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Conserved domains on  [gi|1844652981|gb|QJY12705|]
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isopentenyl-diphosphate Delta-isomerase [Shigella sonnei]

Protein Classification

isopentenyl-diphosphate delta-isomerase( domain architecture ID 10012074)

isopentenyl-diphosphate delta-isomerase catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), a key step in the isoprenoid biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
1-182 1.91e-118

isopentenyl-diphosphate Delta-isomerase;


:

Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 332.70  E-value: 1.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAV 80
Cdd:PRK03759    3 METELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  81 IRRCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSP 160
Cdd:PRK03759   83 IRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWVDPADLLRAVDATPWAFSP 162
                         170       180
                  ....*....|....*....|..
gi 1844652981 161 WMVMQAANSEARKLLSAFAQHN 182
Cdd:PRK03759  163 WMVLQAANLEARELLLAFAQRN 184
 
Name Accession Description Interval E-value
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
1-182 1.91e-118

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 332.70  E-value: 1.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAV 80
Cdd:PRK03759    3 METELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  81 IRRCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSP 160
Cdd:PRK03759   83 IRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWVDPADLLRAVDATPWAFSP 162
                         170       180
                  ....*....|....*....|..
gi 1844652981 161 WMVMQAANSEARKLLSAFAQHN 182
Cdd:PRK03759  163 WMVLQAANLEARELLLAFAQRN 184
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
5-167 9.08e-86

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: 249.33  E-value: 9.08e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   5 HVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRC 84
Cdd:cd02885     1 EVILVDEDDNPIGTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  85 RYELGVEITPPESIyPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd02885    81 REELGIPVCDLEEL-PRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEELRELLAATPEAFTPWFRL 159

                  ...
gi 1844652981 165 QAA 167
Cdd:cd02885   160 ILE 162
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
3-165 8.38e-78

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: 228.93  E-value: 8.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   3 TEHVILLNAQGVPTGTLEKYAAHtADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIR 82
Cdd:COG1443     1 EELVDLVDEDGRPIGTAERAEVH-RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  83 RCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWM 162
Cdd:COG1443    80 ELEEELGITVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAGPEAFTPWF 159

                  ...
gi 1844652981 163 VMQ 165
Cdd:COG1443   160 RLY 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
6-166 6.92e-66

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: 198.72  E-value: 6.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   6 VILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGEsnEDAVIRRCR 85
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLPGE--LEAAIRRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  86 YELGVEITP-PESIYPDFRYRATD-PNGivENEVCPVFAARTTSALQINdDEVMDYQWCDLaDVLHGIDATPWA-FSPWM 162
Cdd:TIGR02150  79 HELGIPADDvPLTVLPRFSYRARDdAWG--EHELCPVFFARANVDLNPN-PEVAEYRWVSL-EELKEILAKPWAgFSPWF 154

                  ....
gi 1844652981 163 VMQA 166
Cdd:TIGR02150 155 RIQA 158
NUDIX pfam00293
NUDIX domain;
30-162 2.25e-19

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 79.45  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  30 RLHLAFSSWLFNAKGQLLVTRRalSKKAWPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDP 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRR--SKKPFPGWWS-LPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844652981 110 NGIVENEVCPVFAARTTSALQINDD-EVMDYQWCDLADVL-HGIDATPWAFSPWM 162
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLlLKLAPGDRKLLPWL 132
 
Name Accession Description Interval E-value
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
1-182 1.91e-118

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 332.70  E-value: 1.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAV 80
Cdd:PRK03759    3 METELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  81 IRRCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSP 160
Cdd:PRK03759   83 IRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWVDPADLLRAVDATPWAFSP 162
                         170       180
                  ....*....|....*....|..
gi 1844652981 161 WMVMQAANSEARKLLSAFAQHN 182
Cdd:PRK03759  163 WMVLQAANLEARELLLAFAQRN 184
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
5-167 9.08e-86

