NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488216424|ref|WP_002287632|]
View 

MULTISPECIES: nicotinate-nucleotide adenylyltransferase [Enterococcus]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10003000)

nicotinate-nucleotide adenylyltransferase catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide

CATH:  3.40.50.620
Gene Ontology:  GO:0004515|GO:0005524|GO:0009435
PubMed:  19273075
SCOP:  4003834

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 26-212 1.95e-99

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: 286.63  E-value: 1.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  26 KKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARG 105
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 106 GKSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTD---------TPYPVIWVDVPE 176
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDeleelealkPGGRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488216424 177 IDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 26-212 1.95e-99

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: 286.63  E-value: 1.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  26 KKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARG 105
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 106 GKSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTD---------TPYPVIWVDVPE 176
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDeleelealkPGGRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488216424 177 IDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
24-213 1.69e-97

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 282.11  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  24 EKKKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELA 103
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 104 RGGKSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDT------------PYPVIW 171
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488216424 172 VDVPEIDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLYE 213
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 29-212 7.30e-89

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: 259.87  E-value: 7.30e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  29 VGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTiDAKHRLNMLELAVEDNPFLQIETIELARGGKS 108
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPA-SFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 109 YTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDTPYP---------VIWVDVPEIDI 179
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488216424 180 SSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 31-212 4.47e-76

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: 227.20  E-value: 4.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424   31 ILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARGGKSYT 110
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  111 YDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDTPYPVIW-----------VDVPEIDI 179
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 488216424  180 SSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 31-187 3.78e-33

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: 115.88  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424   31 ILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARggksyt 110
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216424  111 yDTMKELtqnNPDtdyYFIIGGDMVEYLpkWYKIDELTSMVNFVGIRRPGYttdtpypvIWVDVPEIDISSTKIRQK 187
Cdd:pfam01467  75 -ELLKEL---NPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPTNGISSTDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 26-212 1.95e-99

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: 286.63  E-value: 1.95e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  26 KKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARG 105
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 106 GKSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTD---------TPYPVIWVDVPE 176
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDeleelealkPGGRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488216424 177 IDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
24-213 1.69e-97

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 282.11  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  24 EKKKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELA 103
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 104 RGGKSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDT------------PYPVIW 171
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488216424 172 VDVPEIDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLYE 213
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 29-212 7.30e-89

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: 259.87  E-value: 7.30e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  29 VGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTiDAKHRLNMLELAVEDNPFLQIETIELARGGKS 108
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPA-SFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 109 YTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDTPYP---------VIWVDVPEIDI 179
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488216424 180 SSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 31-212 4.47e-76

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: 227.20  E-value: 4.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424   31 ILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARGGKSYT 110
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  111 YDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDTPYPVIW-----------VDVPEIDI 179
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 488216424  180 SSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
27-212 2.56e-50

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 166.28  E-value: 2.56e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  27 KQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARGG 106
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 107 KSYTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGYTTDT---PYPVIWVDVPEIDISSTK 183
Cdd:PRK07152  81 VSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKnlkKYNVLLLKNKNLNISSTK 160

                        170       180
                 ....*....|....*....|....*....
gi 488216424 184 IRQKIKEGcsiryLVPDKVIDYIQNEGLY 212
Cdd:PRK07152 161 IRKGNLLG-----KLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 31-187 3.78e-33

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: 115.88  E-value: 3.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424   31 ILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVDEKQTIDAKHRLNMLELAVEDNPFLQIETIELARggksyt 110
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216424  111 yDTMKELtqnNPDtdyYFIIGGDMVEYLpkWYKIDELTSMVNFVGIRRPGYttdtpypvIWVDVPEIDISSTKIRQK 187
Cdd:pfam01467  75 -ELLKEL---NPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPTNGISSTDIRER 134
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
13-212 1.51e-26

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 102.17  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  13 QLFPEEMPQFLEKKKQVGILGGTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPhvdEKQTID-AKHRLNMLELAVE- 90
Cdd:PRK06973   8 PTPNAEPAPPLARPRRIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPW---QKADVSaAEHRLAMTRAAAAs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  91 -DNPFLQIE--TIELARGGKSYTYDTMKELTQN-NPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGIRRPGY----- 161
Cdd:PRK06973  85 lVLPGVTVRvaTDEIEHAGPTYTVDTLARWRERiGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFdlgaa 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216424 162 -------------TTD----TPYPVIWVDVP-EIDISSTKIRQKIKEGCSIRYLVPDK--------VIDYIQNEGLY 212
Cdd:PRK06973 165 spavaaeiaarqaDADvlqaTPAGHLLIDTTlAFDLSATDIRAHLRACIARRAQVPDAsaehvpaaVWAYILQHRLY 241
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
27-213 5.26e-20

