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Conserved domains on  [gi|502850097|ref|WP_013085073|]
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MULTISPECIES: nicotinate-nucleotide adenylyltransferase [Priestia]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10003000)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-187 2.11e-95

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: 275.46  E-value: 2.11e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPY---------PIKEVEVPQ 151
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502850097 152 FDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-187 2.11e-95

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: 275.46  E-value: 2.11e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPY---------PIKEVEVPQ 151
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502850097 152 FDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-189 1.03e-90

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 263.62  E-value: 1.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITS------------PYPIKEVE 148
Cdd:PRK00071  83 GPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITLLD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 502850097 149 VPQFDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLYES 189
Cdd:PRK00071 163 VPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-187 2.72e-79

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: 234.44  E-value: 2.72e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   4 IGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTiKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERKEPS 83
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKP-PKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  84 YTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPYP---------IKEVEVPQFDV 154
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 502850097 155 SSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-187 5.97e-70

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: 210.64  E-value: 5.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097    6 ILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERKEPSYT 85
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   86 YDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPYP-----------IKEVEVPQFDV 154
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLekailrmhhgnLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 502850097  155 SSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-162 2.22e-29

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: 105.48  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097    6 ILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERkepsyt 85
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502850097   86 ydtmRILTEKYPTYqfhFIVGADMVEYLpkWYEIDELVNLVTFVGVKRPGYTItspypikeVEVPQFDVSSSFIRER 162
Cdd:pfam01467  75 ----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFI--------PLKPTNGISSTDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-187 2.11e-95

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: 275.46  E-value: 2.11e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPY---------PIKEVEVPQ 151
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502850097 152 FDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-189 1.03e-90

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 263.62  E-value: 1.03e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITS------------PYPIKEVE 148
Cdd:PRK00071  83 GPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITLLD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 502850097 149 VPQFDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLYES 189
Cdd:PRK00071 163 VPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYRS 203
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-187 2.72e-79

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: 234.44  E-value: 2.72e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   4 IGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTiKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERKEPS 83
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKP-PKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  84 YTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPYP---------IKEVEVPQFDV 154
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 502850097 155 SSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-187 5.97e-70

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: 210.64  E-value: 5.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097    6 ILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERKEPSYT 85
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   86 YDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPYP-----------IKEVEVPQFDV 154
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLekailrmhhgnLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 502850097  155 SSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-187 4.78e-46

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 154.33  E-value: 4.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKsIGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERK 80
Cdd:PRK07152   1 MK-IAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  81 EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGY---TITSPYPIKEVEVPQFDVSSS 157
Cdd:PRK07152  80 NVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNinkKNLKKYNVLLLKNKNLNISST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 502850097 158 FIRervvkKETIRYFIPAGVKQYIEENQLY 187
Cdd:PRK07152 160 KIR-----KGNLLGKLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-162 2.22e-29

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: 105.48  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097    6 ILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFERkepsyt 85
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502850097   86 ydtmRILTEKYPTYqfhFIVGADMVEYLpkWYEIDELVNLVTFVGVKRPGYTItspypikeVEVPQFDVSSSFIRER 162
Cdd:pfam01467  75 ----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFI--------PLKPTNGISSTDIRER 134
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
4-189 2.00e-25

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 98.32  E-value: 2.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   4 IGILGGTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPPHKTIKEPIEpyHRLHMLKLAIEE----HDQFTLQPIEFER 79
Cdd:PRK06973  24 IGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSAAE--HRLAMTRAAAASlvlpGVTVRVATDEIEH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  80 KEPSYTYDTMRILTEKY-PTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRPGYTITSPYPIKEVEVPQ------- 151
Cdd:PRK06973 102 AGPTYTVDTLARWRERIgPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLGAASPAVAAEIAArqadadv 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502850097 152 ----------------FDVSSSFIRERVVKKETIRYF--------IPAGVKQYIEENQLYES 189
Cdd:PRK06973 182 lqatpaghllidttlaFDLSATDIRAHLRACIARRAQvpdasaehVPAAVWAYILQHRLYHR 243
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-162 7.77e-19

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: 78.64  E-value: 7.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   4 IGILGGTFNPPHLGHLMMANEVLHALkLDEIWFMPSYIPPHKTIKEPIEPYH-RLHMLKLAIEehDQFTLQPIEFERKEP 82
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEA-LDEVIIIIVSNPPKKKRNKDPFSLHeRVEMLKEILK--DRLKVVPVDFPEVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  83 SYTYDTMRILTEKYPtyQFHFIVGADMVEYLPKWY--EIDELVNLVTFVGVKRPGytitspypikevevPQFDVSSSFIR 160
Cdd:cd02039   78 LLAVVFILKILLKVG--PDKVVVGEDFAFGKNASYnkDLKELFLDIEIVEVPRVR--------------DGKKISSTLIR 141


                 ..
gi 502850097 161 ER 162
Cdd:cd02039  142 EL 143
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-189 1.68e-14

