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Conserved domains on  [gi|896154412|ref|WP_049171017|]
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MULTISPECIES: nicotinate-nucleotide adenylyltransferase [Corynebacterium]

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]; ...
 25-219 3.04e-105

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: 302.81  E-value: 3.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  25 RQRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRP 104
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 105 GATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLraEDLEGID----ASRLHLIEI 180
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYEL--DELEELEalkpGGRIILLDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 896154412 181 PAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQ 219
Cdd:COG1057  159 PLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 25-219 3.04e-105

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: 302.81  E-value: 3.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  25 RQRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRP 104
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 105 GATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLraEDLEGID----ASRLHLIEI 180
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYEL--DELEELEalkpGGRIILLDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 896154412 181 PAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQ 219
Cdd:COG1057  159 PLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
23-220 1.29e-100

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 291.35  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  23 APRQRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDID 102
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 103 RPGATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLEGI-----DASRLHL 177
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALqqlleAAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 896154412 178 IEIPAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQS 220
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 30-218 4.52e-78

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: 233.75  E-value: 4.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412   30 VMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRPGATYT 109
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  110 VDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLEGI----DASRLHLIEIPAMAI 185
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmHHGNLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 896154412  186 SSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 28-218 2.10e-74

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: 224.43  E-value: 2.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  28 IGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKrGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRPGAT 107
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK-PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 108 YTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLE--GIDASRLHLIEIPAMAI 185
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEklLLPGGRIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896154412 186 SSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 30-193 7.24e-27

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: 100.86  E-value: 7.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412   30 VMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRpgatyt 109
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  110 vDTLRDLkviypNADlFFITGADALQKImtWRDWEEMFDAATFVGVTRPGVHLRAEDLEGidasrlhlieipamaISSTD 189
Cdd:pfam01467  75 -ELLKEL-----NPD-VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFIPLKPTNG---------------ISSTD 130


                  ....
gi 896154412  190 CRKR 193
Cdd:pfam01467 131 IRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 25-219 3.04e-105

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: 302.81  E-value: 3.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  25 RQRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRP 104
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 105 GATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLraEDLEGID----ASRLHLIEI 180
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYEL--DELEELEalkpGGRIILLDV 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 896154412 181 PAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQ 219
Cdd:COG1057  159 PLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
23-220 1.29e-100

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 291.35  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  23 APRQRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDID 102
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 103 RPGATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLEGI-----DASRLHL 177
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALqqlleAAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 896154412 178 IEIPAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQS 220
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 30-218 4.52e-78

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: 233.75  E-value: 4.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412   30 VMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRPGATYT 109
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  110 VDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLEGI----DASRLHLIEIPAMAI 185
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmHHGNLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 896154412  186 SSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 28-218 2.10e-74

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: 224.43  E-value: 2.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  28 IGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKrGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRPGAT 107
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK-PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 108 YTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHLRAEDLE--GIDASRLHLIEIPAMAI 185
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEklLLPGGRIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896154412 186 SSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
13-220 4.90e-45

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 151.09  E-value: 4.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  13 HAALTAKSAEAPRqRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKrgRKVSHSEDRYLMTVIATAS-- 90
Cdd:PRK06973  10 PNAEPAPPLARPR-RIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQK--ADVSAAEHRLAMTRAAAASlv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  91 --NPQFSVSRVDIDRPGATYTVDTLRDLKVIY-PNADLFFITGADALQKIMTWRDWEEMFDAATFVGVTRPGVHL----- 162
Cdd:PRK06973  87 lpGVTVRVATDEIEHAGPTYTVDTLARWRERIgPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLgaasp 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896154412 163 -----------RAEDLEGIDASRLHLIEIPAMAISSTDCR--------KRAEAGRPVWYLVPDGVVQYIAKRGLYQS 220
Cdd:PRK06973 167 avaaeiaarqaDADVLQATPAGHLLIDTTLAFDLSATDIRahlraciaRRAQVPDASAEHVPAAVWAYILQHRLYHR 243
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
26-218 2.48e-38

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 136.61  E-value: 2.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  26 QRIGVMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRPG 105
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 106 ATYTVDTLRDLKVIYPNADLFFITGADALQKIMTWRDWEEMFDAATFVgvtrpgVHLRAEDLEGIDASRLHLIEIPA--M 183
Cdd:PRK07152  81 VSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIV------VFKRKKNINKKNLKKYNVLLLKNknL 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896154412 184 AISSTDCRKRAEAGrpvwyLVPDGVVQYIAKRGLY 218
Cdd:PRK07152 155 NISSTKIRKGNLLG-----KLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 30-193 7.24e-27

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: 100.86  E-value: 7.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412   30 VMGGTFDPIHNGHLVAASEVADRFDLDFVLFVPTGEPWQKRGRKVSHSEDRYLMTVIATASNPQFSVSRVDIDRpgatyt 109
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  110 vDTLRDLkviypNADlFFITGADALQKImtWRDWEEMFDAATFVGVTRPGVHLRAEDLEGidasrlhlieipamaISSTD 189
Cdd:pfam01467  75 -ELLKEL-----NPD-VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFIPLKPTNG---------------ISSTD 130


                  ....
gi 896154412  190 CRKR 193
Cdd:pfam01467 131 IRER 134
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
27-221 1.35e-09