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 83.24  E-value: 5.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  27 KQVGILGGTFNPVHLAHLVMAEQAGRnlgLDRVFLMPSYQppHVDEKQTIDAKHRLNMLELAVED--NPFLQIETIE--L 102
Cdd:PRK08887   2 KKIAVFGSAFNPPSLGHKSVIESLSH---FDLVLLVPSIA--HAWGKTMLDYETRCQLVDAFIQDlgLSNVQRSDIEqeL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 103 ARGGKS-YTYDTMKELTQNNPDTDYYFIIGGDMVEYLPKWYKIDELTSMVNFVGirrpgyttdtpypviwvdVPE-IDIS 180
Cdd:PRK08887  77 YAPDESvTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMA------------------CPEkVPIR 138

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488216424 181 STKIRQKIKEGCSIRYLVPDKVIDYIQNEGLYE 213
Cdd:PRK08887 139 STDIRNALQNGKDISHLTTPGVARLLKEHQLYT 171
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 34-212 5.88e-20

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: 84.28  E-value: 5.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  34 GTFNPVHLAHLVMAEQAGRNL---GLDRV---FLMP---SYQpphvdeKQT-IDAKHRLNMLELAVEDNPFLQIETIELA 103
Cdd:cd09286    7 GSFNPITNMHLRMFELARDHLhetGRYEVvggIISPvndAYG------KKGlASAKHRVAMCRLAVQSSDWIRVDDWESL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 104 RggKSY--TYDTMK---ELTQNNPDTDY----------------YFIIGGDMVEYL--PKWYKIDELTSMVNFVG---IR 157
Cdd:cd09286   81 Q--PEWmrTAKVLRhhrEEINNKYGGIEgaakrvldgsrrevkiMLLCGADLLESFgiPGLWKDADLEEILGEFGlvvVE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216424 158 RPGYTTDT---PYPVIWV----------DVPEiDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:cd09286  159 RTGSDPENfiaSSDILRKyqdnihlvkdWIPN-DISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 34-212 1.87e-17

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 77.80  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  34 GTFNPVHLAHLVMAEQAGRNLGLDRVFLMPSYQPPHVD---EKQTIDAKHRLNMLELAVEDNPFLQIETIELARGGKSYT 110
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPVNDaykKKGLASAEHRIQMCQLACEDSDFIMVDPWEARQSTYQRT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424 111 YDTMKE----LTQNNPDTD----YYFIIGGDMVEYL--PKWYKIDELTSMVN---FVGIRRPG-------YTTDTPYP-- 168
Cdd:PLN02945 109 LTVLARvetsLNNNGLASEesvrVMLLCGSDLLESFstPGVWIPDQVRTICRdygVVCIRREGqdveklvSQDEILNEnr 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488216424 169 --VIWVD--VPEiDISSTKIRQKIKEGCSIRYLVPDKVIDYIQNEGLY 212
Cdd:PLN02945 189 gnILVVDdlVPN-SISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 29-186 6.12e-14

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: 66.31  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216424  29 VGILGGTFNPVHLAHLVMAEQAgRNLGLDRVFLMP-SYQPPHVDEKQTIDAKHRLNMLELAVedNPFLQIETIELARGGK 107
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEA-LEEALDEVIIIIvSNPPKKKRNKDPFSLHERVEMLKEIL--KDRLKVVPVDFPEVKI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216424 108 SYTYDTMKELTQNNPDTdyYFIIGGDMVEYLPKWYKIDELtSMVNFVGIrrpgyttdtpYPVIWVdVPEIDISSTKIRQ 186
Cdd:cd02039   78 LLAVVFILKILLKVGPD--KVVVGEDFAFGKNASYNKDLK-ELFLDIEI----------VEVPRV-RDGKKISSTLIRE 142
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 29-93 4.72e-07

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: 45.76  E-value: 4.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488216424   29 VGILGGTFNPVHLAHLVMAEQAgRNLGLDRVFLMPSYQPPHVDEKQTI-DAKHRLNMLELAVEDNP 93
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERA-KELFDELIVGVGSDQFVNPLKGEPVfSLEERLEMLKALKYVDE 65
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 167-207 2.45e-04

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: 40.18  E-value: 2.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488216424 167 YPVIWV-DVPEIDISSTKIRQKIKEGCSIRYLVPDKVIDYIQ 207
Cdd:COG1056  114 YEVLLPpLFEREEYSGTEIRRLMLEGEDWESLVPPAVAEVIE 155
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH