NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|507077523|ref|WP_016148294|]
View 

nicotinate (nicotinamide) nucleotide adenylyltransferase [Butyricicoccus pullicaecorum]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10003000)

nicotinate-nicotinamide nucleotide adenylyltransferase catalyzes the coupling of ATP and nicotinate-nucleotide to nicotinic acid adenine dinucleotide, and or may catalyze the coupling of ATP and nicotinamide-nucleotide to NAD+

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]; ...
 1-195 5.08e-75

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: 224.23  E-value: 5.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKiPEGSATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKK-HKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTLHALHDA-GYDDLTLIVGTDMLLTFDvCWRAPEEIARLARLAVVARDVNDQQALRDKAELLRHtmnAKISLI 159
Cdd:COG1057   81 GPSYTIDTLRELREEyPDAELYFIIGADALLQLP-KWKRWEELLELAHLVVVPRPGYELDELEELEALKPG---GRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 507077523 160 DAPVLPLSSTDVRR-------IGFfeqMTPPPVAAYIRENRLY 195
Cdd:COG1057  157 DVPLLDISSTEIRErlaegksIRY---LVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-195 5.08e-75

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: 224.23  E-value: 5.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKiPEGSATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKK-HKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTLHALHDA-GYDDLTLIVGTDMLLTFDvCWRAPEEIARLARLAVVARDVNDQQALRDKAELLRHtmnAKISLI 159
Cdd:COG1057   81 GPSYTIDTLRELREEyPDAELYFIIGADALLQLP-KWKRWEELLELAHLVVVPRPGYELDELEELEALKPG---GRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 507077523 160 DAPVLPLSSTDVRR-------IGFfeqMTPPPVAAYIRENRLY 195
Cdd:COG1057  157 DVPLLDISSTEIRErlaegksIRY---LVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-195 4.73e-65

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: 199.01  E-value: 4.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   3 TGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKkiPEGSATAQQRCEMVRLMAEPYDWAELCDIEVRRGGA 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK--PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  83 SYTVDTLHALHDA-GYDDLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNDQQALRDKAELLRHTmnaKISLIDA 161
Cdd:cd02165   79 SYTIDTLEELRERyPNAELYFIIGSDNLIRLPK-WYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGG---RIILLDN 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 507077523 162 PVLPLSSTDVR-RIGF---FEQMTPPPVAAYIRENRLY 195
Cdd:cd02165  155 PLLNISSTEIReRLKNgksIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-197 6.28e-61

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 188.89  E-value: 6.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIPEGsATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPL-APLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTLHALHDAGYD-DLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVAR--DVNDQQALRDKAELLRHtmNAKIS 157
Cdd:PRK00071  83 GPSYTIDTLRELRARYPDvELVFIIGADALAQLPR-WKRWEEILDLVHFVVVPRpgYPLEALALPALQQLLEA--AGAIT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 507077523 158 LIDAPVLPLSSTDVRRIGFFEQ----MTPPPVAAYIRENRLYEK 197
Cdd:PRK00071 160 LLDVPLLAISSTAIRERIKEGRpiryLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-195 1.25e-55

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: 174.81  E-value: 1.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523    5 VLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIPEGSAtAQQRCEMVRLMAEPYDWAELCDIEVRRGGASY 84
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAAS-SHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   85 TVDTLHALHDA-GYDDLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNDQ-QALRDKAELLRHTMNakISLIDAP 162
Cdd:TIGR00482  80 TIDTLKHLKKKyPDVELYFIIGADALRSFPL-WKDWQELLELVHLVIVPRPGYTLdKALLEKAILRMHHGN--LTLLHNP 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 507077523  163 VLPLSSTDVRRIGFF----EQMTPPPVAAYIRENRLY 195
Cdd:TIGR00482 157 RVPISSTEIRQRIRQgksiEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-174 3.79e-24

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: 92.38  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523    5 VLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIpEGSATAQQRCEMVRLMAEPYDWAELCDIEVrrggasy 84
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWEL------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   85 TVDTLHALH-DAgyddltLIVGTDMLLTFdvcWRAPEEIARLARLAVVARDVndqqalrdkaellrhtmnakISLIDAPV 163
Cdd:pfam01467  73 TRELLKELNpDV------LVIGADSLLDF---WYELDEILGNVKLVVVVRPV--------------------FFIPLKPT 123