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 55.89  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  27 RIGVMGGTFDPIHNGHLvaasEVADR---FDLdfVLFVPT-GEPWqkrGRKVSHSEDRYLM--TVIATASNPQFSVSRVD 100
Cdd:PRK08887   3 KIAVFGSAFNPPSLGHK----SVIESlshFDL--VLLVPSiAHAW---GKTMLDYETRCQLvdAFIQDLGLSNVQRSDIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 101 --IDRPG-ATYTVDTLRDLKVIYPNADLFFITGADALQKImtwrdweemfdaATFvgvtrpgvhLRAEDLegidASRLHL 177
Cdd:PRK08887  74 qeLYAPDeSVTTYALLTRLQELYPEADLTFVIGPDNFLKF------------AKF---------YKADEI----TQRWTV 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 896154412 178 IEIP-AMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLYQSA 221
Cdd:PRK08887 129 MACPeKVPIRSTDIRNALQNGKDISHLTTPGVARLLKEHQLYTEP 173
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 28-163 1.82e-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: 54.75  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  28 IGVMGGTFDPIHNGHL----VAASEVADrfdlDFVLFVPTGEPWQKRGRKVSHSEDRYLMtvIATASNPQFSVSRVDIDR 103
Cdd:cd02039    1 VGIIIGRFEPFHLGHLklikEALEEALD----EVIIIIVSNPPKKKRNKDPFSLHERVEM--LKEILKDRLKVVPVDFPE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896154412 104 PGATYTVDTLrdLKVIYPNADLFFITGADALQKIMTWR--DWEEMFDAATFVGVTRPGVHLR 163
Cdd:cd02039   75 VKILLAVVFI--LKILLKVGPDKVVVGEDFAFGKNASYnkDLKELFLDIEIVEVPRVRDGKK 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 28-92 1.44e-08

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: 50.00  E-value: 1.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896154412   28 IGVMGGTFDPIHNGHLVAASEVADRFDlDFVLFVPTGE--PWQKrGRKVSHSEDRYLMTVIATASNP 92
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFD-ELIVGVGSDQfvNPLK-GEPVFSLEERLEMLKALKYVDE 65
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 33-218 1.95e-07

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: 50.38  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  33 GTFDPIHNGHL----VAASEV--ADRFDLDFVLFVPTGEPWQKRGrkVSHSEDRYLMTVIATASNPQFSVSRVDIDRPGA 106
Cdd:cd09286    7 GSFNPITNMHLrmfeLARDHLheTGRYEVVGGIISPVNDAYGKKG--LASAKHRVAMCRLAVQSSDWIRVDDWESLQPEW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 107 TYTVDTLRDLK--------VIYPNA-----------DLFFITGADALQKIMT---W--RDWEEMFDAATFVGVTRPG--V 160
Cdd:cd09286   85 MRTAKVLRHHReeinnkygGIEGAAkrvldgsrrevKIMLLCGADLLESFGIpglWkdADLEEILGEFGLVVVERTGsdP 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896154412 161 HLRAEDLEGIDASRLHLIEIPAMA---ISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:cd09286  165 ENFIASSDILRKYQDNIHLVKDWIpndISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 30-218 5.20e-07

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 49.30  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  30 VMGGTFDPIHNGHL----VAASEVADR-FDLDFVLFVPTGEPWQKRGrkVSHSEDRYLMTVIATASNPQFSVSRVDIDRP 104
Cdd:PLN02945  26 VATGSFNPPTYMHLrmfeLARDALMSEgYHVLGGYMSPVNDAYKKKG--LASAEHRIQMCQLACEDSDFIMVDPWEARQS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412 105 GATYTVDTLR--------DLKVIYPNADLFFITGADALQKIMT---WR--DWEEMFDAATFVGVTRPGvhlraEDLEGI- 170
Cdd:PLN02945 104 TYQRTLTVLArvetslnnNGLASEESVRVMLLCGSDLLESFSTpgvWIpdQVRTICRDYGVVCIRREG-----QDVEKLv 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896154412 171 -DASRLH--------LIEIPAMAISSTDCRKRAEAGRPVWYLVPDGVVQYIAKRGLY 218
Cdd:PLN02945 179 sQDEILNenrgnilvVDDLVPNSISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 30-51 1.17e-03

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440642  Cd Length: 154  Bit Score: 38.26  E-value: 1.17e-03
                         10        20
                 ....*....|....*....|....*
gi 896154412  30 VMGGTFDPIHNGH---LVAASEVAD 51
Cdd:COG1019    5 AVGGTFDPLHDGHralLERAFELGG 29
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 28-124 1.99e-03

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 37.64  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896154412  28 IGVMGGTFDPIHNGH---LVAASEVADRfdlDFVLFVPTGE------------PWQKRGRKVSHsedrYLMTViatasNP 92
Cdd:cd02164    1 KVAVGGTFDRLHDGHkilLSVAFLLAGE---KLIIGVTSDEllknkslkeliePYEERIANLHE----FLVDL-----KP 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896154412  93 QFSVSRVDIDRP-GATytvDTLRDLKVI------YPNAD 124
Cdd:cd02164   69 TLKYEIVPIDDPyGPT---GTDPDLEAIvvspetYPGAL 104
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
30-52 6.57e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 36.35  E-value: 6.57e-03
                         10        20
                 ....*....|....*....|....*.
gi 896154412  30 VMGGTFDPIHNGH---LVAASEVADR 52
Cdd:PRK00777   5 AVGGTFDPLHDGHralLRKAFELGKR 30
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 27-43 9.10e-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: 35.75  E-value: 9.10e-03
                         10
                 ....*....|....*..
gi 896154412  27 RIGVMGGTFDPIHNGHL 43
Cdd:COG0669    2 RIAVYPGSFDPITNGHL 18
 
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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