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Conserved domains on  [gi|79514626|ref|NP_197148|]
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isopentenyl diphosphate isomerase 1 [Arabidopsis thaliana]

Protein Classification

isopentenyl-diphosphate delta-isomerase( domain architecture ID 10791402)

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

CATH:  3.90.79.10
EC:  5.3.3.2
Gene Ontology:  GO:0046872
PubMed:  9418296|15581572|16378245
SCOP:  3000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
 58-291 3.65e-162

isopentenyl-diphosphate delta-isomerase


:

Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 450.72  E-value: 3.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   58 TMTDSNDAGMDAVQRRLMFEDECILVDENDRVVGHDTKYNCHLMEKIEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTF 137
Cdd:PLN02552   3 TMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  138 PLVWTNTCCSHPLY--------RESELIEENVLGVRNAAQRKLFDELGIVAEDVPVDEFTPLGRMLYKAPSD------GK 203
Cdd:PLN02552  83 PLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdGK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  204 WGEHEVDYLLFI--VRDVKLQPNPDEVAEIKYVSREELKELVKKadagDEAVKLSPWFRLVVDNFLMKWWDHVEKGtiTE 281
Cdd:PLN02552 163 WGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKG--TE 236

                        250
                 ....*....|
gi 79514626  282 AADMKTIHKL 291
Cdd:PLN02552 237 AVDMKTIHKL 246
 
Name Accession Description Interval E-value
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
 58-291 3.65e-162

isopentenyl-diphosphate delta-isomerase


Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 450.72  E-value: 3.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   58 TMTDSNDAGMDAVQRRLMFEDECILVDENDRVVGHDTKYNCHLMEKIEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTF 137
Cdd:PLN02552   3 TMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  138 PLVWTNTCCSHPLY--------RESELIEENVLGVRNAAQRKLFDELGIVAEDVPVDEFTPLGRMLYKAPSD------GK 203
Cdd:PLN02552  83 PLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdGK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  204 WGEHEVDYLLFI--VRDVKLQPNPDEVAEIKYVSREELKELVKKadagDEAVKLSPWFRLVVDNFLMKWWDHVEKGtiTE 281
Cdd:PLN02552 163 WGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKG--TE 236

                        250
                 ....*....|
gi 79514626  282 AADMKTIHKL 291
Cdd:PLN02552 237 AVDMKTIHKL 246
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 79-264 1.69e-83

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: 247.79  E-value: 1.69e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  79 ECILVDENDRVVGHDTKYNCHLMEkieaeNLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYREselie 158
Cdd:cd02885   1 EVILVDEDDNPIGTAEKLEAHRKG-----TLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGE----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 159 envlGVRNAAQRKLFDELGIvaedvPVDEFTPLGRMLYKAPSDGKWGEHEVDYLLFIVRDVKLQPNPDEVAEIKYVSREE 238
Cdd:cd02885  71 ----GVEDAAQRRLREELGI-----PVCDLEELPRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEE 141

                       170       180
                ....*....|....*....|....*.
gi 79514626 239 LKELVKKADAgdeavKLSPWFRLVVD 264
Cdd:cd02885 142 LRELLAATPE-----AFTPWFRLILE 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
 80-263 3.26e-73

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: 221.83  E-value: 3.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626    80 CILVDENDRVVGHDTKYNCHLMEkieaeNLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYreseliee 159
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQE-----TPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLP-------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   160 nvlGVRNAAQRKLFDELGIVAEDVPvdeFTPLGRMLYKAPSDGkWGEHEVDYLLFIVRDVKLQPNPdEVAEIKYVSREEL 239
Cdd:TIGR02150  68 ---GELEAAIRRLRHELGIPADDVP---LTVLPRFSYRARDDA-WGEHELCPVFFARANVDLNPNP-EVAEYRWVSLEEL 139

                         170       180
                  ....*....|....*....|....
gi 79514626   240 KELVKKADAGdeavkLSPWFRLVV 263
Cdd:TIGR02150 140 KEILAKPWAG-----FSPWFRIQA 158
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 81-262 5.56e-56

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: 178.08  E-value: 5.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  81 ILVDENDRVVGHDTKYNCHlmekieAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYRESelieen 160
Cdd:COG1443   5 DLVDEDGRPIGTAERAEVH------RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGET------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 161 vlgVRNAAQRKLFDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHEVDYLLFIVRDVKLQPNPDEVAEIKYVSREELK 240
Cdd:COG1443  73 ---YEEAAVRELEEELGI----TVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELL 145

                       170       180
                ....*....|....*....|..
gi 79514626 241 ELVKKADAgdeavKLSPWFRLV 262
Cdd:COG1443 146 ALLEAGPE-----AFTPWFRLY 162
NUDIX pfam00293
NUDIX domain;
109-259 1.05e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 72.13  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   109 LLHRAFSVFLFNSKYELLLQQRSKTKvtfPLVWTNTCCSHPlyRESELIEEnvlgvrnAAQRKLFDELGIVAEDVPVdef 188
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKP---FPGWWSLPGGKV--EPGETPEE-------AARRELEEETGLEPELLEL--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79514626   189 tpLGRMLYKAPSDGKWG-EHEVDYLLFIVRDVKLQPNPD-EVAEIKYVSREELKELVKKADAGdeavKLSPWF 259
Cdd:pfam00293  66 --LGSLHYLAPFDGRFPdEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKLAPGDR----KLLPWL 132
 
Name Accession Description Interval E-value
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
 58-291 3.65e-162

isopentenyl-diphosphate delta-isomerase


Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 450.72  E-value: 3.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   58 TMTDSNDAGMDAVQRRLMFEDECILVDENDRVVGHDTKYNCHLMEKIEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTF 137
Cdd:PLN02552   3 TMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  138 PLVWTNTCCSHPLY--------RESELIEENVLGVRNAAQRKLFDELGIVAEDVPVDEFTPLGRMLYKAPSD------GK 203
Cdd:PLN02552  83 PLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdGK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  204 WGEHEVDYLLFI--VRDVKLQPNPDEVAEIKYVSREELKELVKKadagDEAVKLSPWFRLVVDNFLMKWWDHVEKGtiTE 281
Cdd:PLN02552 163 WGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKG--TE 236

                        250
                 ....*....|
gi 79514626  282 AADMKTIHKL 291
Cdd:PLN02552 237 AVDMKTIHKL 246
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 79-264 1.69e-83

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: 247.79  E-value: 1.69e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  79 ECILVDENDRVVGHDTKYNCHLMEkieaeNLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYREselie 158
Cdd:cd02885   1 EVILVDEDDNPIGTAEKLEAHRKG-----TLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGE----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 159 envlGVRNAAQRKLFDELGIvaedvPVDEFTPLGRMLYKAPSDGKWGEHEVDYLLFIVRDVKLQPNPDEVAEIKYVSREE 238
Cdd:cd02885  71 ----GVEDAAQRRLREELGI-----PVCDLEELPRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEE 141

                       170       180
                ....*....|....*....|....*.
gi 79514626 239 LKELVKKADAgdeavKLSPWFRLVVD 264
Cdd:cd02885 142 LRELLAATPE-----AFTPWFRLILE 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
 80-263 3.26e-73

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: 221.83  E-value: 3.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626    80 CILVDENDRVVGHDTKYNCHLMEkieaeNLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYreseliee 159
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQE-----TPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLP-------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   160 nvlGVRNAAQRKLFDELGIVAEDVPvdeFTPLGRMLYKAPSDGkWGEHEVDYLLFIVRDVKLQPNPdEVAEIKYVSREEL 239
Cdd:TIGR02150  68 ---GELEAAIRRLRHELGIPADDVP---LTVLPRFSYRARDDA-WGEHELCPVFFARANVDLNPNP-EVAEYRWVSLEEL 139

                         170       180
                  ....*....|....*....|....
gi 79514626   240 KELVKKADAGdeavkLSPWFRLVV 263
Cdd:TIGR02150 140 KEILAKPWAG-----FSPWFRIQA 158
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 81-262 5.56e-56

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: 178.08  E-value: 5.56e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  81 ILVDENDRVVGHDTKYNCHlmekieAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYRESelieen 160
Cdd:COG1443   5 DLVDEDGRPIGTAERAEVH------RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGET------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 161 vlgVRNAAQRKLFDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHEVDYLLFIVRDVKLQPNPDEVAEIKYVSREELK 240
Cdd:COG1443  73 ---YEEAAVRELEEELGI----TVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELL 145

                       170       180
                ....*....|....*....|..
gi 79514626 241 ELVKKADAgdeavKLSPWFRLV 262
Cdd:COG1443 146 ALLEAGPE-----AFTPWFRLY 162
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
75-266 3.55e-40

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 138.18  E-value: 3.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   75 MFEDECILVDENDRVVGHDTKYNCHlmekiEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYRES 154
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAH-----TADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  155 elieenvlgVRNAAQRKLFDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHEVDYLLFIVRDVKLQPNPDEVAEIKYV 234
Cdd:PRK03759  78 ---------LEDAVIRRCREELGV----EITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWV 144

                        170       180       190
                 ....*....|....*....|....*....|..
gi 79514626  235 sreELKELVKKADAGDEAVklSPWFRLVVDNF 266
Cdd:PRK03759 145 ---DPADLLRAVDATPWAF--SPWMVLQAANL 171
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 83-235 2.22e-19

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: 82.22  E-value: 2.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  83 VDENDRVVGHDTKynchlmEKIEAENLLHRAFSVFLFNSK-YELLLQQRSKTKVTFPLVWTNTCCSHPLYRESelieenv 161
Cdd:cd04692   4 VDEDGRPIGVATR------SEVHRQGLWHRTVHVWLVNPEeGRLLLQKRSANKDDFPGLWDISAAGHIDAGET------- 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79514626 162 lgVRNAAQRKLFDELGIvaeDVPVDEFTPLGRMLYKApSDGKWGEHEVDYLLFIVRDVKLQ---PNPDEVAEIKYVS 235
Cdd:cd04692  71 --YEEAAVRELEEELGL---TVSPEDLIFLGVIREEV-IGGDFIDNEFVHVYLYETDRPLEefkLQPEEVAGVVFVD 141
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 80-248 1.62e-17

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: 77.66  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  80 CILVDENDRVVGHDTKynchlmEKIEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWtnTCCSHPLYRESELIEE 159
Cdd:cd04697   1 VDIVDENNEVVGAATR------AEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYL--DPATGGVVGAGESYEE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 160 NvlgvrnaAQRKLFDELGIvaEDVPvdeFTPLGRMLYKAPSDGKWGE-HEVDYllfivrDVKLQPNPDEVAEIKYVSREE 238
Cdd:cd04697  73 N-------ARRELEEELGI--DGVP---LRPLFTFYYEDDRSRVWGAlFECVY------DGPLKLQPEEVAEVDWMSEDE 134

                       170
                ....*....|
gi 79514626 239 LKELVKKADA 248
Cdd:cd04697 135 ILQAARGEEF 144
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 82-245 8.26e-16

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: 72.94  E-value: 8.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  82 LVDENDRVVGHDTKYNchlmEKIeAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYRESELIeenv 161
Cdd:cd04693   5 LYDENRNKTGRTHRRG----EPL-PEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLE---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 162 lgvrnAAQRKLFDELGIvaeDVPVDEFTPLGRMlykapsdgkWGEHEVDYLLFIVRDV---KLQPNPDEVAEIKYVSREE 238
Cdd:cd04693  76 -----AAIRELKEELGI---DLDADELRPILTI---------RFDNGFDDIYLFRKDVdieDLTLQKEEVQDVKWVTLEE 138


                ....*..
gi 79514626 239 LKELVKK 245
Cdd:cd04693 139 ILEMIES 145
NUDIX pfam00293
NUDIX domain;
109-259 1.05e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 72.13  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   109 LLHRAFSVFLFNSKYELLLQQRSKTKvtfPLVWTNTCCSHPlyRESELIEEnvlgvrnAAQRKLFDELGIVAEDVPVdef 188
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKP---FPGWWSLPGGKV--EPGETPEE-------AARRELEEETGLEPELLEL--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79514626   189 tpLGRMLYKAPSDGKWG-EHEVDYLLFIVRDVKLQPNPD-EVAEIKYVSREELKELVKKADAGdeavKLSPWF 259
Cdd:pfam00293  66 --LGSLHYLAPFDGRFPdEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKLAPGDR----KLLPWL 132
PLN02791 PLN02791
Nudix hydrolase homolog
 111-247 1.61e-09

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 58.29  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  111 HRAFSVFLF-NSKYELLLQQRSKTKVTFPLVWTNTCCSHPLYRESELIeenvlgvrnAAQRKLFDELGIVaedVPVDEFT 189
Cdd:PLN02791  32 HRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLL---------SAQRELEEELGII---LPKDAFE 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79514626  190 PLGRMLYK-APSDGKWGEHEVD--YLLFIVRDVKLQP---NPDEVAEIKYVSREELKELVKKAD 247
Cdd:PLN02791 100 LLFVFLQEcVINDGKFINNEYNdvYLVTTLDPIPLEAftlQESEVSAVKYMSIEEYKSALAKED 163
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 71-241 6.40e-09

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 54.42  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626   71 QRRLMFEDECILVDENDRVVGHDTKynchlmEKIEAENLLHRAFSVFLFNSKYELLLQQRSKTKVTFPlVWTNTCCSHPL 150
Cdd:PRK15393   3 QRRLASTEWVDIVNENNEVIAQASR------EQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLP-GMLDATAGGVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626  151 yreseLIEENVLgvrNAAQRKLFDELGIVaeDVPvdeFTPLGRMLYKAPSDGKWGEhevdyLLFIVRDVKLQPNPDEVAE 230
Cdd:PRK15393  76 -----QAGEQLL---ESARREAEEELGIA--GVP---FAEHGQFYFEDENCRVWGA-----LFSCVSHGPFALQEEEVSE 137

                        170
                 ....*....|.
gi 79514626  231 IKYVSREELKE 241
Cdd:PRK15393 138 VCWMTPEEITA 148
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 167-244 2.46e-03

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: 37.70  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 167 AAQRKLFDELGIVAEDVpvdefTPLGRMlykaPSDGKWGEHEVDYLLFIVRDVKLQ--PNPDEVAEIKYVSREELKELVK 244
Cdd:COG0494  58 AALRELREETGLTAEDL-----ELLGEL----PSPGYTDEKVHVFLARGLGPGEEVglDDEDEFIEVRWVPLDEALALVT 128
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
 113-244 4.28e-03

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: 36.89  E-value: 4.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79514626 113 AFSVFLFNSKYELLLQQRSKTKVTFPLVWTntccshPLYRESELiEENVLgvrNAAQRKLFDELGIvaEDVPVDEFTPLG 192
Cdd:cd04694   4 GVVVLIEDSDDRVLLTRRAKHMRTFPGVWV------PPGGHVEL-GESLL---EAGLRELQEETGL--EVSDIQSLSLLG 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79514626 193 rmLYKA--PSDGKWGE----HEVDYLLFIVR-----DVKLQPNPDEVAEIKYVSREELKELVK 244
Cdd:cd04694  72 --LWESvyPTLLSIGLpkrhHIVVYYLVKLSeshenQEQLKLQEDEVDAAVWLPKSLLAKLLE 132
 
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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