-SPEEAALRELREETGLTAEDLELLGELPS-PGY 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598949 105 HGIEVTPYVA-FIPDFVEYQPND-GEIAAVFNVPLSFFRD 142
Cdd:COG0494  86 TDEKVHVFLArGLGPGEEVGLDDeDEFIEVRWVPLDEALA 125

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949  28 QAAVLVPIT-RSDDPELVLTLRAAGLSTHGGEVAFPGGRRDPEDADLVRTALREAEEEIALPPGLVEVVGPLSTLVSRHG 106
Cdd:cd03426   2 RAAVLIPLVeGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEIGLPPESVEVLGRLDPLYTPSG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598949 107 IEVTPYVAFIPDFVEYQPNDGEIAAVFNVPLSFFRDDPREVTHRIDYFG--RSWYVPSYRFGEFKIWGLTAIMVVEL 181
Cdd:cd03426  82 FVVTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGprGTYRVPFYPYEGYVIWGLTARILSEL 158

nudix hydrolase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949    7 ELRQRIEAHRPRQLDTDQRFP--QAAVLVPI---TRSDDPEL--VLTLRAAGLSTHGGEVAFPGGRRDPEDADLVRTALR 79
Cdd:PLN02709  10 ELQNLIKLFQNCETHLRQHFPakSSAVLVCLyqeQREDKNELrvILTKRSSTLSSHPGEVALPGGKRDEEDKDDIATALR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949   80 EAEEEIALPPGLVEVVGPLSTLVSRHGIEVTPYVAFIPDFVEYQ--PNDGEIAAVFNVPLSFFRDDPREVTHRIDYFGRS 157
Cdd:PLN02709  90 EAREEIGLDPSLVTIISVLEPFVNKKGMSVAPVIGFLHDKKAFKplPNPAEVEEIFDVPLEMFLKDKNKRAEEREHEGER 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15598949  158 WYVPSYRF------GEFKIWGLTAIMVVELVNLLY 186
Cdd:PLN02709 170 YLLQYFDYysedkeRNFIIWALTAGILIRVASIVY 204

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 15598949  29 AAVLVPITRSDD--PELVLTLRAaGLSTHGGEVAFPGGRRDP-EDAdlVRTALREAEEEIALPPGLVEVVGplsTLVSRH 105
Cdd:cd18877  18 AAGLLLFAPAEDggPHVLLQHRA-WWTHQGGTWALPGGARDSgETP--EAAALRETEEETGLDADTLRVVG---THVDDH 91

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598949 106 GIEV-TPYVAFIPDFVEYQPNDGEIAAVFNVPLS 138
Cdd:cd18877  92 GGWSyTTVLASAPEPLPVRPANEESVELRWVPLD 125

Nucleoside diphosphate-linked moiety X)) motif 19; Acyl CoA diphosphohydrolase (also known as NUDIX (nucleoside diphosphate linked moiety X))-type motif 10; Nudt19; testosterone-regulated protein rp2) has activity towards CoA, oxidized CoA and a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. CoA is the major acyl carrier in mammals and a key cofactor in energy metabolism. Dynamic regulation of CoA in different tissues and organs supports metabolic flexibility. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598949  29 AAVLVPITR-SDDPELVLTLRAAGLSTHGGEVAFPGGRRDPEDADLVRTALREAEEEIALPPG 90
Cdd:cd18870   2 AATVILLRDgADGLEVLLLRRSSTMSFMPGAYVFPGGRVDPADRDAPWAGLLPPDVASASRPG 64

thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a bifunctional enzyme composed of a C-terminal thiamine pyrophosphokinase domain, which transfers pyrophosphate from ATP to thiamine and an N-terminal NUDIX hydrolase domain that converts oxidized derivatives of thiamine diphosphate (oxothiamine and oxythiamine) to their respective monophosphates. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases 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 _ "house-cleaning" enzymes. Substrate specificity is used to define 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598949  37 RSDDPELVLTLRAAGLSTHGGE----VAfpGGRRDPEDadLVRTALREAEEEIALPPGLVE----VVGPLSTLVSRHGIE 108
Cdd:cd03676  17 DGDGLRLWVARRSATKATYPGKldnlVA--GGVPAGES--PLETLVREAEEEAGLPEDLARqarpAAGRVSYFYRSDEGG 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15598949 109 VTPYVAFI-----PDFVEYQPNDGEIAavfnvplSFFRDDPREVTHRI 151
Cdd:cd03676  93 LQPEVLYVydlelPEDFVPKPQDGEVE-------SFELMSVDEVLEAL 133

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
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598949  62 PGGRRDPeDADLVRTALREAEEEIALPPGLVEVVGPLSTLVSRHGIEVTPYVA 114
Cdd:cd03674  30 PGGHVEP-DEDPLEAALREAREETGLDVELLSPLSPDPLDIDVHPIPANPGEP 81