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Conserved domains on  [gi|1196667125|ref|WP_086249011|]
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MULTISPECIES: nicotinate (nicotinamide) nucleotide adenylyltransferase [Campylobacter]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10114920)

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
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-173 4.37e-51

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: 162.41  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAPPNLRLQWCRALWENLsPKIIVSDYETSQNRAV 82
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDN-PKFEVSDIEIKRDGPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  83 ASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDI------------NVKI 150
Cdd:cd02165    80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLlpggriilldnpLLNI 159

                         170       180
                  ....*....|....*....|....*...
gi 1196667125 151 SSSKIKSELN-----FKQVPSAILSSVQ 173
Cdd:cd02165   160 SSTEIRERLKngksiRYLLPPAVADYIK 187
 
Name Accession Description Interval E-value
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-173 4.37e-51

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: 162.41  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAPPNLRLQWCRALWENLsPKIIVSDYETSQNRAV 82
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDN-PKFEVSDIEIKRDGPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  83 ASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDI------------NVKI 150
Cdd:cd02165    80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLlpggriilldnpLLNI 159

                         170       180
                  ....*....|....*....|....*...
gi 1196667125 151 SSSKIKSELN-----FKQVPSAILSSVQ 173
Cdd:cd02165   160 SSTEIRERLKngksiRYLLPPAVADYIK 187
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-155 1.78e-46

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: 150.66  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEF-GAPPNLRLQWCRALWENLsPKIIVSDYETSQN 79
Cdd:COG1057     2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKpLASAEHRLAMLRLAIADN-PRFEVSDIELERP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  80 RAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDINVK---------- 149
Cdd:COG1057    81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELEALKPGgriilldvpl 160


                  ....*...
gi 1196667125 150 --ISSSKI 155
Cdd:COG1057   161 ldISSTEI 168
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-180 7.12e-45

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: 146.70  E-value: 7.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   5 IFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAPPN-LRLQWCRALWENLsPKIIVSDYETSQNRAVA 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASShHRLAMLKLAIEDN-PKFEVDDFEIKRGGPSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  84 SIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDIN--------------VK 149
Cdd:TIGR00482  80 TIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILrmhhgnltllhnprVP 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1196667125 150 ISSSKIKSELNF-KQVPSAILSSVQSFYKDKN 180
Cdd:TIGR00482 160 ISSTEIRQRIRQgKSIEYLLPDPVIKYIKQHG 191
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-169 2.70e-43

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 147.02  E-value: 2.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAP-PNLRLQWCRALWENLsPKIIVSDYETSQN 79
Cdd:PRK07152    1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASnGEHRLNMLKLALKNL-PKMEVSDFEIKRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  80 RAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDI------NVKISSS 153
Cdd:PRK07152   80 NVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNLKKYNVlllknkNLNISST 159

                         170
                  ....*....|....*.
gi 1196667125 154 KIKSELNFKQVPSAIL 169
Cdd:PRK07152  160 KIRKGNLLGKLDPKVN 175
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-156 9.33e-15

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: 67.34  E-value: 9.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   5 IFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTflNPFKSEFGAPPN---LRLQWCRaLWENLSPKIIVSDYETSQNra 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPS--DEPPHKLKRPLFsaeERLEMLE-LAKWVDEVIVVAPWELTRE-- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196667125  82 vasidsvsyFKNKFNASriYLIIGADQLNSLhkWHRYDELKALVSFVVACRDDIkidenLQKLDINVKISSSKIK 156
Cdd:pfam01467  76 ---------LLKELNPD--VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF-----FIPLKPTNGISSTDIR 132
 
Name Accession Description Interval E-value
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-173 4.37e-51

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: 162.41  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAPPNLRLQWCRALWENLsPKIIVSDYETSQNRAV 82
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDN-PKFEVSDIEIKRDGPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  83 ASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDI------------NVKI 150
Cdd:cd02165    80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLlpggriilldnpLLNI 159

                         170       180
                  ....*....|....*....|....*...
gi 1196667125 151 SSSKIKSELN-----FKQVPSAILSSVQ 173
Cdd:cd02165   160 SSTEIRERLKngksiRYLLPPAVADYIK 187
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-155 1.78e-46

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: 150.66  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEF-GAPPNLRLQWCRALWENLsPKIIVSDYETSQN 79
Cdd:COG1057     2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKpLASAEHRLAMLRLAIADN-PRFEVSDIELERP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  80 RAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDINVK---------- 149
Cdd:COG1057    81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELEALKPGgriilldvpl 160


                  ....*...
gi 1196667125 150 --ISSSKI 155
Cdd:COG1057   161 ldISSTEI 168
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-180 7.12e-45

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: 146.70  E-value: 7.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   5 IFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAPPN-LRLQWCRALWENLsPKIIVSDYETSQNRAVA 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASShHRLAMLKLAIEDN-PKFEVDDFEIKRGGPSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  84 SIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDIN--------------VK 149
Cdd:TIGR00482  80 TIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILrmhhgnltllhnprVP 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1196667125 150 ISSSKIKSELNF-KQVPSAILSSVQSFYKDKN 180
Cdd:TIGR00482 160 ISSTEIRQRIRQgKSIEYLLPDPVIKYIKQHG 191
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-169 2.70e-43

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 147.02  E-value: 2.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFGAP-PNLRLQWCRALWENLsPKIIVSDYETSQN 79
Cdd:PRK07152    1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASnGEHRLNMLKLALKNL-PKMEVSDFEIKRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  80 RAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDENLQKLDI------NVKISSS 153
Cdd:PRK07152   80 NVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNLKKYNVlllknkNLNISST 159

                         170
                  ....*....|....*.
gi 1196667125 154 KIKSELNFKQVPSAIL 169
Cdd:PRK07152  160 KIRKGNLLGKLDPKVN 175
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-155 5.85e-36

