NCBI Conserved Domain Search

isopentenyl-diphosphate Delta-isomerase;

Pssm-ID: 235156 [Multi-domain] Cd Length: 184 Bit Score: 330.39 E-value: 1.57e-117

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAV 80
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  81 IRRCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTNSALQINDDEVMDYQWCDLADVLHGIDATPWAFSP 160
Cdd:PRK03759  83 IRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWVDPADLLRAVDATPWAFSP 162

                        170       180
                 ....*....|....*....|..
gi 447115534 161 WMVMQAANSEARKLLSAFAQHN 182
Cdd:PRK03759 163 WMVLQAANLEARELLLAFAQRN 184

Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the NUDIX hydrolase superfamily, is a key enzyme in the isoprenoid biosynthetic pathway. Isoprenoids comprise a large family of natural products including sterols, carotenoids, dolichols and prenylated proteins. These compounds are synthesized from two precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IPP isomerase catalyzes the interconversion of IPP and DMAPP by a stereoselective antarafacial transposition of hydrogen. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N-terminus), the core structure is highly conserved.

Pssm-ID: 467529 [Multi-domain] Cd Length: 162 Bit Score: 250.88 E-value: 1.96e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   5 HVILLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRC 84
Cdd:cd02885    1 EVILVDEDDNPIGTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  85 RYELGVEITPPESIyPDFRYRATDPNGIVENEVCPVFAARTNSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd02885   81 REELGIPVCDLEEL-PRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEELRELLAATPEAFTPWFRL 159


                 ...
gi 447115534 165 QAA 167
Cdd:cd02885  160 ILE 162

Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis

Pssm-ID: 441052 [Multi-domain] Cd Length: 162 Bit Score: 232.40 E-value: 4.65e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   3 TEHVILLNAQGVPTGTLEKYAAHtADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIR 82
Cdd:COG1443    1 EELVDLVDEDGRPIGTAERAEVH-RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  83 RCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTNSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWM 162
Cdd:COG1443   80 ELEEELGITVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAGPEAFTPWF 159


                 ...
gi 447115534 163 VMQ 165
Cdd:COG1443  160 RLY 162

isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two non-homologous families of the enzyme isopentenyl-diphosphate delta-isomerase (IPP isomerase). IPP is an essential building block for many compounds, including enzyme cofactors, sterols, and prenyl groups. This inzyme interconverts isopentenyl diphosphate and dimethylallyl diphosphate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

Pssm-ID: 273998 [Multi-domain] Cd Length: 158 Bit Score: 201.03 E-value: 8.47e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534    6 VILLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGEsnEDAVIRRCR 85
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLPGE--LEAAIRRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   86 YELGVEITP-PESIYPDFRYRATD-PNGivENEVCPVFAARTNSALQINdDEVMDYQWCDLaDVLHGIDATPWA-FSPWM 162
Cdd:TIGR02150  79 HELGIPADDvPLTVLPRFSYRARDdAWG--EHELCPVFFARANVDLNPN-PEVAEYRWVSL-EELKEILAKPWAgFSPWF 154


                  ....
gi 447115534  163 VMQA 166
Cdd:TIGR02150 155 RIQA 158

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.

Pssm-ID: 467574 [Multi-domain] Cd Length: 142 Bit Score: 88.00 E-value: 1.22e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   9 LNAQGVPTGTLEKYAAHtADTLLHLAFSSWLFNAK-GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04692    4 VDEDGRPIGVATRSEVH-RQGLWHRTVHVWLVNPEeGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELEEE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447115534  88 LGVEITPPESIY-PDFRYRATDPNGIvENEVCPVFAARTN---SALQINDDEV 136
Cdd:cd04692   83 LGLTVSPEDLIFlGVIREEVIGGDFI-DNEFVHVYLYETDrplEEFKLQPEEV 134

isopentenyl-diphosphate delta-isomerase

Pssm-ID: 215303 [Multi-domain] Cd Length: 247 Bit Score: 90.56 E-value: 1.36e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   1 MQTEHVILLNAQGVPTGTLEKYAAH-----TADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLG-E 74
Cdd:PLN02552  20 MFEDECILVDENDNVVGHDSKYNCHlfekiEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTFPLVWTNTCCSHPLYGqD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  75 SNE----------------DAVIRRCRYELGV--EITPPESIYP----------DFRYRATDPNGivENEVCPVFAARTN 126
Cdd:PLN02552 100 PNEvdreselidgnvlgvkNAAQRKLLHELGIpaEDVPVDQFTFltrlhykaadDVTHGPDGKWG--EHELDYLLFIRPV 177

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 447115534 127 SALQI--NDDEVMDYQWCDLADVLHGIDATP-WAFSPW 161
Cdd:PLN02552 178 RDVKVnpNPDEVADVKYVNREELKEMMRKESgLKLSPW 215

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.