                         170
                  ....*....|.
gi 507077523  164 LPLSSTDVRRI 174
Cdd:pfam01467 124 NGISSTDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-195 5.08e-75

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: 224.23  E-value: 5.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKiPEGSATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKK-HKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTLHALHDA-GYDDLTLIVGTDMLLTFDvCWRAPEEIARLARLAVVARDVNDQQALRDKAELLRHtmnAKISLI 159
Cdd:COG1057   81 GPSYTIDTLRELREEyPDAELYFIIGADALLQLP-KWKRWEELLELAHLVVVPRPGYELDELEELEALKPG---GRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 507077523 160 DAPVLPLSSTDVRR-------IGFfeqMTPPPVAAYIRENRLY 195
Cdd:COG1057  157 DVPLLDISSTEIRErlaegksIRY---LVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-195 4.73e-65

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: 199.01  E-value: 4.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   3 TGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKkiPEGSATAQQRCEMVRLMAEPYDWAELCDIEVRRGGA 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK--PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  83 SYTVDTLHALHDA-GYDDLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNDQQALRDKAELLRHTmnaKISLIDA 161
Cdd:cd02165   79 SYTIDTLEELRERyPNAELYFIIGSDNLIRLPK-WYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGG---RIILLDN 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 507077523 162 PVLPLSSTDVR-RIGF---FEQMTPPPVAAYIRENRLY 195
Cdd:cd02165  155 PLLNISSTEIReRLKNgksIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-197 6.28e-61

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 188.89  E-value: 6.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIPEGsATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPL-APLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTLHALHDAGYD-DLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVAR--DVNDQQALRDKAELLRHtmNAKIS 157
Cdd:PRK00071  83 GPSYTIDTLRELRARYPDvELVFIIGADALAQLPR-WKRWEEILDLVHFVVVPRpgYPLEALALPALQQLLEA--AGAIT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 507077523 158 LIDAPVLPLSSTDVRRIGFFEQ----MTPPPVAAYIRENRLYEK 197
Cdd:PRK00071 160 LLDVPLLAISSTAIRERIKEGRpiryLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-195 1.25e-55

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: 174.81  E-value: 1.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523    5 VLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIPEGSAtAQQRCEMVRLMAEPYDWAELCDIEVRRGGASY 84
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAAS-SHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   85 TVDTLHALHDA-GYDDLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNDQ-QALRDKAELLRHTMNakISLIDAP 162
Cdd:TIGR00482  80 TIDTLKHLKKKyPDVELYFIIGADALRSFPL-WKDWQELLELVHLVIVPRPGYTLdKALLEKAILRMHHGN--LTLLHNP 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 507077523  163 VLPLSSTDVRRIGFF----EQMTPPPVAAYIRENRLY 195
Cdd:TIGR00482 157 RVPISSTEIRQRIRQgksiEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-195 1.15e-36

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 130.45  E-value: 1.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIPEgSATAQQRCEMVRLMAEPYDWAELCDIEVRRG 80
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQK-ASNGEHRLNMLKLALKNLPKMEVSDFEIKRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 GASYTVDTL-HALHDAGYDDLTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNdqqalRDKAELLRHtmnaKISLI 159
Cdd:PRK07152  80 NVSYTIDTIkYFKKKYPNDEIYFIIGSDNLEKFKK-WKNIEEILKKVQIVVFKRKKN-----INKKNLKKY----NVLLL 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 507077523 160 DAPVLPLSSTDVrRIGFFEQMTPPPVAAYIRENRLY 195
Cdd:PRK07152 150 KNKNLNISSTKI-RKGNLLGKLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-174 3.79e-24

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: 92.38  E-value: 3.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523    5 VLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKIpEGSATAQQRCEMVRLMAEPYDWAELCDIEVrrggasy 84
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLK-RPLFSAEERLEMLELAKWVDEVIVVAPWEL------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   85 TVDTLHALH-DAgyddltLIVGTDMLLTFdvcWRAPEEIARLARLAVVARDVndqqalrdkaellrhtmnakISLIDAPV 163
Cdd:pfam01467  73 TRELLKELNpDV------LVIGADSLLDF---WYELDEILGNVKLVVVVRPV--------------------FFIPLKPT 123

