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Conserved domains on  [gi|254766685|sp|B3QYZ5|]
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RecName: Full=Probable nicotinate-nucleotide adenylyltransferase; AltName: Full=Deamido-NAD(+) diphosphorylase; AltName: Full=Deamido-NAD(+) pyrophosphorylase; AltName: Full=Nicotinate mononucleotide adenylyltransferase; Short=NaMN adenylyltransferase

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]; ...
 1-196 2.52e-67

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: 204.58  E-value: 2.52e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISK-NPLKGSAN-APEAHQLAMAKLMAEELgktgPVFEVSDWE 78
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGqPPHKKHKPlASAEHRLAMLRLAIADN----PRFEVSDIE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQ--QSSRIIPPERYTWV 156
Cdd:COG1057   77 LERPGPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDEleELEALKPGGRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254766685 157 QLD-LPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQ 196
Cdd:COG1057  157 DVPlLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-196 2.52e-67

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: 204.58  E-value: 2.52e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISK-NPLKGSAN-APEAHQLAMAKLMAEELgktgPVFEVSDWE 78
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGqPPHKKHKPlASAEHRLAMLRLAIADN----PRFEVSDIE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQ--QSSRIIPPERYTWV 156
Cdd:COG1057   77 LERPGPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDEleELEALKPGGRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254766685 157 QLD-LPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQ 196
Cdd:COG1057  157 DVPlLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-195 2.32e-59

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: 183.98  E-value: 2.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   4 IALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISK-NPLKGSANAPEAHQLAMAKLMAEELGKtgpvFEVSDWELRRA 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSAnPPHKPPKPASFEHRLEMLKLAIEDNPK----FEVSDIEIKRD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  83 GFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSSRIIPPERYTWVQLDLPL 162
Cdd:cd02165   77 GPSYTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGGRIILLDNPL 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 254766685 163 ---SSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:cd02165  157 lniSSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-196 1.66e-56

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 177.33  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSIS-KNPLKGSAN-APEAHQLAMAKLMAEELgktgPVFEVSDWE 78
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNpGPPHKPQKPlAPLEHRLAMLELAIADN----PRFSVSDIE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSS---RIIPPERYTW 155
Cdd:PRK00071  79 LERPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALpalQQLLEAAGAI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 254766685 156 VQLDLPL---SSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQ 196
Cdd:PRK00071 159 TLLDVPLlaiSSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-195 9.15e-53

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: 167.50  E-value: 9.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685    6 LFGGSFDPPHYGHFALCTLTRELFSPEKIILSIS-KNPLKGSAN-APEAHQLAMAKLMAEELGKtgpvFEVSDWELRRAG 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTaNPPHKKTYEaASSHHRLAMLKLAIEDNPK----FEVDDFEIKRGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   84 FSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSG-TQGEQQSSRIIPPE-RYTWVQLDLP 161
Cdd:TIGR00482  77 PSYTIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGyTLDKALLEKAILRMhHGNLTLLHNP 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 254766685  162 ---LSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:TIGR00482 157 rvpISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-169 7.51e-16

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: 70.81  E-value: 7.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685    6 LFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLK--GSANAPEAHQLAMAKLMAEelgkTGPVFEVSDWELrrag 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHklKRPLFSAEERLEMLELAKW----VDEVIVVAPWEL---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   84 fsyTIETLRhfhaiEPNAELLLcIGEDNYQIFekWKAYQEILQLAHLVVFARSGTqgeqqssrIIPPERYtwvqldLPLS 163
Cdd:pfam01467  73 ---TRELLK-----ELNPDVLV-IGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPT------NGIS 127


                  ....*.
gi 254766685  164 SSDLRR 169
Cdd:pfam01467 128 STDIRE 133
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-196 2.52e-67

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: 204.58  E-value: 2.52e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISK-NPLKGSAN-APEAHQLAMAKLMAEELgktgPVFEVSDWE 78
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGqPPHKKHKPlASAEHRLAMLRLAIADN----PRFEVSDIE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQ--QSSRIIPPERYTWV 156
Cdd:COG1057   77 LERPGPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDEleELEALKPGGRIILL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 254766685 157 QLD-LPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQ 196
Cdd:COG1057  157 DVPlLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-195 2.32e-59

