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Conserved domains on  [gi|1039790598|ref|XP_017168434|]
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peroxisomal coenzyme A diphosphatase NUDT7 isoform X1 [Mus musculus]

Protein Classification

NUDIX hydrolase( domain architecture ID 10130767)

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; such as coenzyme A pyrophosphatase that hydrolyzes the pyrophosphate moiety of coenzyme A

CATH:  3.90.79.10
EC:  3.6.-.-
Gene Ontology:  GO:0016817|GO:0009132|GO:0046872
PubMed:  15581572|16378245
SCOP:  3000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
 65-196 8.15e-45

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


:

Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 147.26  E-value: 8.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEE--------------------NDAL 124
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEiglppesvevlgrldplytpSGFV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039790598 125 VTPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRD--FIMHCFEYKDpetgvnYLIQGMT 196
Cdd:cd03426    84 VTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGPRgtYRVPFYPYEG------YVIWGLT 151
 
Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
 65-196 8.15e-45

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 147.26  E-value: 8.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEE--------------------NDAL 124
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEiglppesvevlgrldplytpSGFV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039790598 125 VTPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRD--FIMHCFEYKDpetgvnYLIQGMT 196
Cdd:cd03426    84 VTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGPRgtYRVPFYPYEG------YVIWGLT 151
PRK10707 PRK10707
putative NUDIX hydrolase; Provisional
 66-196 2.37e-27

putative NUDIX hydrolase; Provisional


Pssm-ID: 182663  Cd Length: 190  Bit Score: 103.53  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  66 VLVPLLARGgKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEENDA--------------------LV 125
Cdd:PRK10707   34 VLIPIVRRP-QPTLLLTQRSIHLRKHAGQVAFPGGAVDPTDASLIATALREAQEEVAIppsavevigvlppvdsstgyQV 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039790598 126 TPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRDFIMHCFEYKDpetgvnYLIQGMT 196
Cdd:PRK10707  113 TPVVGIIPPDLPYRANEDEVAAVFEMPLAEALHLGRYHPLDIYRRGQSHRVWLSWYEQ------YFVWGMT 177
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 65-157 2.35e-05

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: 43.10  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLmftVRSDKLKREPGEVCFPGGKRDPVDTDdTATALREAQEE-------------------NDALV 125
Cdd:COG0494    15 AVVVVLLDDDGRVLL---VRRYRYGVGPGLWEFPGGKIEPGESP-EEAALRELREEtgltaedlellgelpspgyTDEKV 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039790598 126 TPVVG-FLDHNFQAQPNA-DEVKEVFFVPLDYFL 157
Cdd:COG0494    91 HVFLArGLGPGEEVGLDDeDEFIEVRWVPLDEAL 124
NUDIX pfam00293
NUDIX domain;
65-161 1.87e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 40.16  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLmftVRSdKLKREPGEVCFPGGKrdpVDTDDT--ATALREAQEE--NDALVTPVVGFLDHNFQAQ- 139
Cdd:pfam00293   5 AVGVVLLNEKGRVLL---VRR-SKKPFPGWWSLPGGK---VEPGETpeEAARRELEEEtgLEPELLELLGSLHYLAPFDg 77

                          90       100
                  ....*....|....*....|....
gi 1039790598 140 --PNADEVKEVFFVPLDYFLHPQV 161
Cdd:pfam00293  78 rfPDEHEILYVFLAEVEGELEPDP 101
 
Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
 65-196 8.15e-45

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 147.26  E-value: 8.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEE--------------------NDAL 124
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGDESPVETALRETEEEiglppesvevlgrldplytpSGFV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039790598 125 VTPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRD--FIMHCFEYKDpetgvnYLIQGMT 196
Cdd:cd03426    84 VTPFVGLLDDPPPLRPNPDEVAEVFTVPLSFLLDPEPRRYETFLRSGPRgtYRVPFYPYEG------YVIWGLT 151
PRK10707 PRK10707
putative NUDIX hydrolase; Provisional
 66-196 2.37e-27

putative NUDIX hydrolase; Provisional


Pssm-ID: 182663  Cd Length: 190  Bit Score: 103.53  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  66 VLVPLLARGgKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEENDA--------------------LV 125
Cdd:PRK10707   34 VLIPIVRRP-QPTLLLTQRSIHLRKHAGQVAFPGGAVDPTDASLIATALREAQEEVAIppsavevigvlppvdsstgyQV 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039790598 126 TPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRDFIMHCFEYKDpetgvnYLIQGMT 196
Cdd:PRK10707  113 TPVVGIIPPDLPYRANEDEVAAVFEMPLAEALHLGRYHPLDIYRRGQSHRVWLSWYEQ------YFVWGMT 177
PLN02709 PLN02709
nudix hydrolase
 58-215 8.85e-25

nudix hydrolase


Pssm-ID: 178311  Cd Length: 222  Bit Score: 97.88  E-value: 8.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  58 HLSSNKFSVLVPLLAR----GGKLYLMFTVRSDKLKREPGEVCFPGGKRDPVDTDDTATALREAQEE---NDALVT---- 126
Cdd:PLN02709   28 HFPAKSSAVLVCLYQEqredKNELRVILTKRSSTLSSHPGEVALPGGKRDEEDKDDIATALREAREEiglDPSLVTiisv 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598 127 -------------PVVGFL--DHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGRDFIMHCFEYKDPETGVNYL 191
Cdd:PLN02709  108 lepfvnkkgmsvaPVIGFLhdKKAFKPLPNPAEVEEIFDVPLEMFLKDKNKRAEEREHEGERYLLQYFDYYSEDKERNFI 187

                         170       180
                  ....*....|....*....|....
gi 1039790598 192 IQGMTSKLAVLVALIILEQSPAFK 215
Cdd:PLN02709  188 IWALTAGILIRVASIVYQRLPEFQ 211
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 65-157 2.35e-05

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: 43.10  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLmftVRSDKLKREPGEVCFPGGKRDPVDTDdTATALREAQEE-------------------NDALV 125
Cdd:COG0494    15 AVVVVLLDDDGRVLL---VRRYRYGVGPGLWEFPGGKIEPGESP-EEAALRELREEtgltaedlellgelpspgyTDEKV 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039790598 126 TPVVG-FLDHNFQAQPNA-DEVKEVFFVPLDYFL 157
Cdd:COG0494    91 HVFLArGLGPGEEVGLDDeDEFIEVRWVPLDEAL 124
NUDIX pfam00293
NUDIX domain;
65-161 1.87e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 40.16  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039790598  65 SVLVPLLARGGKLYLmftVRSdKLKREPGEVCFPGGKrdpVDTDDT--ATALREAQEE--NDALVTPVVGFLDHNFQAQ- 139
Cdd:pfam00293   5 AVGVVLLNEKGRVLL---VRR-SKKPFPGWWSLPGGK---VEPGETpeEAARRELEEEtgLEPELLELLGSLHYLAPFDg 77

                          90       100
                  ....*....|....*....|....
gi 1039790598 140 --PNADEVKEVFFVPLDYFLHPQV 161
Cdd:pfam00293  78 rfPDEHEILYVFLAEVEGELEPDP 101
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
 98-151 5.25e-03

MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside diphosphate-linked moiety X)) motif 1 (Nudt1), is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467533 [Multi-domain]  Cd Length: 136  Bit Score: 35.97  E-value: 5.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039790598  98 PGGKRDPVDTDDTAtALREAQEENDALVTPV--VGFLDHNFQAQPNADEVkEVFFV 151
Cdd:cd03427    32 FGGKVEPGETIEEA-AVRELEEEAGLTATELekVGRLKFEFPDDPEAMDV-HVFRA 85
 
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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