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Conserved domains on  [gi|546770421|ref|WP_021892493|]
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MULTISPECIES: nicotinate (nicotinamide) nucleotide adenylyltransferase [Barnesiella]

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]; ...
 5-193 5.58e-81

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


:

Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 238.87  E-value: 5.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   5 KTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRP 84
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  85 SYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLP------ANVKLCHAPIIE 158
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELealkpgGRIILLDVPLLD 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 546770421 159 ISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:COG1057  163 ISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 5-193 5.58e-81

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 238.87  E-value: 5.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   5 KTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRP 84
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  85 SYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLP------ANVKLCHAPIIE 158
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELealkpgGRIILLDVPLLD 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 546770421 159 ISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:COG1057  163 ISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-193 6.24e-76

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 226.64  E-value: 6.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   1 MQPIKTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFT 80
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  81 LPRPSYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLPA---------NVKL 151
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPAlqqlleaagAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 546770421 152 CHAPIIEISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 6-192 2.43e-64

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: 196.69  E-value: 2.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   6 TAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDrQRIEMLNMAVNGNSKIRTTDIEFTLPRPS 85
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFE-HRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  86 YTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLPANVKLC------HAPIIEI 159
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGgriillDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 546770421 160 SSTQIRQGISEGKNMNYFIPRPVYDYIINHGLY 192
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 8-192 1.26e-59

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: 184.83  E-value: 1.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421    8 FFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRPSYT 87
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   88 IQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLP--------ANVKLCHAPIIEI 159
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEkailrmhhGNLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 546770421  160 SSTQIRQGISEGKNMNYFIPRPVYDYIINHGLY 192
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 8-166 2.36e-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: 69.27  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421    8 FFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEftlprpsyt 87
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWE--------- 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546770421   88 iQTLEALRKKHPErifTLIIGADNWLSFnrWKDYDKIIEEYPIYIYPRRGYDIDErslpanvklchAPIIEISSTQIRQ 166
Cdd:pfam01467  72 -LTRELLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFIPL-----------KPTNGISSTDIRE 133
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 5-193 5.58e-81

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 238.87  E-value: 5.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   5 KTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRP 84
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERPGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  85 SYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLP------ANVKLCHAPIIE 158
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEELealkpgGRIILLDVPLLD 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 546770421 159 ISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:COG1057  163 ISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-193 6.24e-76

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 226.64  E-value: 6.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   1 MQPIKTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFT 80
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  81 LPRPSYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLPA---------NVKL 151
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPAlqqlleaagAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 546770421 152 CHAPIIEISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 6-192 2.43e-64

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: 196.69  E-value: 2.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   6 TAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDrQRIEMLNMAVNGNSKIRTTDIEFTLPRPS 85
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFE-HRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  86 YTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLPANVKLC------HAPIIEI 159
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGgriillDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 546770421 160 SSTQIRQGISEGKNMNYFIPRPVYDYIINHGLY 192
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 8-192 1.26e-59

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: 184.83  E-value: 1.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421    8 FFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRPSYT 87
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   88 IQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLP--------ANVKLCHAPIIEI 159
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEkailrmhhGNLTLLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 546770421  160 SSTQIRQGISEGKNMNYFIPRPVYDYIINHGLY 192
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
5-192 2.86e-40

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 139.70  E-value: 2.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   5 KTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTLPRP 84
Cdd:PRK07152   2 KIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQNV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  85 SYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYDIDERSLPANVKLCHAPIIEISSTQI 164
Cdd:PRK07152  82 SYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNLKKYNVLLLKNKNLNISSTKI 161

                        170       180
                 ....*....|....*....|....*...
gi 546770421 165 RQGisegkNMNYFIPRPVYDYIINHGLY 192
Cdd:PRK07152 162 RKG-----NLLGKLDPKVNDYINENFLY 184
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
2-194 6.26e-20

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 84.07  E-value: 6.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   2 QPIKTAFFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDrqRIEMLNMA----VNGNSKIRTTDI 77
Cdd:PRK06973  20 RPRRIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSAAEH--RLAMTRAAaaslVLPGVTVRVATD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  78 EFTLPRPSYTIQTLEALRKKH-PERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRGYD-----------IDERSL 145
Cdd:PRK06973  98 EIEHAGPTYTVDTLARWRERIgPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDlgaaspavaaeIAARQA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546770421 146 PANVKLC----HAPI-----IEISSTQIRQGISEGKNMNYFIPRP--------VYDYIINHGLYKN 194
Cdd:PRK06973 178 DADVLQAtpagHLLIdttlaFDLSATDIRAHLRACIARRAQVPDAsaehvpaaVWAYILQHRLYHR 243
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 11-192 7.92e-16