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 67.83  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLmmanEVLHALK-LDEIWFMPSYipPHKTIKEPIEPYHRLHMLKLAIEEHDQFTLQPIEFER 79
Cdd:PRK08887   1 MKKIAVFGSAFNPPSLGHK----SVIESLShFDLVLLVPSI--AHAWGKTMLDYETRCQLVDAFIQDLGLSNVQRSDIEQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  80 K-----EPSYTYDTMRILTEKYPTYQFHFIVGADMVEYLPKWYEIDELVNLVTFVGVKRpgytitspypikevEVPqfdV 154
Cdd:PRK08887  75 ElyapdESVTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMACPE--------------KVP---I 137

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 502850097 155 SSSFIRERVVKKETIRYFIPAGVKQYIEENQLYES 189
Cdd:PRK08887 138 RSTDIRNALQNGKDISHLTTPGVARLLKEHQLYTE 172
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 9-187 3.21e-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: 65.40  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   9 GTFNPPHLGHLMM---ANEVLHalKLDEIWFMPSYIPP-HKTIKEP--IEPYHRLHMLKLAIEEHDQFTLQPIEFERKEP 82
Cdd:cd09286    7 GSFNPITNMHLRMfelARDHLH--ETGRYEVVGGIISPvNDAYGKKglASAKHRVAMCRLAVQSSDWIRVDDWESLQPEW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  83 SYTYDTMRILTEKYPT-------------------YQFHFIVGADMVEYLPK---WYEID--ELVNLVTFVGVKR----P 134
Cdd:cd09286   85 MRTAKVLRHHREEINNkyggiegaakrvldgsrreVKIMLLCGADLLESFGIpglWKDADleEILGEFGLVVVERtgsdP 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502850097 135 GYTITSPYPIKE--------VEVPQFDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:cd09286  165 ENFIASSDILRKyqdnihlvKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-65 8.97e-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: 47.30  E-value: 8.97e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502850097    4 IGILGGTFNPPHLGHLMMANEvlhALKL--DEIWFMPS--YIPPHKtiKEPIEPY-HRLHMLKLAIE 65
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLER---AKELfdELIVGVGSdqFVNPLK--GEPVFSLeERLEMLKALKY 62
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 9-187 2.05e-05

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 43.52  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   9 GTFNPPHLGHLMMANEVLHALKLDEIWFMPSYIPP-----HKTIKEPIEpyHRLHMLKLAIEEHDQFTLQPieFERKEPS 83
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPvndayKKKGLASAE--HRIQMCQLACEDSDFIMVDP--WEARQST 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  84 YTyDTMRILTE-----------KYPTYQFHFIVGADMVEYLPK---WyeIDELVNLVT----FVGVKRPGYTITSPYPIK 145
Cdd:PLN02945 105 YQ-RTLTVLARvetslnnnglaSEESVRVMLLCGSDLLESFSTpgvW--IPDQVRTICrdygVVCIRREGQDVEKLVSQD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502850097 146 EV------------EVPQFDVSSSFIRERVVKKETIRYFIPAGVKQYIEENQLY 187
Cdd:PLN02945 182 EIlnenrgnilvvdDLVPNSISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 9-183 4.57e-03

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: 36.12  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   9 GTFNPPHLGHLMMANEVLHalKLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEhdqftlqpieferkepsYTYDT 88
Cdd:cd02166    6 GRFQPFHLGHLKVIKWILE--EVDELIIGIGSAQESHTLENPFTAGERVLMIRRALEE-----------------EGIDL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  89 MRILTEKYPTYQFHFIVGADMVEYLPKW---YEIDELVNLVtfvgVKRPGYTITSPypikevevPQFD---VSSSFIRER 162
Cdd:cd02166   67 SRYYIIPVPDIERNSLWVSYVESLTPPFdvvYSGNPLVARL----FKEAGYEVRRP--------PMFNreeYSGTEIRRL 134

                        170       180
                 ....*....|....*....|.
gi 502850097 163 VVKKETIRYFIPAGVKQYIEE 183
Cdd:cd02166  135 MLGGEDWEELVPKSVAEVIKE 155
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-184 6.65e-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: 35.56  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097   1 MKSIGILGGTFNPPHLGHLMManeVLHAL-KLDEIWFMPSYIPPHKTIKEPIEPYHRLHMLKLAIEEHDQFtlqpiefer 79
Cdd:COG1056    1 MMKRGLFIGRFQPFHLGHLAV---IKWALeEVDELIIGIGSAQESHTPRNPFTAGERIEMIRAALKEEGLS--------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502850097  80 kepsytydtmRILTEKYPTYQFHFIVGADMVEYLPKwyeIDELVNLVTFVGV--KRPGYTITSPypikevevPQFD---V 154
Cdd:COG1056   69 ----------RVYIVPIPDINNNSLWVSHVKSLVPP---FDVVYSNNPLVGRlfKEAGYEVLLP--------PLFEreeY 127

                        170       180       190
                 ....*....|....*....|....*....|
gi 502850097 155 SSSFIRERVVKKETIRYFIPAGVKQYIEEN 184
Cdd:COG1056  128 SGTEIRRLMLEGEDWESLVPPAVAEVIEEI 157
 
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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