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Conserved domains on  [gi|259511188|sp|C1A4H9|]
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RecName: Full=Probable nicotinate-nucleotide adenylyltransferase; AltName: Full=Deamido-NAD(+) diphosphorylase; AltName: Full=Deamido-NAD(+) pyrophosphorylase; AltName: Full=Nicotinate mononucleotide adenylyltransferase; Short=NaMN adenylyltransferase

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

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List of domain hits

 Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-196 1.03e-80

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: 238.87  E-value: 1.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKkHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAeVLSTRQ 159
Cdd:COG1057   82 PSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELEALKPGGRII-LLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 259511188 160 VDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYR 196
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-196 1.03e-80

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: 238.87  E-value: 1.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKkHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAeVLSTRQ 159
Cdd:COG1057   82 PSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELEALKPGGRII-LLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 259511188 160 VDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYR 196
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-195 2.65e-71

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: 214.80  E-value: 2.65e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   3 LGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGGLSF 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  83 MVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAEvLSTRQVDM 162
Cdd:cd02165   81 TIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGGRIIL-LDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 259511188 163 SSTEIRSRVRDGRSIRGFVPDAVATYIASTGLY 195
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-197 2.18e-65

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 200.45  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKpQKPLAPLEHRLAMLELAIADNPRFSVSDIELERPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAE--SDSGVVAEVLST 157
Cdd:PRK00071  84 PSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALQqlLEAAGAITLLDV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 259511188 158 RQVDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYRE 197
Cdd:PRK00071 164 PLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-195 1.91e-61

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: 189.84  E-value: 1.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188    5 LFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQ-TSAHHRLAMVRACFEGVQGIEVDPVEIERGGLSFM 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEaASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   84 VDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAEV-LSTRQVDM 162
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 259511188  163 SSTEIRSRVRDGRSIRGFVPDAVATYIASTGLY 195
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-170 2.79e-19

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: 80.06  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188    5 LFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERgglsfm 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   84 vdtvEAVRRRWPDAhlhLLVGRDVVPTLprWHDVDRLLSMVRLVVLTRDaapqegPLLIDAESDSGVvaevlstrqvdmS 163
Cdd:pfam01467  75 ----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRP------VFFIPLKPTNGI------------S 127


                  ....*..
gi 259511188  164 STEIRSR 170
Cdd:pfam01467 128 STDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-196 1.03e-80

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: 238.87  E-value: 1.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKkHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAeVLSTRQ 159
Cdd:COG1057   82 PSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELEALKPGGRII-LLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 259511188 160 VDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYR 196
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-195 2.65e-71

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: 214.80  E-value: 2.65e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   3 LGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGGLSF 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  83 MVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAEvLSTRQVDM 162
Cdd:cd02165   81 TIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGGRIIL-LDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 259511188 163 SSTEIRSRVRDGRSIRGFVPDAVATYIASTGLY 195
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-197 2.18e-65

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 200.45  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKpQKPLAPLEHRLAMLELAIADNPRFSVSDIELERPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAE--SDSGVVAEVLST 157
Cdd:PRK00071  84 PSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALQqlLEAAGAITLLDV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 259511188 158 RQVDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYRE 197
Cdd:PRK00071 164 PLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-195 1.91e-61

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: 189.84  E-value: 1.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188    5 LFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQ-TSAHHRLAMVRACFEGVQGIEVDPVEIERGGLSFM 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEaASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   84 VDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAEV-LSTRQVDM 162
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 259511188  163 SSTEIRSRVRDGRSIRGFVPDAVATYIASTGLY 195
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-195 1.29e-39

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 138.54  E-value: 1.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQTSA-HHRLAMVRACFEGVQGIEVDPVEIERGG 79
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNgEHRLNMLKLALKNLPKMEVSDFEIKRQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEgpllIDAESDSgvvAEVLSTRQ 159
Cdd:PRK07152  81 VSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINK----KNLKKYN---VLLLKNKN 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 259511188 160 VDMSSTEIRSRVRDGRsirgfVPDAVATYIASTGLY 195
Cdd:PRK07152 154 LNISSTKIRKGNLLGK-----LDPKVNDYINENFLY 184
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
2-196 8.75e-35