                         170
                  ....*....|.
gi 507077523  164 LPLSSTDVRRI 174
Cdd:pfam01467 124 NGISSTDIRER 134
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
4-195 6.40e-21

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 86.76  E-value: 6.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   4 GVLGGTFNPPHNGHLAAAKHVREALGLDRVLFIPTNLPPHKKipeGSATAQQRCEMVRLMAE----PYDWAELCDIEVRR 79
Cdd:PRK06973  25 GILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKA---DVSAAEHRLAMTRAAAAslvlPGVTVRVATDEIEH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  80 GGASYTVDTLHALHDAGYDD--LTLIVGTDMLLTFDVcWRAPEEIARLARLAVVARDVNDQQAL-----------RDKAE 146
Cdd:PRK06973 102 AGPTYTVDTLARWRERIGPDasLALLIGADQLVRLDT-WRDWRRLFDYAHLCAATRPGFDLGAAspavaaeiaarQADAD 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507077523 147 LLRHTMNAKIsLIDAPV-LPLSSTDVRR-----IGFFEQMT-------PPPVAAYIRENRLY 195
Cdd:PRK06973 181 VLQATPAGHL-LIDTTLaFDLSATDIRAhlracIARRAQVPdasaehvPAAVWAYILQHRLY 241
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 8-195 2.92e-13

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: 65.79  E-value: 2.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   8 GTFNPPHNGHL----AAAKHVREAlGLDRVL--FI-PTNlPPHKKipEGSATAQQRCEMVRLMAEPYDWAELCDIEV--- 77
Cdd:cd09286    7 GSFNPITNMHLrmfeLARDHLHET-GRYEVVggIIsPVN-DAYGK--KGLASAKHRVAMCRLAVQSSDWIRVDDWESlqp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  78 ------------------RRGGASYTVDTLHALHDAGYdDLTLIVGTDMLLTFDV--CWrAPEEIARLAR---LAVVARD 134
Cdd:cd09286   83 ewmrtakvlrhhreeinnKYGGIEGAAKRVLDGSRREV-KIMLLCGADLLESFGIpgLW-KDADLEEILGefgLVVVERT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507077523 135 VND-QQALRDKAELLRHTMNakISLIDAPVLP-LSSTDVRRI----GFFEQMTPPPVAAYIRENRLY 195
Cdd:cd09286  161 GSDpENFIASSDILRKYQDN--IHLVKDWIPNdISSTKVRRAlrrgMSVKYLLPDPVIEYIEQHQLY 225
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-118 1.38e-10

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: 57.06  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   4 GVLGGTFNPPHNGHLaaaKHVREAL--GLDRVLFIPTNLPPHKKIPEGSATAQQRCEMVRLMAepYDWAELCDIEVRRGG 81
Cdd:cd02039    2 GIIIGRFEPFHLGHL---KLIKEALeeALDEVIIIIVSNPPKKKRNKDPFSLHERVEMLKEIL--KDRLKVVPVDFPEVK 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 507077523  82 ASYTVDTLHAlHDAGYDDLTLIVGTDMLLTFDVCWRA 118
Cdd:cd02039   77 ILLAVVFILK-ILLKVGPDKVVVGEDFAFGKNASYNK 112
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-196 5.46e-09

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 53.19  E-value: 5.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   1 MKTGVLGGTFNPPHNGHlaaaKHVREALG-LDRVLFIPT-------NLPPHkkipegsataQQRCEMVRL----MAEPYd 68
Cdd:PRK08887   2 KKIAVFGSAFNPPSLGH----KSVIESLShFDLVLLVPSiahawgkTMLDY----------ETRCQLVDAfiqdLGLSN- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  69 wAELCDIE--VRRGGAS-YTVDTLHALHDAgY--DDLTLIVGTDMLLTFDVCWRAPEEIARLARLAVVARdvndqqalrd 143
Cdd:PRK08887  67 -VQRSDIEqeLYAPDESvTTYALLTRLQEL-YpeADLTFVIGPDNFLKFAKFYKADEITQRWTVMACPEK---------- 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507077523 144 kaellrhtmnakislidapvLPLSSTDVR-RIGF---FEQMTPPPVAAYIRENRLYE 196
Cdd:PRK08887 135 --------------------VPIRSTDIRnALQNgkdISHLTTPGVARLLKEHQLYT 171
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 8-195 1.69e-08

