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Conserved domains on  [gi|170655090|gb|ACB24145|]
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pantetheine-phosphate adenylyltransferase [Methylobacterium radiotolerans JCM 2831]

Protein Classification

pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)

pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway

CATH:  3.40.50.620
EC:  2.7.7.3
Gene Ontology:  GO:0005524|GO:0015937|GO:0004595
PubMed:  33271445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-164 2.34e-82

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440433  Cd Length: 159  Bit Score: 239.90  E-value: 2.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   2 TRTALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTETCGPVAQaegaaLEIVTFNDLAVS 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPN-----VEVDSFDGLLVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090  82 AARRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQ 161
Cdd:COG0669   76 FAREVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKE 155


                 ...
gi 170655090 162 RFA 164
Cdd:COG0669  156 KFA 158
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-164 2.34e-82

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 239.90  E-value: 2.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   2 TRTALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTETCGPVAQaegaaLEIVTFNDLAVS 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPN-----VEVDSFDGLLVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090  82 AARRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQ 161
Cdd:COG0669   76 FAREVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKE 155


                 ...
gi 170655090 162 RFA 164
Cdd:COG0669  156 KFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-161 1.09e-73

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 217.72  E-value: 1.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   4 TALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTETCgpvaqAEGAALEIVTFNDLAVSAA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREAT-----KHLPNVEVDGFDGLLVDFA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170655090  84 RRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQ 161
Cdd:cd02163   76 RKHGANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-163 3.20e-67

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 201.35  E-value: 3.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090    4 TALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTEtcgpvAQAEGAALEIVTFNDLAVSAA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKD-----ATKHLPNVRVDVFDGLLVDYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   84 RRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQRF 163
Cdd:TIGR01510  76 KELGATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-140 1.26e-20

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 81.98  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090    6 LYAGSFDPVTNGHLDVVRQACRLVDR-LVIAIG----VHPGKAPLFSAEERAALLtETCGPVAQAEGAAleivtFNDLAV 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPsdepPHKLKRPLFSAEERLEML-ELAKWVDEVIVVA-----PWELTR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   81 SAARRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQI 140
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-55 2.55e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.29  E-value: 2.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   1 MTRTALYAGSFDPVTNGHLDVVRQACRLVDR-----LVIAIGVHPGKAPLFSAEERAALL 55
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLdevwfLPNPGPPHKPQKPLAPLEHRLAML 62
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-164 2.34e-82

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 239.90  E-value: 2.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   2 TRTALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTETCGPVAQaegaaLEIVTFNDLAVS 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPN-----VEVDSFDGLLVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090  82 AARRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQ 161
Cdd:COG0669   76 FAREVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKE 155


                 ...
gi 170655090 162 RFA 164
Cdd:COG0669  156 KFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-161 1.09e-73

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 217.72  E-value: 1.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   4 TALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTETCgpvaqAEGAALEIVTFNDLAVSAA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREAT-----KHLPNVEVDGFDGLLVDFA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170655090  84 RRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQ 161
Cdd:cd02163   76 RKHGANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-163 3.20e-67

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 201.35  E-value: 3.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090    4 TALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPGKAPLFSAEERAALLTEtcgpvAQAEGAALEIVTFNDLAVSAA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKD-----ATKHLPNVRVDVFDGLLVDYA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   84 RRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQRF 163
Cdd:TIGR01510  76 KELGATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-140 1.26e-20

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 81.98  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090    6 LYAGSFDPVTNGHLDVVRQACRLVDR-LVIAIG----VHPGKAPLFSAEERAALLtETCGPVAQAEGAAleivtFNDLAV 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPsdepPHKLKRPLFSAEERLEML-ELAKWVDEVIVVA-----PWELTR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   81 SAARRCGAAIFIRGLRDGTDLDYEMQLAGMNGAMAPEVQTVFLPASTQARPITATLVRQI 140
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 5-55 7.37e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 65.41  E-value: 7.37e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 170655090    5 ALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIG----VHPGK-APLFSAEERAALL 55
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGsdqfVNPLKgEPVFSLEERLEML 57
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 5-139 1.16e-08