Pssm-ID: 467575 [Multi-domain] Cd Length: 157 Bit Score: 88.35 E-value: 1.48e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   8 LLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04693    5 LYDENRNKTGRTHRRGEPLPEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLEAAIRELKEE 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447115534  88 LGVEITpPESIYPDFRYRatDPNGIVEnevcpVFAARTN---SALQINDDEVMDYQWCDLADVLHGIDA 153
Cdd:cd04693   85 LGIDLD-ADELRPILTIR--FDNGFDD-----IYLFRKDvdiEDLTLQKEEVQDVKWVTLEEILEMIES 145

NUDIX domain;

Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 79.83 E-value: 1.78e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   30 LLHLAFSSWLFNAKGQLLVTRRalSKKAWPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDP 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRR--SKKPFPGWWS-LPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 447115534  110 NGIVENEVCPVFAARTNSALQINDD-EVMDYQWCDLADVL-HGIDATPWAFSPWM 162
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLlLKLAPGDRKLLPWL 132

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.

Pssm-ID: 467578 [Multi-domain] Cd Length: 157 Bit Score: 56.47 E-value: 1.71e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  30 LLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpDFRYratdp 109
Cdd:cd04697   24 LIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEEELGIDGVPLRPLF-TFYY----- 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447115534 110 ngivENEVCPV----FAARTNSALQINDDEVMDYQWCDLADVLhgIDATPWAFSP 160
Cdd:cd04697   98 ----EDDRSRVwgalFECVYDGPLKLQPEEVAEVDWMSEDEIL--QAARGEEFTP 146

NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus radiodurans protein DR_0079 is one of 21 NUDIX hydrolases that it encodes, and it has been observed to have a marked preference for cytosine ribonucleoside 5'-diphosphate (CDP) and cytosine ribonucleoside 5'-triphosphate (CTP), and for their corresponding deoxyribose nucleotides, dCDP and dCTP, to a lesser degree. Members of the NUDIX hydrolase superfamily catalyze 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 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.

Pssm-ID: 467602 [Multi-domain] Cd Length: 121 Bit Score: 55.68 E-value: 1.92e-10

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447115534  39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITP 94
Cdd:cd24154    9 LINSQGQLWIPRRTADKRIFPLALDMSVGGHVSSGETYEQAFVRELQEELNLDLDQ 64

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.

Pssm-ID: 467528 [Multi-domain] Cd Length: 106 Bit Score: 53.56 E-value: 8.71e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  39 LFNAKGQLLVTRRalSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfrYRATDPNGIVENEVC 118
Cdd:cd02883    7 VFDDEGRVLLVRR--SDGPGPGGW-ELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLG----VYEFPDPDEGRHVVV 79

                         90       100
                 ....*....|....*....|....*..
gi 447115534 119 PVFAARTNS--ALQINDDEVMDYQWCD 143
Cdd:cd02883   80 LVFLARVVGgePPPLDDEEISEVRWVP 106

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.

Pssm-ID: 467572 [Multi-domain] Cd Length: 123 Bit Score: 53.31 E-value: 1.46e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  38 WLFNAKGQLLVTRRAlSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITpPESIYPDFRYRAT---DPNGI 112
Cdd:cd04690    6 VIIIKDGRLLLVRKR-GTDAFylPG-------GKREPGETPLQALVRELKEELGLDLD-PDSLRFLGTFEAPaanEPGTT 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447115534 113 VENEvcpVFAARTNSALQInDDEVMDYQWCDLAD 146
Cdd:cd04690   77 VRMT---CFTADYDGEPQP-AAEIEELRWLDPAD 106

Nudix hydrolase homolog

Pssm-ID: 215425 [Multi-domain] Cd Length: 770 Bit Score: 55.21 E-value: 3.23e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTLLHLAFSSWLF-NAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDA 79
Cdd:PLN02791   1 MMEEHLDVLTAAGEKTGVSKPRGEVHRDGDYHRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLS 80

                         90
                 ....*....|.
gi 447115534  80 VIRRCRYELGV 90
Cdd:PLN02791  81 AQRELEEELGI 91

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.