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 52.77  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   8 GTFNPPHNGHLAAAKHVREAL---GLDrVL---FIPTNLPPHKKipeGSATAQQRCEMVRLMAEPYDWAELCDIEVRRGG 81
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARDALmseGYH-VLggyMSPVNDAYKKK---GLASAEHRIQMCQLACEDSDFIMVDPWEARQST 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  82 ASYTVDTLHALHDAGYDD---------LTLIVGTDMLLTFDV--CWRaPEEIARLAR---LAVVARDVNDQQALRDKAEL 147
Cdd:PLN02945 105 YQRTLTVLARVETSLNNNglaseesvrVMLLCGSDLLESFSTpgVWI-PDQVRTICRdygVVCIRREGQDVEKLVSQDEI 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507077523 148 LrHTMNAKISLIDApVLP--LSSTDVRR-------IGFfeqMTPPPVAAYIRENRLY 195
Cdd:PLN02945 184 L-NENRGNILVVDD-LVPnsISSTRVREcisrglsVKY---LTPDGVIDYIKEHGLY 235
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-62 1.35e-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: 46.92  E-value: 1.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507077523    4 GVLGGTFNPPHNGHLAAAKHVREaLGLDRVLFIPTNL--PPHKKIPEgsATAQQRCEMVRL 62
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKE-LFDELIVGVGSDQfvNPLKGEPV--FSLEERLEMLKA 59
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
4-188 1.30e-05

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 44.62  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   4 GVLGGTFNPPHNGHLAAakhVREALGL-DRVLFIP--TNLPPHKKIPegsATAQQRCEMVRLMAEPydwAELCDIEVRrg 80
Cdd:PRK05379   9 LVFIGRFQPFHNGHLAV---IREALSRaKKVIVLIgsADLARSIKNP---FSFEERAQMIRAALAG---IDLARVTIR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523  81 gasytvdtlhALHDAGYDDlTLIVGtdmlltfDVCWRAPEEIARLARLAVVARDVNDQQA-LRdkaellrhtMNAKISLI 159
Cdd:PRK05379  78 ----------PLRDSLYND-SLWLA-------EVQAAVAEHAGADARIGLIGHEKDASSYyLR---------SFPQWELV 130

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 507077523 160 DAPVLP-LSSTDVRR-------IGFFEQMTPPPVAAY 188
Cdd:PRK05379 131 DVPNTEdLSATEIRDayfegriSSFYGWAVPAPVYAF 167
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 4-78 1.60e-03

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: 37.74  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507077523   4 GVLGGTFNPPHNGHLAAakhVREALGLDRVLFIPT---NLPPHKKIPegsATAQQRCEMVRLM--AEPYDWAELCDIEVR 78
Cdd:cd02168    2 LVYIGRFQPFHNGHLAV---VLIALEKAKKVIILIgsaRTARNIKNP---WTSEEREVMIEAAlsDAGADLARVHFRPLR 75
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-61 2.37e-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: 37.10  E-value: 2.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507077523   1 MKTGVLGGTFNPPHNGHLA----AAKHVRE---ALGLDRVLFIPTNlPPhkkipegsaTAQQRCEMVR 61
Cdd:COG1056    2 MKRGLFIGRFQPFHLGHLAvikwALEEVDEliiGIGSAQESHTPRN-PF---------TAGERIEMIR 59
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-61 3.72e-03

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: 36.52  E-value: 3.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507077523   1 MKTGVLGGTFNPPHNGHLAAakhVREALGL-DRV-LFIPTNlpPHKKipeGSATAQQRCEMVR 61
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDI---IERAAKLfDEViVAVAVN--PSKK---PLFSLEERVELIR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH