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Conserved domains on  [gi|506991406|ref|WP_016082000|]
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MULTISPECIES: NUDIX domain-containing protein [Bacillus]

Protein Classification

NUDIX hydrolase( domain architecture ID 10140399)

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

CATH:  3.90.79.10
EC:  3.6.1.-
Gene Ontology:  GO:0016817|GO:0009132|GO:0046872
PubMed:  15581572|16378245|27936487
SCOP:  3000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 5-144 5.10e-49

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: 156.18  E-value: 5.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   5 LTIFDPERNTLGKKLRDEVHRDGDWHETFHCWFVEKdaEDMFLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLRE 84
Cdd:cd04692    1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVWLVNP--EEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991406  85 IEEELGLSFQTTDLIYKGIFKIDYEISNLTDREFCHMYFHNVINPL--PFAPGEEVDDVMKV 144
Cdd:cd04692   79 LEEELGLTVSPEDLIFLGVIREEVIGGDFIDNEFVHVYLYETDRPLeeFKLQPEEVAGVVFV 140
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 5-144 5.10e-49

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: 156.18  E-value: 5.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   5 LTIFDPERNTLGKKLRDEVHRDGDWHETFHCWFVEKdaEDMFLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLRE 84
Cdd:cd04692    1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVWLVNP--EEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991406  85 IEEELGLSFQTTDLIYKGIFKIDYEISNLTDREFCHMYFHNVINPL--PFAPGEEVDDVMKV 144
Cdd:cd04692   79 LEEELGLTVSPEDLIFLGVIREEVIGGDFIDNEFVHVYLYETDRPLeeFKLQPEEVAGVVFV 140
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 2-160 4.53e-38

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: 129.16  E-value: 4.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   2 TEWLTIFDPERNTLGKKLRDEVHRDGDWHETFHCWFVEKDAEdmfLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGG 81
Cdd:COG1443    1 EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGR---LLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406  82 LREIEEELGLSFqTTDLIYKGIFKIDYEISN-LTDREFCHMYFHNVINPLPFAPgEEVDDVMKVHATSFLQLLKREISSL 160
Cdd:COG1443   78 VRELEEELGITV-DDDLRPLGTFRYRAVDANgLVENEFCHVFVARLDGPLTPQP-EEVAEVRWVTLEELLALLEAGPEAF 155
PLN02791 PLN02791
Nudix hydrolase homolog
 18-156 2.63e-16

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 76.40  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406  18 KLRDEVHRDGDWHETFHCW-FVEKDAEdmfLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREIEEELGLSFQTT 96
Cdd:PLN02791  20 KPRGEVHRDGDYHRAVHVWiYSESTQE---LLLQRRADCKDSWPGQWDISSAGHISAGDTSLLSAQRELEEELGIILPKD 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991406  97 DLIYKGIFKIDYEISN--LTDREFCHMYFHNVINPLP---FAPGE-EVDDVMKVHATSFLQLLKRE 156
Cdd:PLN02791  97 AFELLFVFLQECVINDgkFINNEYNDVYLVTTLDPIPleaFTLQEsEVSAVKYMSIEEYKSALAKE 162
NUDIX pfam00293
NUDIX domain;
63-141 1.47e-05

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 42.86  E-value: 1.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991406   63 WDITSAGHIMHDEDVQIGGLREIEEELGLSFQTTDLIYKGIFKIDYEISNLTDREFCHMYFHNVINPLPFAPGEEVDDV 141
Cdd:pfam00293  30 WWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFPDEHEILYVFLAEVEGELEPDPDGEVEEV 108
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 5-144 5.10e-49

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: 156.18  E-value: 5.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   5 LTIFDPERNTLGKKLRDEVHRDGDWHETFHCWFVEKdaEDMFLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLRE 84
Cdd:cd04692    1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVWLVNP--EEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506991406  85 IEEELGLSFQTTDLIYKGIFKIDYEISNLTDREFCHMYFHNVINPL--PFAPGEEVDDVMKV 144
Cdd:cd04692   79 LEEELGLTVSPEDLIFLGVIREEVIGGDFIDNEFVHVYLYETDRPLeeFKLQPEEVAGVVFV 140
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 2-160 4.53e-38

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: 129.16  E-value: 4.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   2 TEWLTIFDPERNTLGKKLRDEVHRDGDWHETFHCWFVEKDAEdmfLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGG 81
Cdd:COG1443    1 EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGR---LLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406  82 LREIEEELGLSFqTTDLIYKGIFKIDYEISN-LTDREFCHMYFHNVINPLPFAPgEEVDDVMKVHATSFLQLLKREISSL 160
Cdd:COG1443   78 VRELEEELGITV-DDDLRPLGTFRYRAVDANgLVENEFCHVFVARLDGPLTPQP-EEVAEVRWVTLEELLALLEAGPEAF 155
PLN02791 PLN02791
Nudix hydrolase homolog
 18-156 2.63e-16

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 76.40  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406  18 KLRDEVHRDGDWHETFHCW-FVEKDAEdmfLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREIEEELGLSFQTT 96
Cdd:PLN02791  20 KPRGEVHRDGDYHRAVHVWiYSESTQE---LLLQRRADCKDSWPGQWDISSAGHISAGDTSLLSAQRELEEELGIILPKD 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506991406  97 DLIYKGIFKIDYEISN--LTDREFCHMYFHNVINPLP---FAPGE-EVDDVMKVHATSFLQLLKRE 156
Cdd:PLN02791  97 AFELLFVFLQECVINDgkFINNEYNDVYLVTTLDPIPleaFTLQEsEVSAVKYMSIEEYKSALAKE 162
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 3-114 9.65e-13

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: 62.93  E-value: 9.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   3 EWLTIFDPERNTLGKKL-RDEVHRDGDWHETFHCWFVekDAEDMFLyFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGG 81
Cdd:cd04693    1 ELWDLYDENRNKTGRTHrRGEPLPEGEYHLVVHVWIF--NSDGEIL-IQQRSPDKKGFPGMWEASTGGSVLAGETSLEAA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 506991406  82 LREIEEELGLSFQTTDLIYKG------------IFKIDYEISNLT 114
Cdd:cd04693   78 IRELKEELGIDLDADELRPILtirfdngfddiyLFRKDVDIEDLT 122
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
9-153 1.21e-07

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 49.58  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   9 DPERNTLGKKLRDEVH-RDGDWHETFHCWFVekDAEDMFLyFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREIEE 87
Cdd:PRK03759  12 DEQGVPTGTAEKAAAHtADTPLHLAFSCYLF--DADGRLL-VTRRALSKKTWPGVWTNSCCGHPQPGESLEDAVIRRCRE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506991406  88 ELGLSFQTTDLIYkGIFKIDYEISN-LTDREFCHMYFHNVINPLPFAPgEEVDDVMKVHATSFLQLL 153
Cdd:PRK03759  89 ELGVEITDLELVL-PDFRYRATDPNgIVENEVCPVFAARVTSALQPNP-DEVMDYQWVDPADLLRAV 153
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 9-156 1.33e-07

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: 49.03  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   9 DPERNTLGKKLRDEVHRDGD-WHETFHCwFVEKDAEDMFLyfQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREIEE 87
Cdd:cd02885    6 DEDDNPIGTAEKLEAHRKGTlLHRAFSV-FLFNSKGELLL--QRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRLRE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506991406  88 ELGLSFQ----TTDLIYKGIFKidyeiSNLTDREFCHMYFHN-----VINPlpfapgEEVDDVMKVHATSFLQLLKRE 156
Cdd:cd02885   83 ELGIPVCdleeLPRFRYRATDD-----NGLVEHEIDHVFVGRadgdpVPNP------EEVSDYRWVSLEELRELLAAT 149
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 7-92 3.10e-06

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: 45.30  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   7 IFDPERNTLGKKLRDEVHRDGDWHE-TFhcWFVEKDAEDmfLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREI 85
Cdd:cd04697    3 IVDENNEVVGAATRAEMRRQKLIHRaTY--IVVRNAAGR--LLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARREL 78


                 ....*..
gi 506991406  86 EEELGLS 92
Cdd:cd04697   79 EEELGID 85
NUDIX pfam00293
NUDIX domain;
63-141 1.47e-05

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 42.86  E-value: 1.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506991406   63 WDITSAGHIMHDEDVQIGGLREIEEELGLSFQTTDLIYKGIFKIDYEISNLTDREFCHMYFHNVINPLPFAPGEEVDDV 141
Cdd:pfam00293  30 WWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFPDEHEILYVFLAEVEGELEPDPDGEVEEV 108
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 69-109 1.49e-03

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: 37.24  E-value: 1.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 506991406  69 GHIMHDEDVQIGGLREIEEELGLSFQTTDLIYKGIFKIDYE 109
Cdd:cd03674   32 GHVEPDEDPLEAALREAREETGLDVELLSPLSPDPLDIDVH 72
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 2-91 1.56e-03

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 37.86  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506991406   2 TEWLTIFDPERNTLGKKLRDEVHRDGDWHETfhCWFVEKDAEDMFLyFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGG 81
Cdd:PRK15393   9 TEWVDIVNENNEVIAQASREQMRAQCLRHRA--TYIVVHDGMGKIL-VQRRTETKDFLPGMLDATAGGVVQAGEQLLESA 85

                         90
                 ....*....|
gi 506991406  82 LREIEEELGL 91
Cdd:PRK15393  86 RREAEEELGI 95
NUDIX_Tnr3_like cd03676
thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a ...
 40-92 2.02e-03

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: 37.09  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 506991406  40 KDAEDMFLYFQLRSKNKKEAPCIWDITSAGHIMHDEDVQIGGLREIEEELGLS 92
Cdd:cd03676   16 RDGDGLRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLP 68
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 68-141 3.25e-03

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: 35.84  E-value: 3.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506991406  68 AGHIMHDEDVQIGGLREIEEELGLSFQTTDLIykGIFkiDYEISNLTDREFCHMYFHNVINP-LPFAPGEEVDDV 141
Cdd:cd02883   32 GGGVEPGETPEEAAVREVREETGLDVEVLRLL--GVY--EFPDPDEGRHVVVLVFLARVVGGePPPLDDEEISEV 102
 
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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