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: 72.72  E-value: 7.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  11 GTFNPVHTGHLIL----ANYLCEYEGFDEIWLSVSPQNPLREK--LSSNNDRqrIEMLNMAVNGNSKIRTTDIEFTlpRP 84
Cdd:cd09286    7 GSFNPITNMHLRMfelaRDHLHETGRYEVVGGIISPVNDAYGKkgLASAKHR--VAMCRLAVQSSDWIRVDDWESL--QP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  85 SY--TIQTLEALRKK----------------HPERI---FTLIIGADNWLSF---NRWKDYD--KIIEEYPIYIYPRRGY 138
Cdd:cd09286   83 EWmrTAKVLRHHREEinnkyggiegaakrvlDGSRRevkIMLLCGADLLESFgipGLWKDADleEILGEFGLVVVERTGS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546770421 139 DIDER--SLPANVKLCHAPII-------EISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLY 192
Cdd:cd09286  163 DPENFiaSSDILRKYQDNIHLvkdwipnDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 8-166 2.36e-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: 69.27  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421    8 FFSGTFNPVHTGHLILANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEftlprpsyt 87
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWE--------- 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546770421   88 iQTLEALRKKHPErifTLIIGADNWLSFnrWKDYDKIIEEYPIYIYPRRGYDIDErslpanvklchAPIIEISSTQIRQ 166
Cdd:pfam01467  72 -LTRELLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVFFIPL-----------KPTNGISSTDIRE 133
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
5-193 3.78e-15

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 69.76  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   5 KTAFFSGTFNPVHTGHLILANYLCEyegFDEIWLSVSPQNPL-REKLSSNNdrqRIEMLNMAVN--GNSKIRTTDIE--- 78
Cdd:PRK08887   3 KIAVFGSAFNPPSLGHKSVIESLSH---FDLVLLVPSIAHAWgKTMLDYET---RCQLVDAFIQdlGLSNVQRSDIEqel 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  79 FTLPRPSYTIQTLEALRKKHPERIFTLIIGADNWLSFNRWKDYDKIIEEYPIYIYPRRgydiderslpanvklchapiIE 158
Cdd:PRK08887  77 YAPDESVTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMACPEK--------------------VP 136

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 546770421 159 ISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:PRK08887 137 IRSTDIRNALQNGKDISHLTTPGVARLLKEHQLYT 171
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 11-193 1.46e-08

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 52.77  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  11 GTFNPVHTGHLI---LANYLCEYEGFDEIWLSVSPQNPLREKLSSNNDRQRIEMLNMAVNGNSKIRTTDIEFTlpRPSYT 87
Cdd:PLN02945  29 GSFNPPTYMHLRmfeLARDALMSEGYHVLGGYMSPVNDAYKKKGLASAEHRIQMCQLACEDSDFIMVDPWEAR--QSTYQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  88 iQTLEALRKKH------------PERIFtLIIGADNWLSFNR---WKDYD--KIIEEYPIYIYPRRGYDIdERSLPANVK 150
Cdd:PLN02945 107 -RTLTVLARVEtslnnnglaseeSVRVM-LLCGSDLLESFSTpgvWIPDQvrTICRDYGVVCIRREGQDV-EKLVSQDEI 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 546770421 151 L--CHAPII--------EISSTQIRQGISEGKNMNYFIPRPVYDYIINHGLYK 193
Cdd:PLN02945 184 LneNRGNILvvddlvpnSISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLYM 236
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 7-166 4.15e-07

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: 47.43  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421   7 AFFSGTFNPVHTGHLILANYLCEyEGFDEIWLSV---SPQNPLREKLSSNNDrqRIEMLNMAVngNSKIRTTDIEFTLPR 83
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALE-EALDEVIIIIvsnPPKKKRNKDPFSLHE--RVEMLKEIL--KDRLKVVPVDFPEVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546770421  84 PSYTIQTLEALRKKHPERIFtlIIGADNWLSFNRWKDYDKIIEEYPIYIYprrGYDIDERSLPanvklchapiieISSTQ 163
Cdd:cd02039   77 ILLAVVFILKILLKVGPDKV--VVGEDFAFGKNASYNKDLKELFLDIEIV---EVPRVRDGKK------------ISSTL 139


                 ...
gi 546770421 164 IRQ 166
Cdd:cd02039  140 IRE 142
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 7-62 2.03e-04

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: 38.06  E-value: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 546770421    7 AFFSGTFNPVHTGHLILANYLCEYegFDEIWLSVSP---QNPLReKLSSNNDRQRIEML 62
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKEL--FDELIVGVGSdqfVNPLK-GEPVFSLEERLEML 57
 
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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