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 123.36  E-value: 8.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   2 RLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAqQPLKGAHQTSAHHRLAMVRACFEGVQG----IEVDPVEIER 77
Cdd:PRK06973  23 RIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAG-QPWQKADVSAAEHRLAMTRAAAASLVLpgvtVRVATDEIEH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  78 GGLSFMVDTVEAVRRRW-PDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAapqegpllIDAESDSGVVAEVLS 156
Cdd:PRK06973 102 AGPTYTVDTLARWRERIgPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPG--------FDLGAASPAVAAEIA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259511188 157 TRQ---------------------VDMSSTEIRSRVRDGRSIRGFVPD--------AVATYIASTGLYR 196
Cdd:PRK06973 174 ARQadadvlqatpaghllidttlaFDLSATDIRAHLRACIARRAQVPDasaehvpaAVWAYILQHRLYH 242
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-170 2.79e-19

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: 80.06  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188    5 LFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLK-GAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERgglsfm 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   84 vdtvEAVRRRWPDAhlhLLVGRDVVPTLprWHDVDRLLSMVRLVVLTRDaapqegPLLIDAESDSGVvaevlstrqvdmS 163
Cdd:pfam01467  75 ----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRP------VFFIPLKPTNGI------------S 127


                  ....*..
gi 259511188  164 STEIRSR 170
Cdd:pfam01467 128 STDIRER 134
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 8-195 2.13e-12

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: 63.48  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   8 GSFDPPHVGHLL---VAQDALEALRLDHLL--IIPAAQQPLKGAHQTSAHHRLAMVRACFEGVQGIEVDPVEIE------ 76
Cdd:cd09286    7 GSFNPITNMHLRmfeLARDHLHETGRYEVVggIISPVNDAYGKKGLASAKHRVAMCRLAVQSSDWIRVDDWESLqpewmr 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  77 ---------------RGGLSFMVDTVEAVRRRwpDAHLHLLVGRDVVPTL--PR-WHDVD--RLLSMVRLVVLTRDAAP- 135
Cdd:cd09286   87 takvlrhhreeinnkYGGIEGAAKRVLDGSRR--EVKIMLLCGADLLESFgiPGlWKDADleEILGEFGLVVVERTGSDp 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259511188 136 ----QEGPLLIDAESDSGVVAEVLstrQVDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLY 195
Cdd:cd09286  165 enfiASSDILRKYQDNIHLVKDWI---PNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-189 1.89e-11

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: 59.82  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLLVAQDALEalRLDHLLI-IPAAQQPLKGAHQTSAHHRLAMVRACF--EGVQGIEVDPVeier 77
Cdd:COG1056    2 MKRGLFIGRFQPFHLGHLAVIKWALE--EVDELIIgIGSAQESHTPRNPFTAGERIEMIRAALkeEGLSRVYIVPI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  78 gglsfmvdtveavrrrwPDAHLHllvgrdvvptlPRWhdVDRLLSMVR--LVVLTRDaapqegPLLIDAESDSGVvaEVL 155
Cdd:COG1056   76 -----------------PDINNN-----------SLW--VSHVKSLVPpfDVVYSNN------PLVGRLFKEAGY--EVL 117

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 259511188 156 STRQVD---MSSTEIRSRVRDGRSIRGFVPDAVATYI 189
Cdd:COG1056  118 LPPLFEreeYSGTEIRRLMLEGEDWESLVPPAVAEVI 154
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 8-196 3.75e-09

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 54.69  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   8 GSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQ----TSAHHRLAMVRACFEGVQGIEVDPVEIERGG---- 79
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPVNDAYKkkglASAEHRIQMCQLACEDSDFIMVDPWEARQSTyqrt 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  80 LSFM--VDTVEAVRRRWPDAHLH--LLVGRDV-----VPTLPRWHDVDRLLSMVRLVVLTRDAAP-----QEGPLLIDAE 145
Cdd:PLN02945 109 LTVLarVETSLNNNGLASEESVRvmLLCGSDLlesfsTPGVWIPDQVRTICRDYGVVCIRREGQDveklvSQDEILNENR 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259511188 146 SDSGVVAEVLSTRqvdMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYR 196
Cdd:PLN02945 189 GNILVVDDLVPNS---ISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLYM 236
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-114 4.36e-09

