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Conserved domains on  [gi|1001624596|ref|NP_001307442|]
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 isoform 5 [Homo sapiens]

Protein Classification

nucleotidyl transferase family protein( domain architecture ID 117)

nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 2-123 5.31e-62

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.


The actual alignment was detected with superfamily member cd09286:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 225  Bit Score: 189.82  E-value: 5.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596   2 EGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHL 81
Cdd:cd09286   104 GIEGAAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHL 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1001624596  82 AKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:cd09286   184 VKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 2-123 5.31e-62

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; 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. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 189.82  E-value: 5.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596   2 EGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHL 81
Cdd:cd09286   104 GIEGAAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHL 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1001624596  82 AKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:cd09286   184 VKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 18-123 1.66e-42

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: 138.99  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  18 PELKLLCGADVLKTFQtpnLWKdaHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVqNEISATYIRR 97
Cdd:TIGR00482  94 VELYFIIGADALRSFP---LWK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLLHNPR-VPISSTEIRQ 167

                          90       100
                  ....*....|....*....|....*.
gi 1001624596  98 ALGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:TIGR00482 168 RIRQGKSIEYLLPDPVIKYIKQHGLY 193
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 22-124 1.08e-33

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 117.86  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  22 LLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQ 101
Cdd:PLN02945  134 LLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVRECISR 213

                          90       100
                  ....*....|....*....|...
gi 1001624596 102 GQSVKYLIPDAVITYIKDHGLYT 124
Cdd:PLN02945  214 GLSVKYLTPDGVIDYIKEHGLYM 236
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 19-123 9.12e-25

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: 93.65  E-value: 9.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  19 ELKLLCGADVLKTFQTpnlWKDahIQEIVEKFGLVCVGRVGHDPKGYIAESPILrmHQHNIHLAKEPVQnEISATYIRRA 98
Cdd:COG1057   100 ELYFIIGADALLQLPK---WKR--WEELLELAHLVVVPRPGYELDELEELEALK--PGGRIILLDVPLL-DISSTEIRER 171

                          90       100
                  ....*....|....*....|....*
gi 1001624596  99 LGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:COG1057   172 LAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 2-123 5.31e-62

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; 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. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 189.82  E-value: 5.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596   2 EGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHL 81
Cdd:cd09286   104 GIEGAAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHL 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1001624596  82 AKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:cd09286   184 VKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 18-123 1.66e-42

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: 138.99  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  18 PELKLLCGADVLKTFQtpnLWKdaHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVqNEISATYIRR 97
Cdd:TIGR00482  94 VELYFIIGADALRSFP---LWK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLLHNPR-VPISSTEIRQ 167

                          90       100
                  ....*....|....*....|....*.
gi 1001624596  98 ALGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:TIGR00482 168 RIRQGKSIEYLLPDPVIKYIKQHGLY 193
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 22-124 1.08e-33

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 117.86  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  22 LLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQ 101
Cdd:PLN02945  134 LLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVRECISR 213

                          90       100
                  ....*....|....*....|...
gi 1001624596 102 GQSVKYLIPDAVITYIKDHGLYT 124
Cdd:PLN02945  214 GLSVKYLTPDGVIDYIKEHGLYM 236
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 19-123 9.12e-25

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: 93.65  E-value: 9.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  19 ELKLLCGADVLKTFQTpnlWKDahIQEIVEKFGLVCVGRVGHDPKGYIAESPILrmHQHNIHLAKEPVQnEISATYIRRA 98
Cdd:COG1057   100 ELYFIIGADALLQLPK---WKR--WEELLELAHLVVVPRPGYELDELEELEALK--PGGRIILLDVPLL-DISSTEIRER 171

                          90       100
                  ....*....|....*....|....*
gi 1001624596  99 LGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:COG1057   172 LAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 19-123 4.11e-17

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: 73.82  E-value: 4.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  19 ELKLLCGADVLKTFQTpnlWKDahIQEIVEKFGLVCVGRVGHDPKGYIAESPILrmHQHNIHLAKEPVQNeISATYIRRA 98
Cdd:cd02165    96 ELYFIIGSDNLIRLPK---WYD--WEELLSLVHLVVAPRPGYPIEDASLEKLLL--PGGRIILLDNPLLN-ISSTEIRER 167

                          90       100
                  ....*....|....*....|....*
gi 1001624596  99 LGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:cd02165   168 LKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
25-123 1.65e-16

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 72.17  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596  25 GADVLKTFQTpnlWKDahIQEIVEKFGLVCVGRvghdpKGYIAESPILRMHQH------NIHLAKEPvQNEISATYIRRA 98
Cdd:PRK00071  108 GADALAQLPR---WKR--WEEILDLVHFVVVPR-----PGYPLEALALPALQQlleaagAITLLDVP-LLAISSTAIRER 176

                          90       100
                  ....*....|....*....|....*
gi 1001624596  99 LGQGQSVKYLIPDAVITYIKDHGLY 123
Cdd:PRK00071  177 IKEGRPIRYLLPEAVLDYIEKHGLY 201
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 7-98 8.40e-04

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: 37.42  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624596   7 GKALFSTPAAVPELKLLCGADvlkTFQTPNLWKDAHIQEIVEKFGLVCVGRVGhdpkgyiaespilrmhqhnihlakepV 86
Cdd:cd02039    81 VVFILKILLKVGPDKVVVGED---FAFGKNASYNKDLKELFLDIEIVEVPRVR--------------------------D 131

                          90
                  ....*....|..
gi 1001624596  87 QNEISATYIRRA 98
Cdd:cd02039   132 GKKISSTLIREL 143
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 87-119 3.88e-03

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 35.56  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1001624596  87 QNEISATYIRRALGQGQSVKYLIPDAVITYIKD 119
Cdd:COG1056   124 REEYSGTEIRRLMLEGEDWESLVPPAVAEVIEE 156
 
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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