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: 249.33  E-value: 9.08e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   5 HVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRC 84
Cdd:cd02885     1 EVILVDEDDNPIGTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  85 RYELGVEITPPESIyPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd02885    81 REELGIPVCDLEEL-PRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEELRELLAATPEAFTPWFRL 159

                  ...
gi 1844652981 165 QAA 167
Cdd:cd02885   160 ILE 162
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
3-165 8.38e-78

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: 228.93  E-value: 8.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   3 TEHVILLNAQGVPTGTLEKYAAHtADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIR 82
Cdd:COG1443     1 EELVDLVDEDGRPIGTAERAEVH-RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  83 RCRYELGVEITPPESIYPDFRYRATDPNGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWM 162
Cdd:COG1443    80 ELEEELGITVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAGPEAFTPWF 159

                  ...
gi 1844652981 163 VMQ 165
Cdd:COG1443   160 RLY 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
6-166 6.92e-66

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: 198.72  E-value: 6.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   6 VILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGEsnEDAVIRRCR 85
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLPGE--LEAAIRRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  86 YELGVEITP-PESIYPDFRYRATD-PNGivENEVCPVFAARTTSALQINdDEVMDYQWCDLaDVLHGIDATPWA-FSPWM 162
Cdd:TIGR02150  79 HELGIPADDvPLTVLPRFSYRARDdAWG--EHELCPVFFARANVDLNPN-PEVAEYRWVSL-EELKEILAKPWAgFSPWF 154

                  ....
gi 1844652981 163 VMQA 166
Cdd:TIGR02150 155 RIQA 158
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
1-161 5.85e-22

isopentenyl-diphosphate delta-isomerase


Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 89.02  E-value: 5.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   1 MQTEHVILLNAQGVPTGTLEKYAAH-----TADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLG-E 74
Cdd:PLN02552   20 MFEDECILVDENDNVVGHDSKYNCHlfekiEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTFPLVWTNTCCSHPLYGqD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  75 SNE----------------DAVIRRCRYELGV--EITPPESIYP----------DFRYRATDPNGivENEVCPVFAARTT 126
Cdd:PLN02552  100 PNEvdreselidgnvlgvkNAAQRKLLHELGIpaEDVPVDQFTFltrlhykaadDVTHGPDGKWG--EHELDYLLFIRPV 177
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1844652981 127 SALQI--NDDEVMDYQWCDLADVLHGIDATP-WAFSPW 161
Cdd:PLN02552  178 RDVKVnpNPDEVADVKYVNREELKEMMRKESgLKLSPW 215
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
8-153 2.17e-21

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: 85.27  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   8 LLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04693     5 LYDENRNKTGRTHRRGEPLPEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLEAAIRELKEE 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844652981  88 LGVEITpPESIYPDFRYRatDPNGIVEnevcpVFAARTT---SALQINDDEVMDYQWCDLADVLHGIDA 153
Cdd:cd04693    85 LGIDLD-ADELRPILTIR--FDNGFDD-----IYLFRKDvdiEDLTLQKEEVQDVKWVTLEEILEMIES 145
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-136 1.65e-20

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: 82.61  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   9 LNAQGVPTGTLEKYAAHtADTRLHLAFSSWLFNAK-GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04692     4 VDEDGRPIGVATRSEVH-RQGLWHRTVHVWLVNPEeGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELEEE 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1844652981  88 LGVEITPPESIY-PDFRYRATDPNGIvENEVCPVFAARTT---SALQINDDEV 136
Cdd:cd04692    83 LGLTVSPEDLIFlGVIREEVIGGDFI-DNEFVHVYLYETDrplEEFKLQPEEV 134
NUDIX pfam00293
NUDIX domain;
30-162 2.25e-19

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 79.45  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  30 RLHLAFSSWLFNAKGQLLVTRRalSKKAWPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDP 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRR--SKKPFPGWWS-LPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844652981 110 NGIVENEVCPVFAARTTSALQINDD-EVMDYQWCDLADVL-HGIDATPWAFSPWM 162
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLlLKLAPGDRKLLPWL 132
NUDIX_DR0079 cd24154
NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus ...
39-94 1.86e-10