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 50.90  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   5 ALYAGSFDPVTNGHLDVVRQACRLV-DRLVIAIGVHPGKAP----LFSAEERAALLTEtcgpvaqAEGAALEIVTFNDLA 79
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKrnkdPFSLHERVEMLKE-------ILKDRLKVVPVDFPE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090  80 VSAARRC----------GAAIFIRGLRDGTDLDYEMQLagMNGAMAPEVQTVFLPASTQARPITATLVRQ 139
Cdd:cd02039   75 VKILLAVvfilkillkvGPDKVVVGEDFAFGKNASYNK--DLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-55 2.62e-08

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 50.89  E-value: 2.62e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170655090   1 MTRTALYAGSFDPVTNGHLDVVRQACRLVD----RLVIAiGVHPGKA--PLFSAEERAALL 55
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGldevIFVPA-GQPPHKKhkPLASAEHRLAML 60
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-55 2.55e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.29  E-value: 2.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   1 MTRTALYAGSFDPVTNGHLDVVRQACRLVDR-----LVIAIGVHPGKAPLFSAEERAALL 55
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLdevwfLPNPGPPHKPQKPLAPLEHRLAML 62
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 5-58 8.36e-07

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 46.40  E-value: 8.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 170655090   5 ALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGV----HPGKAPlFSAEERAALLTET 58
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGSaqesHTLKNP-FTAGERILMIRKA 59
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-126 6.32e-06

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 42.91  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   4 TALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHP---GKAPLFSAEERAALLTETcgpvaqaegaaleivtfndlav 80
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPpvkVWQDPHELEERKESIEED---------------------- 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 170655090  81 saarrcgaaIFIRGLRDGTDLDYEMQlAGMNGAMAPEVQTVFLPAS 126
Cdd:cd02156   59 ---------ISVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRL 94
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-163 1.43e-05

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 43.38  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090   4 TALYAGSFDPVTNGHLDVVRQACRLV--DR-LVIAIGVHP-GKAPLFSAEERAALLTETCGPVAQAEGAALEIV------ 73
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRvLLLPSANPPhKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKrdgpsy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170655090  74 TFNDLAvSAARRCGAA--IFIRGL-------------------------RDGTDLDYEMQLagmngaMAPEVQTVFLPAS 126
Cdd:cd02165   81 TIDTLE-ELRERYPNAelYFIIGSdnlirlpkwydweellslvhlvvapRPGYPIEDASLE------KLLLPGGRIILLD 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 170655090 127 TQARPITATLVRQIAGMGGDVSPFVPAAVAARLRQRF 163
Cdd:cd02165  154 NPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHG 190
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 5-77 1.87e-05

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also containing a Nudix hydrolase domain; N-terminal NMNAT (Nicotinamide/nicotinate mononucleotide adenylyltransferase) domain of a novel bifunctional enzyme endowed with NMN adenylyltransferase and Nudix hydrolase activities. This domain is highly homologous to the archeal NMN adenyltransferase that catalyzes NAD synthesis from NMN and ATP. NMNAT is an essential enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. The C-terminal domain of this enzyme shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family.


Pssm-ID: 173919  Cd Length: 181  Bit Score: 42.75  E-value: 1.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170655090   5 ALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHPG----KAPlFSAEERAALLtETCGPVAQAEGAALEIVTFND 77
Cdd:cd02168    2 LVYIGRFQPFHNGHLAVVLIALEKAKKVIILIGSARTarniKNP-WTSEEREVMI-EAALSDAGADLARVHFRPLRD 76
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
5-75 1.88e-05

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 43.46  E-value: 1.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170655090   5 ALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGVHpGKAPL----FSAEERAALLTetcgpvAQAEGAALEIVTF 75
Cdd:PRK05379   9 LVFIGRFQPFHNGHLAVIREALSRAKKVIVLIGSA-DLARSiknpFSFEERAQMIR------AALAGIDLARVTI 76
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 5-58 1.95e-05

Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present.


Pssm-ID: 173917  Cd Length: 163  Bit Score: 42.67  E-value: 1.95e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 170655090   5 ALYAGSFDPVTNGHLDVVRQACRLVDRLVIAIGV----HPGKAPlFSAEERAALLTET 58
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGSaqesHTLENP-FTAGERVLMIRRA 58
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-55 4.19e-03

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 36.14  E-value: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 170655090    6 LYAGSFDPVTNGHLDVVRQACRLV--DRLVI---AIGVHPGKAPLFSAEERAALL 55
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLdlDKVIFvptANPPHKKTYEAASSHHRLAML 55
 
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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