Pssm-ID: 467564 [Multi-domain] Cd Length: 135 Bit Score: 50.26 E-value: 2.65e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  44 GQLLVTRRAL--SKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEItppesiyPDFRYRATDPN-----GIVE 114
Cdd:cd04681   17 GEILFVRRAKepGKGKLdlPG-------GFVDPGESAEEALRRELREELGLKI-------PKLRYLCSLPNtylykGITY 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447115534 115 NEVCPVFAAR--TNSALQINDDEVMDYQWCDLADV 147
Cdd:cd04681   83 KTCDLFFTAEldEKPKLKKAEDEVAELEWLDLEEI 117

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

Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 49.26 E-value: 6.84e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  38 WLFNAKGQLLVTRRAlSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfryRATDPNGIVENEV 117
Cdd:COG0494   19 VLLDDDGRVLLVRRY-RYGVGPGLW-EFPGGKIEPGESPEEAALRELREETGLTAEDLELLG-----ELPSPGYTDEKVH 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 447115534 118 cpVFAAR---TNSALQIND-DEVMDYQWCDLADVLHGIDA 153
Cdd:COG0494   92 --VFLARglgPGEEVGLDDeDEFIEVRWVPLDEALALVTA 129

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];

Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 48.44 E-value: 8.53e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  39 LFNAKGQLLVTRRAlsKKAWPGVWTNsVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfRYRATDPngivENEVC 118
Cdd:COG1051   13 IFRKDGRVLLVRRA--DEPGKGLWAL-PGGKVEPGETPEEAALRELREETGLEVEVLELLG---VFDHPDR----GHVVS 82

                         90       100
                 ....*....|....*....|....*....
gi 447115534 119 PVFAARTNSALQINDDEVMDYQWCDLADV 147
Cdd:COG1051   83 VAFLAEVLSGEPRADDEIDEARWFPLDEL 111

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze 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 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.

Pssm-ID: 467576 [Multi-domain] Cd Length: 135 Bit Score: 48.06 E-value: 1.83e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  44 GQLLVTRRALSKKAWPGVWtnsVC--GHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPNGIVENE----- 116
Cdd:cd04694   14 DRVLLTRRAKHMRTFPGVW---VPpgGHVELGESLLEAGLRELQEETGLEVSDIQSLSLLGLWESVYPTLLSIGLpkrhh 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447115534 117 VCPVFAARTNSA------LQINDDEVMDYQWCDLADVLHGIDAT 154
Cdd:cd04694   91 IVVYYLVKLSEShenqeqLKLQEDEVDAAVWLPKSLLAKLLEAE 134

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.

Pssm-ID: 467559 [Multi-domain] Cd Length: 144 Bit Score: 47.01 E-value: 4.75e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  28 DTLLHLAFSSWLFNAKGQLLvtrraLSKKAWPGVWTNSVcGHPQLGESNEDAVIRRCRYELGVEITPPESI----YPDFR 103
Cdd:cd04676   13 ELLFTPSVAAVILNEDGRIL-----LQRKGGLGLWSLPA-GAIEPGEHPAEAVIREVREETGLLVKPTRLLgvfgGKEFR 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447115534 104 YraTDPNG-IVENEVCPVFAARTNSALQINDDEVMDYQWCDLAD 146
Cdd:cd04676   87 Y--TYPNGdQVEYTVIAFKCVVTGGTLNAIDGETSELRYFSRTQ 128

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.

Pssm-ID: 467560 [Multi-domain] Cd Length: 137 Bit Score: 45.97 E-value: 1.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  39 LFNAKGQLLvtrraLSKKAWPGVWtnsvcGHP----QLGESNEDAVIRRCRYELGVEITPPE--SIY--PDFRYRAtdPN 110
Cdd:cd04677   19 ILNEQGRIL-----LQKRTDTGDW-----GLPggamELGESLEETARREVFEETGLTVEELEllGVYsgKDLYYTY--PN 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447115534 111 GIVENEVCPVFAAR-TNSALQINDDEVMDYQWCDLAD 146
Cdd:cd04677   87 GDEVYNVTAVYLVRdVSGELKVDDEESLELRFFSLDE 123

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.

Pssm-ID: 467531 [Multi-domain] Cd Length: 123 Bit Score: 43.21 E-value: 7.66e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  44 GQLLVTRRAlSKKAWPGVWtnsvcghpQL-------GESNEDAVIRRCRYELGVEITPPESI------YPDFR-----YR 105
Cdd:cd03425   12 GRVLIAQRP-EGKHLAGLW--------EFpggkvepGETPEQALVRELREELGIEVEVGEPLgtvehdYPDFHvrlhvYL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447115534 106 ATDPNGivenevcpVFAARTNSALQ-INDDEVMDYQWCDlADV 147
Cdd:cd03425   83 CTLWSG--------EPQLLEHQELRwVTPEELDDLDWLP-ADI 116

dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate,the second step in the pterin branch of the folate synthesis pathway in bacteria. Members of the NUDIX hydrolase superfamily catalyze 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 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.

Pssm-ID: 467549 [Multi-domain] Cd Length: 132 Bit Score: 41.08 E-value: 5.08e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  41 NAKGQLLVTRRALSkkawPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITP-------PESIYPDFryRATDPNGIV 113
Cdd:cd04664   11 DEEGEVLLLKRTDD----GGFWQ-SVTGGIEDGETPWQAALRELKEETGLDPLElqlidlnVSNFYEIF--DDWRPGVTV 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447115534 114 ENEvcPVFAARTNSALQIN-DDEVMDYQWCDLADVL 148
Cdd:cd04664   84 NTE--HVFAVEVPEEQPIRlSPEHTDYRWLPYEEAA 117

NUDIX hydrolase YfcD; Provisional

Pssm-ID: 185291 [Multi-domain] Cd Length: 180 Bit Score: 41.71 E-value: 6.37e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  27 ADTLLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESiYPDFRYra 106
Cdd:PRK15393  32 AQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQLLESARREAEEELGIAGVPFAE-HGQFYF-- 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447115534 107 tdpngivENEVCPV----FAARTNSALQINDDEVMDYQWCDLADVLHGIDA-TP---WAFSPWMVMQAANSEARK 173
Cdd:PRK15393 109 -------EDENCRVwgalFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEfTPdslKALALWLTRNAKNEAVET 176

diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX (nucleoside diphosphate-linked moiety X)) motif 2/Nudt2, is a member of the NUDIX hydrolase superfamily. Ap4A hydrolases are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one subfamily and fungi/animals/archaea enzymes, represented by this subfamily, fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val) that functions as a metal binding and catalytic site, and a required divalent cation, Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variation. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.

Pssm-ID: 467534 [Multi-domain] Cd Length: 132 Bit Score: 39.84 E-value: 1.54e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  68 GHPQLGESNEDAVIRRCRYELGVEItppESIYPDFRYRAT-DPNGIVENEVcpV-FAARTNSALQIN-DDEVMDYQWCDL 144
Cdd:cd03428   35 GHVEPGESELETALRETKEETGLTV---DDLPPGFRETLTySFKEGVEKTV--VyFLAELTPDVEVKlSEEHQDYKWLPY 109


                 ....
gi 447115534 145 ADVL 148
Cdd:cd03428  110 EEAL 113

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.

Pssm-ID: 467586 [Multi-domain] Cd Length: 125 Bit Score: 39.58 E-value: 1.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  40 FNAKGQLLVTRralSKKaWPGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITP------PESIYPDFRYRatdPNGIV 113
Cdd:cd18874   10 FNPDGKVLLVR---SHK-WNDLYGIP-GGKVEWGETLEEALKREVKEETGLDITDirfilvQESINSEEFHK---PAHFV 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447115534 114 ENEvcpvFAARTNSALQINDDEVMDYQWCDLADVL 148
Cdd:cd18874   82 FVD----YLARTDSSEVVLNEEAVEYLWVEPEEAL 112

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.

Pssm-ID: 467542 [Multi-domain] Cd Length: 130 Bit Score: 39.16 E-value: 2.79e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  32 HLAFSSWLFNAKGQ--LLVTRRALSKKAWPGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITP--PESIYPdfryRAT 107
Cdd:cd03674    1 HFTASAFVVNPDRGkvLLVHHRKLGRWLQPG-------GHVEPDEDPLEAALREAREETGLDVELlsPLSPDP----LDI 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 447115534 108 DPNGIVENEVCP-------VFAART-NSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03674   70 DVHPIPANPGEPahlhldvRYLAVAdGDEALRKSDESSDVRWFPLDELEE 119

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.

Pssm-ID: 467570 [Multi-domain] Cd Length: 130 Bit Score: 39.07 E-value: 3.13e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  44 GQLLVTRrALSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITPP------ESIypdFRYratdpNGIVEN 115
Cdd:cd04688   13 GKVLLAR-GEDDDYYrlPG-------GRVEFGETSEDALVREFKEELGVEVEVVrllfvvENF---FTY-----DGKPFH 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447115534 116 EVCPVFAAR--TNSALQIN------DDEVMDYQWCDLADvLHGIDATP 155
Cdd:cd04688   77 EIGFYYLVElsDEALYEQDiffleeDGEKLEFRWIPLEE-LDEIDLYP 123

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.

Pssm-ID: 467544 Cd Length: 153 Bit Score: 38.63 E-value: 4.41e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  44 GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVE------ITPPESIypdFRYRATDPNGIVENEV 117
Cdd:cd03676   21 LRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLPedlarqARPAAGR---VSYFYRSDEGGLQPEV 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447115534 118 -----CPVFAARTNsalQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd03676   98 lyvydLELPEDFVP---KPQDGEVESFELMSVDEVLEALRAGEFKPNCALVM 146

plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the NUDIX hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.

Pssm-ID: 467539 [Multi-domain] Cd Length: 147 Bit Score: 38.32 E-value: 6.04e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  39 LFNAKGQLLVTRRALSKKAWpgvwtnsvcGHPQ----LGESNEDAVIRrcryELGVEI-TPPESI-----YPD-FRYRAt 107
Cdd:cd03671   10 LFNRDGQVLVGRRIDVPGAW---------QFPQggidEGEDPEEAALR----ELYEETgLSPEDVeiiaeTPDwLTYDL- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447115534 108 dPNGIVENEVCPV--------FAARTN---SALQINDD---EVMDYQWCDLADVL 148
Cdd:cd03671   76 -PEDLIRKGWGGKyrgqkqkwFLFRFTgddSEINLDTHehpEFDAWRWVDLEELP 129

NUDIX hydrolase subfamily; Nucleoside triphosphatase NudI catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). It is a members of the NUDIX hydrolase superfamily which catalyze 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 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.

Pssm-ID: 467577 [Multi-domain] Cd Length: 134 Bit Score: 37.99 E-value: 7.53e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQlGESNEDAVIRRCRYELGVEIT----PPESIYPDFRYRaTDPNGIVE 114
Cdd:cd04696    8 LIENEGCYLLCKMADDRGVFPGQWALSGGGVEP-GERIEEALRREIREELGEQLIlsdiTPWTFRDDIRIK-TYPDGRQE 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447115534 115 nEVCPVF----AARTNSALQINdDEVMDYQWCDLADV 147
Cdd:cd04696   86 -EIYMIYlifdCVSANRDVCIN-DEFQDYAWVKPADL 120

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.

Pssm-ID: 467595 [Multi-domain] Cd Length: 125 Bit Score: 37.78 E-value: 7.97e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  56 KAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESI--YPDFRYratdpngiveNEVCPVFAARTNSALQINd 133
Cdd:cd18884   28 KAWPEGWYGLVTGFLEAGESPEEAVLREVKEELGLDGHEAKFIghYAFPER----------NQLIIAYHVRARGNVKLN- 96

                         90       100
                 ....*....|....*....|....*
gi 447115534 134 DEVMDYQWCDLADVlhgidaTPWAF 158
Cdd:cd18884   97 EELDDYKIVPIDKL------RPWPF 115

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.

Pssm-ID: 467532 [Multi-domain] Cd Length: 158 Bit Score: 37.86 E-value: 1.00e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  45 QLLVTRRALSKKAWPGvwtnSVC---GHPQLG-ESNEDAVIRRCRYELGVeitPPESI-----YPDFRyratDPNGIVen 115
Cdd:cd03426   17 HVLLTKRASHLRSHPG----QIAfpgGKREPGdESPVETALRETEEEIGL---PPESVevlgrLDPLY----TPSGFV-- 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447115534 116 eVCP-VFAARTNSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03426   84 -VTPfVGLLDDPPPLRPNPDEVAEVFTVPLSFLLD 117

ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.

Pssm-ID: 467573 [Multi-domain] Cd Length: 122 Bit Score: 36.12 E-value: 2.44e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447115534  43 KGQLLVTRRALSKKAwpGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITPPESIypDFRYRatdPNGIVENEVCPVFA 122
Cdd:cd04691   11 EGKVLLVKRAYGPGK--GRWTLP-GGFVEEGETLDEAIVREVLEETGIDAKPVGII--GVRSG---VIRDGKSDNYVVFL 82

                         90       100
                 ....*....|....*....|....*..
gi 447115534 123 AR-TNSALQINDDEVMDYQWCDLADVL 148
Cdd:cd04691   83 LEyVGGEPKPDERENSEAGFLTLEEAL 109