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: 53.21  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   4 GLFGGSFDPPHVGHLLVAQDALE-ALRLDHLLIIPAAQQPLKGAHQTSAHHRLAMVRACFEGVqgIEVDPVEIERGGLSF 82
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEeALDEVIIIIVSNPPKKKRNKDPFSLHERVEMLKEILKDR--LKVVPVDFPEVKILL 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 259511188  83 MVDTVEAVRRRWPDahLHLLVGRDVVPTLPRW 114
Cdd:cd02039   80 AVVFILKILLKVGP--DKVVVGEDFAFGKNAS 109
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-73 6.38e-09

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: 50.77  E-value: 6.38e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259511188    4 GLFGGSFDPPHVGHLLVAQDALEAlrLDHLLIIP---AAQQPLKGAHQTSAHHRLAMVRACfegvqgIEVDPV 73
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKEL--FDELIVGVgsdQFVNPLKGEPVFSLEERLEMLKAL------KYVDEV 66
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-93 5.45e-06

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: 44.61  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   1 MRLGLFGGSFDPPHVGHLlvaqDALE-ALRL-DHlLIIPAAQQPLKgahQT--SAHHRLAMVRACFEGVQGIEVDPVEie 76
Cdd:COG0669    1 MRIAVYPGSFDPITNGHL----DIIErAAKLfDE-VIVAVAVNPSK---KPlfSLEERVELIREALADLPNVEVDSFD-- 70

                         90
                 ....*....|....*..
gi 259511188  77 rgGLsfmvdTVEAVRRR 93
Cdd:COG0669   71 --GL-----LVDFAREV 80
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 4-76 7.89e-06

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: 44.68  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   4 GLFGGSFDPPHVGHLLVAQDALEALRldHLLIipaaqqpLKGAHQT--------SAHHRLAMVRACFEGvQGIEVDPVEI 75
Cdd:cd02168    2 LVYIGRFQPFHNGHLAVVLIALEKAK--KVII-------LIGSARTarniknpwTSEEREVMIEAALSD-AGADLARVHF 71


                 .
gi 259511188  76 E 76
Cdd:cd02168   72 R 72
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-189 1.08e-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: 43.82  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   4 GLFGGSFDPPHVGHLLVAQDALEalRLDHLLI-IPAAQQPLKGAHQTSAHHRLAMVRACFEgvqgievdpvEIERGGLSF 82
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILE--EVDELIIgIGSAQESHTLENPFTAGERVLMIRRALE----------EEGIDLSRY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188  83 MVDTVeavrrrwPDAHLHLLVGRDVVPTLPRWHdvdrllsmvrlVVLTRDaapqegPLLIDAESDSGVvaEVLSTRQVD- 161
Cdd:cd02166   70 YIIPV-------PDIERNSLWVSYVESLTPPFD-----------VVYSGN------PLVARLFKEAGY--EVRRPPMFNr 123

                        170       180       190
                 ....*....|....*....|....*....|
gi 259511188 162 --MSSTEIRSRVRDGRSIRGFVPDAVATYI 189
Cdd:cd02166  124 eeYSGTEIRRLMLGGEDWEELVPKSVAEVI 153
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
4-66 8.81e-05

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 42.30  E-value: 8.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259511188   4 GLFGGSFDPPHVGHLLVAQDALEalRLDHLLIIP-AAQQPLKGAHQTSAHHRLAMVRACFEGVQ 66
Cdd:PRK05379   9 LVFIGRFQPFHNGHLAVIREALS--RAKKVIVLIgSADLARSIKNPFSFEERAQMIRAALAGID 70
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-93 4.90e-03

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: 36.29  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511188   4 GLFGGSFDPPHVGHLlvaqDALE-ALRL-DHLLIIPA---AQQPLkgahqTSAHHRLAMVRACFEGVQGIEVDPVEierg 78
Cdd:cd02163    2 AVYPGSFDPITNGHL----DIIErASKLfDEVIVAVAvnpSKKPL-----FSLEERVELIREATKHLPNVEVDGFD---- 68

                         90
                 ....*....|....*
gi 259511188  79 GLsfmvdTVEAVRRR 93
Cdd:cd02163   69 GL-----LVDFARKH 78
 
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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