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Conserved domains on  [gi|15232981|ref|NP_186927|]
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isopentenyl pyrophosphate:dimethylallyl pyrophosphate isomerase 2 [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
 50-284 7.43e-163

isopentenyl-diphosphate delta-isomerase


:

Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 451.88  E-value: 7.43e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   50 TAMTDTKDAGMDAVQRRLMFEDECILVDETDRVVGHDSKYNCHLMENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVT 129
Cdd:PLN02552   2 GTMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  130 FPLVWTNTCCSHPLY--------RESELIQDNALGVRNAAQRKLLDELGIVAEDVPVDEFTPLGRMLYKAPSD------G 195
Cdd:PLN02552  82 FPLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  196 KWGEHELDYLLFI--VRDVKVQPNPDEVAEIKYVSREELKELVKKadagEEGLKLSPWFRLVVDNFLMKWWDHVEKGTlv 273
Cdd:PLN02552 162 KWGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKGT-- 235

                        250
                 ....*....|.
gi 15232981  274 EAIDMKTIHKL 284
Cdd:PLN02552 236 EAVDMKTIHKL 246
 
Name Accession Description Interval E-value
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
 50-284 7.43e-163

isopentenyl-diphosphate delta-isomerase


Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 451.88  E-value: 7.43e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   50 TAMTDTKDAGMDAVQRRLMFEDECILVDETDRVVGHDSKYNCHLMENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVT 129
Cdd:PLN02552   2 GTMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  130 FPLVWTNTCCSHPLY--------RESELIQDNALGVRNAAQRKLLDELGIVAEDVPVDEFTPLGRMLYKAPSD------G 195
Cdd:PLN02552  82 FPLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  196 KWGEHELDYLLFI--VRDVKVQPNPDEVAEIKYVSREELKELVKKadagEEGLKLSPWFRLVVDNFLMKWWDHVEKGTlv 273
Cdd:PLN02552 162 KWGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKGT-- 235

                        250
                 ....*....|.
gi 15232981  274 EAIDMKTIHKL 284
Cdd:PLN02552 236 EAVDMKTIHKL 246
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 72-257 3.49e-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: 247.02  E-value: 3.49e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  72 ECILVDETDRVVGHDSKYNCHLMENieaknLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYREseliq 151
Cdd:cd02885   1 EVILVDEDDNPIGTAEKLEAHRKGT-----LLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGE----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 152 dnalGVRNAAQRKLLDELGIvaedvPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYVSREE 231
Cdd:cd02885  71 ----GVEDAAQRRLREELGI-----PVCDLEELPRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEE 141

                       170       180
                ....*....|....*....|....*.
gi 15232981 232 LKELVKkadagEEGLKLSPWFRLVVD 257
Cdd:cd02885 142 LRELLA-----ATPEAFTPWFRLILE 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
 73-256 1.18e-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: 222.60  E-value: 1.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981    73 CILVDETDRVVGHDSKYNCHLMENIeaknlLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYreseliqd 152
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETP-----LHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLP-------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   153 nalGVRNAAQRKLLDELGIVAEDVPvdeFTPLGRMLYKAPSDGkWGEHELDYLLFIVRDVKVQPNPdEVAEIKYVSREEL 232
Cdd:TIGR02150  68 ---GELEAAIRRLRHELGIPADDVP---LTVLPRFSYRARDDA-WGEHELCPVFFARANVDLNPNP-EVAEYRWVSLEEL 139

                         170       180
                  ....*....|....*....|....
gi 15232981   233 KELVKKADAGeeglkLSPWFRLVV 256
Cdd:TIGR02150 140 KEILAKPWAG-----FSPWFRIQA 158
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 74-255 1.99e-54

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: 173.85  E-value: 1.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  74 ILVDETDRVVGHDSKYNCHlmenieAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRESeliqdn 153
Cdd:COG1443   5 DLVDEDGRPIGTAERAEVH------RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGET------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 154 algVRNAAQRKLLDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYVSREELK 233
Cdd:COG1443  73 ---YEEAAVRELEEELGI----TVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELL 145

                       170       180
                ....*....|....*....|..
gi 15232981 234 ELVKkadagEEGLKLSPWFRLV 255
Cdd:COG1443 146 ALLE-----AGPEAFTPWFRLY 162
NUDIX pfam00293
NUDIX domain;
102-252 4.15e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 70.59  E-value: 4.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   102 LLHRAFSVFLFNSKYELLLQQRSNTKvtfPLVWTNTCCSHPLYRESeliqdnalgVRNAAQRKLLDELGIVAEDVPVdef 181
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKP---FPGWWSLPGGKVEPGET---------PEEAARRELEEETGLEPELLEL--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232981   182 tpLGRMLYKAPSDGKWG-EHELDYLLFIVRDVKVQPNPD-EVAEIKYVSREELKELVKKADAGeeglKLSPWF 252
Cdd:pfam00293  66 --LGSLHYLAPFDGRFPdEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKLAPGDR----KLLPWL 132
 
Name Accession Description Interval E-value
PLN02552 PLN02552
isopentenyl-diphosphate delta-isomerase
 50-284 7.43e-163

isopentenyl-diphosphate delta-isomerase


Pssm-ID: 215303 [Multi-domain]  Cd Length: 247  Bit Score: 451.88  E-value: 7.43e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   50 TAMTDTKDAGMDAVQRRLMFEDECILVDETDRVVGHDSKYNCHLMENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVT 129
Cdd:PLN02552   2 GTMADATWAGMDAVQRRLMFEDECILVDENDNVVGHDSKYNCHLFEKIEPRGLLHRAFSVFLFNSKYELLLQQRAATKVT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  130 FPLVWTNTCCSHPLY--------RESELIQDNALGVRNAAQRKLLDELGIVAEDVPVDEFTPLGRMLYKAPSD------G 195
Cdd:PLN02552  82 FPLVWTNTCCSHPLYgqdpnevdRESELIDGNVLGVKNAAQRKLLHELGIPAEDVPVDQFTFLTRLHYKAADDvthgpdG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  196 KWGEHELDYLLFI--VRDVKVQPNPDEVAEIKYVSREELKELVKKadagEEGLKLSPWFRLVVDNFLMKWWDHVEKGTlv 273
Cdd:PLN02552 162 KWGEHELDYLLFIrpVRDVKVNPNPDEVADVKYVNREELKEMMRK----ESGLKLSPWFRLIVDNFLMKWWDDLEKGT-- 235

                        250
                 ....*....|.
gi 15232981  274 EAIDMKTIHKL 284
Cdd:PLN02552 236 EAVDMKTIHKL 246
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 72-257 3.49e-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: 247.02  E-value: 3.49e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  72 ECILVDETDRVVGHDSKYNCHLMENieaknLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYREseliq 151
Cdd:cd02885   1 EVILVDEDDNPIGTAEKLEAHRKGT-----LLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGE----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 152 dnalGVRNAAQRKLLDELGIvaedvPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYVSREE 231
Cdd:cd02885  71 ----GVEDAAQRRLREELGI-----PVCDLEELPRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEE 141

                       170       180
                ....*....|....*....|....*.
gi 15232981 232 LKELVKkadagEEGLKLSPWFRLVVD 257
Cdd:cd02885 142 LRELLA-----ATPEAFTPWFRLILE 162
IPP_isom_1 TIGR02150
isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ...
 73-256 1.18e-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: 222.60  E-value: 1.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981    73 CILVDETDRVVGHDSKYNCHLMENIeaknlLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYreseliqd 152
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETP-----LHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLP-------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   153 nalGVRNAAQRKLLDELGIVAEDVPvdeFTPLGRMLYKAPSDGkWGEHELDYLLFIVRDVKVQPNPdEVAEIKYVSREEL 232
Cdd:TIGR02150  68 ---GELEAAIRRLRHELGIPADDVP---LTVLPRFSYRARDDA-WGEHELCPVFFARANVDLNPNP-EVAEYRWVSLEEL 139

                         170       180
                  ....*....|....*....|....
gi 15232981   233 KELVKKADAGeeglkLSPWFRLVV 256
Cdd:TIGR02150 140 KEILAKPWAG-----FSPWFRIQA 158
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 74-255 1.99e-54

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: 173.85  E-value: 1.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  74 ILVDETDRVVGHDSKYNCHlmenieAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRESeliqdn 153
Cdd:COG1443   5 DLVDEDGRPIGTAERAEVH------RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGET------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 154 algVRNAAQRKLLDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYVSREELK 233
Cdd:COG1443  73 ---YEEAAVRELEEELGI----TVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELL 145

                       170       180
                ....*....|....*....|..
gi 15232981 234 ELVKkadagEEGLKLSPWFRLV 255
Cdd:COG1443 146 ALLE-----AGPEAFTPWFRLY 162
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
68-259 5.61e-38

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 132.02  E-value: 5.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   68 MFEDECILVDETDRVVGHDSKYNCHlmeniEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRES 147
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAH-----TADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  148 eliqdnalgVRNAAQRKLLDELGIvaedVPVDEFTPLGRMLYKAPSDGKWGEHELDYLLFIVRDVKVQPNPDEVAEIKYV 227
Cdd:PRK03759  78 ---------LEDAVIRRCREELGV----EITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWV 144

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15232981  228 sreELKELVKKADAGeeGLKLSPWFRLVVDNF 259
Cdd:PRK03759 145 ---DPADLLRAVDAT--PWAFSPWMVLQAANL 171
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 76-228 6.67e-18

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: 78.37  E-value: 6.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  76 VDETDRVVGHDSKynchlmENIEAKNLLHRAFSVFLFNSK-YELLLQQRSNTKVTFPLVWTNTCCSHPLYRESeliqdna 154
Cdd:cd04692   4 VDEDGRPIGVATR------SEVHRQGLWHRTVHVWLVNPEeGRLLLQKRSANKDDFPGLWDISAAGHIDAGET------- 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232981 155 lgVRNAAQRKLLDELGIvaeDVPVDEFTPLGRMLYKApSDGKWGEHELDYLLFIVRDVKVQ---PNPDEVAEIKYVS 228
Cdd:cd04692  71 --YEEAAVRELEEELGL---TVSPEDLIFLGVIREEV-IGGDFIDNEFVHVYLYETDRPLEefkLQPEEVAGVVFVD 141
NUDIX pfam00293
NUDIX domain;
102-252 4.15e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 70.59  E-value: 4.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   102 LLHRAFSVFLFNSKYELLLQQRSNTKvtfPLVWTNTCCSHPLYRESeliqdnalgVRNAAQRKLLDELGIVAEDVPVdef 181
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKP---FPGWWSLPGGKVEPGET---------PEEAARRELEEETGLEPELLEL--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232981   182 tpLGRMLYKAPSDGKWG-EHELDYLLFIVRDVKVQPNPD-EVAEIKYVSREELKELVKKADAGeeglKLSPWF 252
Cdd:pfam00293  66 --LGSLHYLAPFDGRFPdEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKLAPGDR----KLLPWL 132
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 73-246 2.16e-14

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: 69.19  E-value: 2.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  73 CILVDETDRVVGHDSKynchlmENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWtnTCCSHPLYRESELIQD 152
Cdd:cd04697   1 VDIVDENNEVVGAATR------AEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYL--DPATGGVVGAGESYEE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 153 NalgvrnaAQRKLLDELGIvaEDVPvdeFTPLGRMLYKAPSDGKWGE-HELDYllfivrDVKVQPNPDEVAEIKYVSREE 231
Cdd:cd04697  73 N-------ARRELEEELGI--DGVP---LRPLFTFYYEDDRSRVWGAlFECVY------DGPLKLQPEEVAEVDWMSEDE 134

                       170
                ....*....|....*
gi 15232981 232 LKELVKKADAGEEGL 246
Cdd:cd04697 135 ILQAARGEEFTPDGR 149
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 99-238 3.11e-14

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: 68.71  E-value: 3.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  99 AKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRESELIqdnalgvrnAAQRKLLDELGIvaeDVPV 178
Cdd:cd04693  24 PEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLE---------AAIRELKEELGI---DLDA 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232981 179 DEFTPLGRMlykapsdgkWGEHELDYLLFIVRDV---KVQPNPDEVAEIKYVSREELKELVKK 238
Cdd:cd04693  92 DELRPILTI---------RFDNGFDDIYLFRKDVdieDLTLQKEEVQDVKWVTLEEILEMIES 145
PLN02791 PLN02791
Nudix hydrolase homolog
 104-240 1.20e-09

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 58.68  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  104 HRAFSVFLF-NSKYELLLQQRSNTKVTFPLVWTNTCCSHPLYRESELIqdnalgvrnAAQRKLLDELGIVaedVPVDEFT 182
Cdd:PLN02791  32 HRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLL---------SAQRELEEELGII---LPKDAFE 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232981  183 PLGRMLYK-APSDGKWGEHELD--YLLFIVRDVKVQP---NPDEVAEIKYVSREELKELVKKAD 240
Cdd:PLN02791 100 LLFVFLQEcVINDGKFINNEYNdvYLVTTLDPIPLEAftlQESEVSAVKYMSIEEYKSALAKED 163
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 64-234 3.46e-06

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 46.33  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981   64 QRRLMFEDECILVDETDRVVGHDSKynchlmENIEAKNLLHRAFSVFLFNSKYELLLQQRSNTKVTFPlVWTNTCCSHPL 143
Cdd:PRK15393   3 QRRLASTEWVDIVNENNEVIAQASR------EQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLP-GMLDATAGGVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981  144 YRESELIQdnalgvrnAAQRKLLDELGIVaeDVPvdeFTPLGRMLYKAPSDGKWGEheldyLLFIVRDVKVQPNPDEVAE 223
Cdd:PRK15393  76 QAGEQLLE--------SARREAEEELGIA--GVP---FAEHGQFYFEDENCRVWGA-----LFSCVSHGPFALQEEEVSE 137

                        170
                 ....*....|.
gi 15232981  224 IKYVSREELKE 234
Cdd:PRK15393 138 VCWMTPEEITA 148
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 160-237 7.19e-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: 36.16  E-value: 7.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232981 160 AAQRKLLDELGIVAEDVpvdefTPLGRMlykaPSDGKWGEHELDYLLFIVRDVKVQ--PNPDEVAEIKYVSREELKELVK 237
Cdd:COG0494  58 AALRELREETGLTAEDL-----ELLGEL----PSPGYTDEKVHVFLARGLGPGEEVglDDEDEFIEVRWVPLDEALALVT 128
 
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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