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: 1.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844652981  39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITP 94
Cdd:cd24154     9 LINSQGQLWIPRRTADKRIFPLALDMSVGGHVSSGETYEQAFVRELQEELNLDLDQ 64
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
38-146 6.79e-10

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: 54.08  E-value: 6.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  38 WLFNAKGQLLVTRRAlSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITpPESIYPDFRYRAT---DPNGI 112
Cdd:cd04690     6 VIIIKDGRLLLVRKR-GTDAFylPG-------GKREPGETPLQALVRELKEELGLDLD-PDSLRFLGTFEAPaanEPGTT 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1844652981 113 VENEvcpVFAARTTSALQInDDEVMDYQWCDLAD 146
Cdd:cd04690    77 VRMT---CFTADYDGEPQP-AAEIEELRWLDPAD 106
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
39-143 7.45e-10

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: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLVTRRalSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfrYRATDPNGIVENEVC 118
Cdd:cd02883     7 VFDDEGRVLLVRR--SDGPGPGGW-ELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLG----VYEFPDPDEGRHVVV 79
                          90       100
                  ....*....|....*....|....*..
gi 1844652981 119 PVFAARTTS--ALQINDDEVMDYQWCD 143
Cdd:cd02883    80 LVFLARVVGgePPPLDDEEISEVRWVP 106
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
39-160 8.14e-10

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: 54.93  E-value: 8.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpDFRYratdpngivENEVC 118
Cdd:cd04697    33 VRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEEELGIDGVPLRPLF-TFYY---------EDDRS 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1844652981 119 PV----FAARTTSALQINDDEVMDYQWCDLADVLhgIDATPWAFSP 160
Cdd:cd04697   103 RVwgalFECVYDGPLKLQPEEVAEVDWMSEDEIL--QAARGEEFTP 146
PLN02791 PLN02791
Nudix hydrolase homolog
1-90 1.66e-09

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 55.98  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981   1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLF-NAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDA 79
Cdd:PLN02791    1 MMEEHLDVLTAAGEKTGVSKPRGEVHRDGDYHRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLS 80
                          90
                  ....*....|.
gi 1844652981  80 VIRRCRYELGV 90
Cdd:PLN02791   81 AQRELEEELGI 91
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
44-147 2.94e-08

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: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  44 GQLLVTRRAL--SKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEItppesiyPDFRYRATDPN-----GIVE 114
Cdd:cd04681    17 GEILFVRRAKepGKGKLdlPG-------GFVDPGESAEEALRRELREELGLKI-------PKLRYLCSLPNtylykGITY 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844652981 115 NEVCPVFAAR--TTSALQINDDEVMDYQWCDLADV 147
Cdd:cd04681    83 KTCDLFFTAEldEKPKLKKAEDEVAELEWLDLEEI 117
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
38-153 3.06e-08

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: 50.03  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  38 WLFNAKGQLLVTRRAlSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfryRATDPNGIVENEV 117
Cdd:COG0494    19 VLLDDDGRVLLVRRY-RYGVGPGLW-EFPGGKIEPGESPEEAALRELREETGLTAEDLELLG-----ELPSPGYTDEKVH 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1844652981 118 cpVFAARTTSALQI----NDDEVMDYQWCDLADVLHGIDA 153
Cdd:COG0494    92 --VFLARGLGPGEEvgldDEDEFIEVRWVPLDEALALVTA 129
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
39-147 4.85e-08

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 49.21  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLVTRRAlsKKAWPGVWTNsVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfRYRATDPngivENEVC 118
Cdd:COG1051    13 IFRKDGRVLLVRRA--DEPGKGLWAL-PGGKVEPGETPEEAALRELREETGLEVEVLELLG---VFDHPDR----GHVVS 82
                          90       100
                  ....*....|....*....|....*....
gi 1844652981 119 PVFAARTTSALQINDDEVMDYQWCDLADV 147
Cdd:COG1051    83 VAFLAEVLSGEPRADDEIDEARWFPLDEL 111
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
39-146 2.40e-07

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: 47.51  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLvtrraLSKKAWPGVWtnsvcGHP----QLGESNEDAVIRRCRYELGVEITPPE--SIY--PDFRYRAtdPN 110
Cdd:cd04677    19 ILNEQGRIL-----LQKRTDTGDW-----GLPggamELGESLEETARREVFEETGLTVEELEllGVYsgKDLYYTY--PN 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1844652981 111 GIVENEVCPVFAARTTS-ALQINDDEVMDYQWCDLAD 146
Cdd:cd04677    87 GDEVYNVTAVYLVRDVSgELKVDDEESLELRFFSLDE 123
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
44-154 3.44e-07

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: 47.29  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  44 GQLLVTRRALSKKAWPGVWtnsVC--GHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPNGIVENE----- 116
Cdd:cd04694    14 DRVLLTRRAKHMRTFPGVW---VPpgGHVELGESLLEAGLRELQEETGLEVSDIQSLSLLGLWESVYPTLLSIGLpkrhh 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1844652981 117 VCPVFAAR------TTSALQINDDEVMDYQWCDLADVLHGIDAT 154
Cdd:cd04694    91 IVVYYLVKlsesheNQEQLKLQEDEVDAAVWLPKSLLAKLLEAE 134
NUDIX_Hydrolase cd04676
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
39-146 8.70e-07

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: 46.24  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLvtrraLSKKAWPGVWTNSVcGHPQLGESNEDAVIRRCRYELGVEITPPESI----YPDFRYraTDPNGIVE 114
Cdd:cd04676    24 ILNEDGRIL-----LQRKGGLGLWSLPA-GAIEPGEHPAEAVIREVREETGLLVKPTRLLgvfgGKEFRY--TYPNGDQV 95
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1844652981 115 NEVCPVFAARTTS-ALQINDDEVMDYQWCDLAD 146
Cdd:cd04676    96 EYTVIAFKCVVTGgTLNAIDGETSELRYFSRTQ 128
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
41-148 3.24e-05

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: 41.85  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  41 NAKGQLLVTRRALSkkawPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITP-------PESIYPDFryRATDPNGIV 113
Cdd:cd04664    11 DEEGEVLLLKRTDD----GGFWQ-SVTGGIEDGETPWQAALRELKEETGLDPLElqlidlnVSNFYEIF--DDWRPGVTV 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1844652981 114 ENEvcPVFAARTTSALQIN-DDEVMDYQWCDLADVL 148
Cdd:cd04664    84 NTE--HVFAVEVPEEQPIRlSPEHTDYRWLPYEEAA 117
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
44-157 4.45e-05

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: 41.28  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  44 GQLLVTRRAlSKKAWPGVWtnsvcghpQL-------GESNEDAVIRRCRYELGVEITPPESI------YPDFR-----YR 105
Cdd:cd03425    12 GRVLIAQRP-EGKHLAGLW--------EFpggkvepGETPEQALVRELREELGIEVEVGEPLgtvehdYPDFHvrlhvYL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1844652981 106 ATdpngIVENEVCPVfaarttsalqinddEVMDYQWCDLADvlhgIDATPWA 157
Cdd:cd03425    83 CT----LWSGEPQLL--------------EHQELRWVTPEE----LDDLDWL 112
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
68-148 7.76e-05

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: 40.61  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  68 GHPQLGESNEDAVIRRCRYELGVEItppESIYPDFRYRAT-DPNGIVENEVcpV-FAARTTSALQIN-DDEVMDYQWCDL 144
Cdd:cd03428    35 GHVEPGESELETALRETKEETGLTV---DDLPPGFRETLTySFKEGVEKTV--VyFLAELTPDVEVKlSEEHQDYKWLPY 109

                  ....
gi 1844652981 145 ADVL 148
Cdd:cd03428   110 EEAL 113
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
32-149 9.08e-05

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: 40.32  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  32 HLAFSSWLFNAKGQ--LLVTRRALSKKAWPGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITP--PESIYPdfryRAT 107
Cdd:cd03674     1 HFTASAFVVNPDRGkvLLVHHRKLGRWLQPG-------GHVEPDEDPLEAALREAREETGLDVELlsPLSPDP----LDI 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1844652981 108 DPNGIVENEVCP-------VFAART-TSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03674    70 DVHPIPANPGEPahlhldvRYLAVAdGDEALRKSDESSDVRWFPLDELEE 119
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
40-148 1.95e-04

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: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  40 FNAKGQLLVTRralSKKaWPGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITP------PESIYPDFRYRatdPNGIV 113
Cdd:cd18874    10 FNPDGKVLLVR---SHK-WNDLYGIP-GGKVEWGETLEEALKREVKEETGLDITDirfilvQESINSEEFHK---PAHFV 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844652981 114 ENEvcpvFAARTTSALQINDDEVMDYQWCDLADVL 148
Cdd:cd18874    82 FVD----YLARTDSSEVVLNEEAVEYLWVEPEEAL 112
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
41-173 2.27e-04

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 40.17  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  41 NAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESiYPDFRYratdpngivENEVCPV 120
Cdd:PRK15393   46 DGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQLLESARREAEEELGIAGVPFAE-HGQFYF---------EDENCRV 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844652981 121 ----FAARTTSALQINDDEVMDYQWCDLADVLHGIDA-TP---WAFSPWMVMQAANSEARK 173
Cdd:PRK15393  116 wgalFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEfTPdslKALALWLTRNAKNEAVET 176
NUDIX_Hydrolase cd18884
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
56-158 2.74e-04

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: 38.93  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  56 KAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESI--YPDFRYratdpngiveNEVCPVFAARTTSALQINd 133
Cdd:cd18884    28 KAWPEGWYGLVTGFLEAGESPEEAVLREVKEELGLDGHEAKFIghYAFPER----------NQLIIAYHVRARGNVKLN- 96
                          90       100
                  ....*....|....*....|....*
gi 1844652981 134 DEVMDYQWCDLADVlhgidaTPWAF 158
Cdd:cd18884    97 EELDDYKIVPIDKL------RPWPF 115
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
44-155 3.63e-04

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: 38.68  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  44 GQLLVTRrALSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITPP------ESIypdFRYratdpNGIVEN 115
Cdd:cd04688    13 GKVLLAR-GEDDDYYrlPG-------GRVEFGETSEDALVREFKEELGVEVEVVrllfvvENF---FTY-----DGKPFH 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1844652981 116 EVCPVFAAR--TTSALQIN------DDEVMDYQWCDLADvLHGIDATP 155
Cdd:cd04688    77 EIGFYYLVElsDEALYEQDiffleeDGEKLEFRWIPLEE-LDEIDLYP 123
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
39-148 3.74e-04

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: 39.09  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLVTRRALSKKAWpgvwtnsvcGHPQ----LGESNEDAVIRrcryELGVEI-TPPESI-----YPD-FRYRAt 107
Cdd:cd03671    10 LFNRDGQVLVGRRIDVPGAW---------QFPQggidEGEDPEEAALR----ELYEETgLSPEDVeiiaeTPDwLTYDL- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844652981 108 dPNGIVENEVCPV--------FAARTT---SALQINDD---EVMDYQWCDLADVL 148
Cdd:cd03671    76 -PEDLIRKGWGGKyrgqkqkwFLFRFTgddSEINLDTHehpEFDAWRWVDLEELP 129
NUDIX_Tnr3_like cd03676
thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a ...
44-164 5.00e-04

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: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  44 GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVE------ITPPESIypdFRYRATDPNGIVENEV 117
Cdd:cd03676    21 LRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLPedlarqARPAAGR---VSYFYRSDEGGLQPEV 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1844652981 118 CPVFAARTTSAL--QINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd03676    98 LYVYDLELPEDFvpKPQDGEVESFELMSVDEVLEALRAGEFKPNCALVM 146
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
41-146 5.97e-04

Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC 3.6.1.-), also known as nucleoside diphosphate-linked moiety X)) motif 6/Nudt6, and similar proteins including peroxisomal coenzyme A diphosphatase/Nudt7 and mitochondrial coenzyme A diphosphatase/Nudt8. The Nudt6 gene overlaps and lies on the opposite strand from FGF2 gene, and is thought to be the FGF2 antisense gene. The two genes are independently transcribed, and their expression shows an inverse relationship, suggesting that this antisense transcript may regulate FGF2 expression. This gene has also been shown to have hormone-regulatory and antiproliferative actions in the pituitary that are independent of FGF2 expression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. 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: 467554 [Multi-domain]  Cd Length: 131  Bit Score: 38.29  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  41 NAKGQLLVTR-RALSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEiTPPESI-----YPDFRYRATDpngi 112
Cdd:cd04670    11 NENNEVLVVQeKYGGPGGWklPG-------GLVDPGEDIGEAAVREVFEETGID-TEFVSIlgfrhQHPGRFGKSD---- 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1844652981 113 veneVCPVFAAR--TTSALQINDDEVMDYQWCDLAD 146
Cdd:cd04670    79 ----LYFVCRLRplSDEEIKICPEEIAEAKWMPLEE 110
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
43-148 7.62e-04

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: 37.66  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  43 KGQLLVTRRALSKKAwpGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITPPESIypDFRYRatdPNGIVENEVCPVFA 122
Cdd:cd04691    11 EGKVLLVKRAYGPGK--GRWTLP-GGFVEEGETLDEAIVREVLEETGIDAKPVGII--GVRSG---VIRDGKSDNYVVFL 82
                          90       100
                  ....*....|....*....|....*..
gi 1844652981 123 ARTTSA-LQINDDEVMDYQWCDLADVL 148
Cdd:cd04691    83 LEYVGGePKPDERENSEAGFLTLEEAL 109
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
45-149 1.96e-03

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: 37.09  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  45 QLLVTRRALSKKAWPGvwtnSVC---GHPQLG-ESNEDAVIRRCRYELGVeitPPESI-----YPDFRyratDPNGIVen 115
Cdd:cd03426    17 HVLLTKRASHLRSHPG----QIAfpgGKREPGdESPVETALRETEEEIGL---PPESVevlgrLDPLY----TPSGFV-- 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844652981 116 eVCP-VFAARTTSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03426    84 -VTPfVGLLDDPPPLRPNPDEVAEVFTVPLSFLLD 117
NUDIX_NudI cd04696
NUDIX hydrolase subfamily; Nucleoside triphosphatase NudI catalyzes the hydrolysis of ...
39-147 3.47e-03

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: 36.06  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQlGESNEDAVIRRCRYELGVEIT----PPESIYPDFRYRaTDPNGIVE 114
Cdd:cd04696     8 LIENEGCYLLCKMADDRGVFPGQWALSGGGVEP-GERIEEALRREIREELGEQLIlsdiTPWTFRDDIRIK-TYPDGRQE 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844652981 115 N--EVCPVFAARTTSALQINDDEVMDYQWCDLADV 147
Cdd:cd04696    86 EiyMIYLIFDCVSANRDVCINDEFQDYAWVKPADL 120
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
43-147 5.90e-03

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467579 [Multi-domain]  Cd Length: 118  Bit Score: 35.29  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844652981  43 KGQLLVTRRAlskKAWPGVWTNsVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPD-FRYRATDPNGIVenevcpVF 121
Cdd:cd04699    12 NGRVLLLRRS---RAGAGEWEL-PGGRLEPGESPEEALKREVKEETGLDVSVGELLDTWtFELDPDKGVFIV------TY 81
                          90       100
                  ....*....|....*....|....*.
gi 1844652981 122 AARTTSALQINDDEVMDYQWCDLADV 147
Cdd:cd04699    82 LCRLVGGEVTLSDEHEEYEWVTPEEL 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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