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 124.18  E-value: 5.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLNPFKSEFG-APPNLRLQWCRALWENLsPKIIVSDYETSQN 79
Cdd:PRK00071    4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPlAPLEHRLAMLELAIADN-PRFSVSDIELERP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  80 RAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSFVVACRDDIKIDEN----LQKLD--------IN 147
Cdd:PRK00071   83 GPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALalpaLQQLLeaagaitlLD 162

                         170
                  ....*....|.
gi 1196667125 148 VK---ISSSKI 155
Cdd:PRK00071  163 VPllaISSTAI 173
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-156 9.33e-15

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: 67.34  E-value: 9.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   5 IFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTflNPFKSEFGAPPN---LRLQWCRaLWENLSPKIIVSDYETSQNra 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPS--DEPPHKLKRPLFsaeERLEMLE-LAKWVDEVIVVAPWELTRE-- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196667125  82 vasidsvsyFKNKFNASriYLIIGADQLNSLhkWHRYDELKALVSFVVACRDDIkidenLQKLDINVKISSSKIK 156
Cdd:pfam01467  76 ---------LLKELNPD--VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF-----FIPLKPTNGISSTDIR 132
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
3-132 2.37e-13

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 65.96  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFlNPFKSEFGAPPNLRLQWCRALWENLSP---KIIVSDYETSQN 79
Cdd:PRK06973   24 IGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAG-QPWQKADVSAAEHRLAMTRAAAASLVLpgvTVRVATDEIEHA 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1196667125  80 RAVASIDSVSYFKNKF--NASrIYLIIGADQLNSLHKWHRYDELKALVSFVVACR 132
Cdd:PRK06973  103 GPTYTVDTLARWRERIgpDAS-LALLIGADQLVRLDTWRDWRRLFDYAHLCAATR 156
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-175 7.18e-08

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 49.72  E-value: 7.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   1 MNIAIFGGSFDPPHFGHDEVVKSaLKNLniDKLIIIPTFLNPFKSEFgAPPNLRLQWCRALWENLS-PKIIVSDYETS-- 77
Cdd:PRK08887    2 KKIAVFGSAFNPPSLGHKSVIES-LSHF--DLVLLVPSIAHAWGKTM-LDYETRCQLVDAFIQDLGlSNVQRSDIEQEly 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125  78 -QNRAVASIDSVSYFKNKFNASRIYLIIGADQLNSLHKWHRYDELKALVSfVVACRDDIKIdenlQKLDINVKISSSKIK 156
Cdd:PRK08887   78 aPDESVTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWT-VMACPEKVPI----RSTDIRNALQNGKDI 152

                         170
                  ....*....|....*....
gi 1196667125 157 SELNFKQVpSAILSSVQSF 175
Cdd:PRK08887  153 SHLTTPGV-ARLLKEHQLY 170
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-50 1.70e-06

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: 43.83  E-value: 1.70e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLniDKLIIIPTFLNPFKSEFGAP 50
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGEP 46
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-156 3.48e-06

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: 44.74  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIDKLIIIPTFLN-PFKSEFGAPPNLRLQWCRALwENLSPKIIVSDyetsqNRA 81
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPkKKRNKDPFSLHERVEMLKEI-LKDRLKVVPVD-----FPE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196667125  82 VASIDSVSYFKNKFNASRI-YLIIGADQLNSLHKWHRYDELKALvsfvvacrDDIKIDENLQKLDiNVKISSSKIK 156
Cdd:cd02039    75 VKILLAVVFILKILLKVGPdKVVVGEDFAFGKNASYNKDLKELF--------LDIEIVEVPRVRD-GKKISSTLIR 141
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 8-112 4.34e-05

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: 42.29  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196667125   8 GSFDPPHFGH---DEVVKSALKnlNIDKLIIIPTFLNPFKSEFG----APPNLRLQWCRALWENlSPKIIVSDYETSQNR 80
Cdd:cd09286     7 GSFNPITNMHlrmFELARDHLH--ETGRYEVVGGIISPVNDAYGkkglASAKHRVAMCRLAVQS-SDWIRVDDWESLQPE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1196667125  81 AVASIDSVSYFKNKFNAS-------------------RIYLIIGADQLNSL 112
Cdd:cd09286    84 WMRTAKVLRHHREEINNKyggiegaakrvldgsrrevKIMLLCGADLLESF 134
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-45 1.24e-04

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


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 40.33  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKNLNIdklIIIPTFLNPFKS 45
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDE---VIVAVAKNPSKK 40
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 3-46 2.02e-04

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: 40.05  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKnlNIDKLIII-------PTFLNPFKSE 46
Cdd:cd02168     1 YLVYIGRFQPFHNGHLAVVLIALE--KAKKVIILigsartaRNIKNPWTSE 49
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-35 3.17e-04

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: 39.37  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1196667125   3 IAIFGGSFDPPHFGHDEVVKSALKnlNIDKLII 35
Cdd:cd02163     1 IAVYPGSFDPITNGHLDIIERASK--LFDEVIV 31
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-43 6.70e-04

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: 38.43  E-value: 6.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1196667125   4 AIFGGSFDPPHFGHDEVVKSALKnlNIDKLIII-------PTFLNPF 43
Cdd:cd02166     2 ALFIGRFQPFHLGHLKVIKWILE--EVDELIIGigsaqesHTLENPF 46
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-43 4.85e-03

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 36.00  E-value: 4.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1196667125   4 AIFGGSFDPPHFGHDEVVKSALKnlNIDKLIII-------PTFLNPF 43
Cdd:PRK01153    3 ALFIGRFQPFHKGHLEVIKWILE--EVDELIIGigsaqesHTLKNPF 47
 
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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