isopentenyl-diphosphate delta-isomerase IDI1 [Saccharomyces cerevisiae S288C]
Protein Classification
NUDIX hydrolase( domain architecture ID 225)
NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg2+ or Mn2+ for its activity
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| NUDIX_Hydrolase super family | cl00447 | NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ... |
54-288 | 3.23e-92 | |||||
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. The actual alignment was detected with superfamily member PLN02552: Pssm-ID: 469772 [Multi-domain] Cd Length: 247 Bit Score: 273.15 E-value: 3.23e-92
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| Name | Accession | Description | Interval | E-value | |||||
| PLN02552 | PLN02552 | isopentenyl-diphosphate delta-isomerase |
54-288 | 3.23e-92 | |||||
isopentenyl-diphosphate delta-isomerase Pssm-ID: 215303 [Multi-domain] Cd Length: 247 Bit Score: 273.15 E-value: 3.23e-92
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| NUDIX_IPP_Isomerase | cd02885 | Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ... |
73-262 | 3.85e-79 | |||||
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: 236.62 E-value: 3.85e-79
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| IPP_isom_1 | TIGR02150 | isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ... |
74-261 | 1.42e-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: 204.88 E-value: 1.42e-66
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| Idi | COG1443 | Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ... |
75-260 | 3.71e-46 | |||||
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: 152.66 E-value: 3.71e-46
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| NUDIX | pfam00293 | NUDIX domain; |
102-257 | 5.77e-18 | |||||
NUDIX domain; Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 78.29 E-value: 5.77e-18
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| Name | Accession | Description | Interval | E-value | |||||
| PLN02552 | PLN02552 | isopentenyl-diphosphate delta-isomerase |
54-288 | 3.23e-92 | |||||
isopentenyl-diphosphate delta-isomerase Pssm-ID: 215303 [Multi-domain] Cd Length: 247 Bit Score: 273.15 E-value: 3.23e-92
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| NUDIX_IPP_Isomerase | cd02885 | Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ... |
73-262 | 3.85e-79 | |||||
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: 236.62 E-value: 3.85e-79
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| IPP_isom_1 | TIGR02150 | isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two ... |
74-261 | 1.42e-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: 204.88 E-value: 1.42e-66
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| Idi | COG1443 | Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ... |
75-260 | 3.71e-46 | |||||
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: 152.66 E-value: 3.71e-46
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| PRK03759 | PRK03759 | isopentenyl-diphosphate Delta-isomerase; |
75-257 | 9.61e-32 | |||||
isopentenyl-diphosphate Delta-isomerase; Pssm-ID: 235156 [Multi-domain] Cd Length: 184 Bit Score: 116.22 E-value: 9.61e-32
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| NUDIX | pfam00293 | NUDIX domain; |
102-257 | 5.77e-18 | |||||
NUDIX domain; Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 78.29 E-value: 5.77e-18
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| NUDIX_Hydrolase | cd04692 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
76-239 | 1.03e-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: 467574 [Multi-domain] Cd Length: 142 Bit Score: 77.60 E-value: 1.03e-17
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| NUDIX_Hydrolase | cd04693 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
96-245 | 1.58e-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: 74.87 E-value: 1.58e-16
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| NUDIX_Hydrolase | cd04697 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
74-255 | 1.52e-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: 467578 [Multi-domain] Cd Length: 157 Bit Score: 52.62 E-value: 1.52e-08
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| YjhB | COG1051 | ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
109-260 | 2.64e-05 | |||||
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 42.66 E-value: 2.64e-05
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| PLN02791 | PLN02791 | Nudix hydrolase homolog |
101-179 | 5.68e-05 | |||||
Nudix hydrolase homolog Pssm-ID: 215425 [Multi-domain] Cd Length: 770 Bit Score: 44.43 E-value: 5.68e-05
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| NUDIX_Hydrolase | cd04681 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
106-244 | 8.43e-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: 467564 [Multi-domain] Cd Length: 135 Bit Score: 38.70 E-value: 8.43e-04
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| NUDIX_DR0079 | cd24154 | NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus ... |
105-131 | 5.30e-03 | |||||
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: 36.04 E-value: 5.30e-03
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