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Conserved domains on  [gi|445928811|ref|WP_000006666|]
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MULTISPECIES: NUDIX hydrolase [Acinetobacter]

Protein Classification

NUDIX hydrolase( domain architecture ID 10632273)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg(2+) or Mn(2+) for its activity

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 37-159 5.03e-64

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 192.79  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  37 PKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARETREEAEAEIEIEQLYCMYNIPRIGQIYVLFK 116
Cdd:cd04511    1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445928811 117 AQLKDGLFGAGEESIESRLFEEHEIPWGELAFPSVEHTLRHYF 159
Cdd:cd04511   81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
 3-33 1.38e-10

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


:

Pssm-ID: 464323  Cd Length: 32  Bit Score: 53.64  E-value: 1.38e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 445928811    3 FCVACGHKTEQKIPLGDHKVRRVCTHCGNIH 33
Cdd:pfam14803   2 FCSQCGGPVELRIPDGDNRPRLVCTACGTIH 32
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 37-159 5.03e-64

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 192.79  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  37 PKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARETREEAEAEIEIEQLYCMYNIPRIGQIYVLFK 116
Cdd:cd04511    1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445928811 117 AQLKDGLFGAGEESIESRLFEEHEIPWGELAFPSVEHTLRHYF 159
Cdd:cd04511   81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
 3-33 1.38e-10

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


Pssm-ID: 464323  Cd Length: 32  Bit Score: 53.64  E-value: 1.38e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 445928811    3 FCVACGHKTEQKIPLGDHKVRRVCTHCGNIH 33
Cdd:pfam14803   2 FCSQCGGPVELRIPDGDNRPRLVCTACGTIH 32
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
37-155 2.35e-10

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 55.37  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  37 PKVICGALALWED-KVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARetre-eaeAEIEIEQLYCMYNIPRIGQIYVL 114
Cdd:COG1051    5 PKVAVDAVIFRKDgRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRelreetglEVEVLELLGVFDHPDRGHVVSVA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 445928811 115 FKAQLKDGLFGAGEESIESRLFEEHEIPwgELAFPSVEHTL 155
Cdd:COG1051   85 FLAEVLSGEPRADDEIDEARWFPLDELP--ELAFTPADHEI 123
nudC PRK00241
NAD(+) diphosphatase;
3-84 1.66e-04

NAD(+) diphosphatase;


Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 40.99  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811   3 FCVACGHKTEQKiplgDHKVRRVCTHCGNIHYE--NPKVICgaLALWEDKVLLCRraiEPRY--GLWTLPAGYMELFETM 78
Cdd:PRK00241 101 FCGYCGHPMHPS----KTEWAMLCPHCRERYYPriAPCIIV--AVRRGDEILLAR---HPRHrnGVYTVLAGFVEVGETL 171


                 ....*.
gi 445928811  79 EQGAAR 84
Cdd:PRK00241 172 EQCVAR 177
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 37-159 5.03e-64

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 192.79  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  37 PKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARETREEAEAEIEIEQLYCMYNIPRIGQIYVLFK 116
Cdd:cd04511    1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445928811 117 AQLKDGLFGAGEESIESRLFEEHEIPWGELAFPSVEHTLRHYF 159
Cdd:cd04511   81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
 3-33 1.38e-10

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


Pssm-ID: 464323  Cd Length: 32  Bit Score: 53.64  E-value: 1.38e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 445928811    3 FCVACGHKTEQKIPLGDHKVRRVCTHCGNIH 33
Cdd:pfam14803   2 FCSQCGGPVELRIPDGDNRPRLVCTACGTIH 32
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
37-155 2.35e-10

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 55.37  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  37 PKVICGALALWED-KVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARetre-eaeAEIEIEQLYCMYNIPRIGQIYVL 114
Cdd:COG1051    5 PKVAVDAVIFRKDgRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRelreetglEVEVLELLGVFDHPDRGHVVSVA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 445928811 115 FKAQLKDGLFGAGEESIESRLFEEHEIPwgELAFPSVEHTL 155
Cdd:COG1051   85 FLAEVLSGEPRADDEIDEARWFPLDELP--ELAFTPADHEI 123
NPY1 COG2816
NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];
3-84 6.11e-08

NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];


Pssm-ID: 442065 [Multi-domain]  Cd Length: 288  Bit Score: 51.07  E-value: 6.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811   3 FCVACGHKTEQKipLGDHkvRRVCTHCGNIHYE--NPKVICgaLALWEDKVLLCRRAIEPRyGLWTLPAGYMELFETMEQ 80
Cdd:COG2816  127 FCGRCGAPTVVA--AAGW--ARRCPACGAEHYPrtDPAVIV--LVTDGDRILLARQARWPP-GRYSLLAGFVEPGETLEQ 199


                 ....
gi 445928811  81 GAAR 84
Cdd:COG2816  200 AVRR 203
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 34-159 1.23e-07

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: 48.33  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811  34 YENPKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAARETREEAEAEIEIEQLYCMY-NIPRIGQIY 112
Cdd:cd04681    2 FHNVAAAVGVIIRNEGEILFVRRAKEPGKGKLDLPGGFVDPGESAEEALRRELREELGLKIPKLRYLCSLpNTYLYKGIT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445928811 113 V-----LFKAQLKDG--LFGAGEESIESRLFEEHEIPWGELAFPSVEHTLRHYF 159
Cdd:cd04681   82 YktcdlFFTAELDEKpkLKKAEDEVAELEWLDLEEIEPEKLAFPSIRKAVERYI 135
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
 42-84 4.93e-07

ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.


Pssm-ID: 467557 [Multi-domain]  Cd Length: 128  Bit Score: 46.74  E-value: 4.93e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 445928811  42 GALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAAR 84
Cdd:cd04673    5 GAVVFRDGRVLLVRRGNPPDAGLWSFPGGKVELGETLEDAALR 47
NUDIX_Hydrolase cd04674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 36-80 1.56e-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: 467558 [Multi-domain]  Cd Length: 118  Bit Score: 45.15  E-value: 1.56e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 445928811  36 NPKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQ 80
Cdd:cd04674    2 NPLPVVVALLPVRDGLLVIRRGIEPGHGELALPGGYIEYGETWQE 46
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
 48-81 8.59e-06

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. 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, U=I, L or V) which functions as 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 _ "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: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 43.30  E-value: 8.59e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 445928811  48 EDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQG 81
Cdd:cd18873   16 ELKVLLIKRKNEPFKGGWALPGGFVREDETLEDA 49
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
 37-84 4.24e-05

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (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: 467562 [Multi-domain]  Cd Length: 126  Bit Score: 41.14  E-value: 4.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 445928811  37 PKVICGALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAAR 84
Cdd:cd04679    1 PRVGCGAAILDDGRLLLVLRLRAPEAGHWGLPGGKVDWLETVEDAVRR 48
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
 42-80 1.09e-04

ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.


Pssm-ID: 467573 [Multi-domain]  Cd Length: 122  Bit Score: 39.98  E-value: 1.09e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 445928811  42 GALALWEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQ 80
Cdd:cd04691    5 GGVVVKEGKVLLVKRAYGPGKGRWTLPGGFVEEGETLDE 43
nudC PRK00241
NAD(+) diphosphatase;
3-84 1.66e-04

NAD(+) diphosphatase;


Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 40.99  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445928811   3 FCVACGHKTEQKiplgDHKVRRVCTHCGNIHYE--NPKVICgaLALWEDKVLLCRraiEPRY--GLWTLPAGYMELFETM 78
Cdd:PRK00241 101 FCGYCGHPMHPS----KTEWAMLCPHCRERYYPriAPCIIV--AVRRGDEILLAR---HPRHrnGVYTVLAGFVEVGETL 171


                 ....*.
gi 445928811  79 EQGAAR 84
Cdd:PRK00241 172 EQCVAR 177
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 39-84 2.35e-04

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: 38.93  E-value: 2.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 445928811  39 VICGALAL-WEDKVLLCRRAIEPRYGLWTLPAGYMELFETMEQGAAR 84
Cdd:cd02883    1 VAVGAVVFdDEGRVLLVRRSDGPGPGGWELPGGGVEPGETPEEAAVR 47
zf-NADH-PPase pfam09297
NADH pyrophosphatase zinc ribbon domain; This domain is found in between two duplicated NUDIX ...
 3-34 1.48e-03

NADH pyrophosphatase zinc ribbon domain; This domain is found in between two duplicated NUDIX domains. It has a zinc ribbon structure.


Pssm-ID: 430510 [Multi-domain]  Cd Length: 32  Bit Score: 34.88  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 445928811    3 FCVACGHKTEQKIplGDHKvrRVCTHCGNIHY 34
Cdd:pfam09297   5 FCGRCGAPTVPAE--GGWA--RVCPSCGHEHY 32
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
 49-80 2.08e-03

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467576 [Multi-domain]  Cd Length: 135  Bit Score: 36.50  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 445928811  49 DKVLLCRRAIEPRY--GLWTLPAGYMELFETMEQ 80
Cdd:cd04694   14 DRVLLTRRAKHMRTfpGVWVPPGGHVELGESLLE 47
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
51-81 6.38e-03

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 36.14  E-value: 6.38e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 445928811  51 VLLCRRAIEPRYGLWTLPAGYMELFETMEQG 81
Cdd:PRK05379 216 VLLVRRRAEPGKGLWALPGGFLEQDETLLDA 246
 
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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