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: 183.98  E-value: 2.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   4 IALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISK-NPLKGSANAPEAHQLAMAKLMAEELGKtgpvFEVSDWELRRA 82
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSAnPPHKPPKPASFEHRLEMLKLAIEDNPK----FEVSDIEIKRD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  83 GFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSSRIIPPERYTWVQLDLPL 162
Cdd:cd02165   77 GPSYTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLLPGGRIILLDNPL 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 254766685 163 ---SSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:cd02165  157 lniSSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-196 1.66e-56

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 177.33  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSIS-KNPLKGSAN-APEAHQLAMAKLMAEELgktgPVFEVSDWE 78
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNpGPPHKPQKPlAPLEHRLAMLELAIADN----PRFSVSDIE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSS---RIIPPERYTW 155
Cdd:PRK00071  79 LERPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALpalQQLLEAAGAI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 254766685 156 VQLDLPL---SSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQ 196
Cdd:PRK00071 159 TLLDVPLlaiSSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-195 9.15e-53

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: 167.50  E-value: 9.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685    6 LFGGSFDPPHYGHFALCTLTRELFSPEKIILSIS-KNPLKGSAN-APEAHQLAMAKLMAEELGKtgpvFEVSDWELRRAG 83
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTaNPPHKKTYEaASSHHRLAMLKLAIEDNPK----FEVDDFEIKRGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   84 FSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSG-TQGEQQSSRIIPPE-RYTWVQLDLP 161
Cdd:TIGR00482  77 PSYTIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGyTLDKALLEKAILRMhHGNLTLLHNP 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 254766685  162 ---LSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:TIGR00482 157 rvpISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
2-198 3.30e-37

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 131.61  E-value: 3.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   2 KKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSIS-KNPLKGSANAPEA-HQLAMAKLMAEELGKtgpvFEVSDWEL 79
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTyINPFKKKQKASNGeHRLNMLKLALKNLPK----MEVSDFEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  80 RRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQssriipPERYTWVQLD 159
Cdd:PRK07152  77 KRQNVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKN------LKKYNVLLLK 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 254766685 160 ---LPLSSSDLRREIAEGqdwqaKMPSSIAAHIAAHRLYQNE 198
Cdd:PRK07152 151 nknLNISSTKIRKGNLLG-----KLDPKVNDYINENFLYLED 187
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
3-197 5.25e-28

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 105.25  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   3 KIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLKGSANAPEAHQLAMAKLMAEELGKTGPVFEVSDWELRRA 82
Cdd:PRK06973  23 RIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSAAEHRLAMTRAAAASLVLPGVTVRVATDEIEHA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  83 GFSYTIETLRHFHA-IEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSG-------------TQGEQQSSRII 148
Cdd:PRK06973 103 GPTYTVDTLARWRErIGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGfdlgaaspavaaeIAARQADADVL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254766685 149 --PPERYTWVQ--LDLPLSSSDLRREIAEGQDWQAKM--------PSSIAAHIAAHRLYQN 197
Cdd:PRK06973 183 qaTPAGHLLIDttLAFDLSATDIRAHLRACIARRAQVpdasaehvPAAVWAYILQHRLYHR 243
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-169 7.51e-16

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: 70.81  E-value: 7.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685    6 LFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLK--GSANAPEAHQLAMAKLMAEelgkTGPVFEVSDWELrrag 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHklKRPLFSAEERLEMLELAKW----VDEVIVVAPWEL---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   84 fsyTIETLRhfhaiEPNAELLLcIGEDNYQIFekWKAYQEILQLAHLVVFARSGTqgeqqssrIIPPERYtwvqldLPLS 163
Cdd:pfam01467  73 ---TRELLK-----ELNPDVLV-IGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPT------NGIS 127


                  ....*.
gi 254766685  164 SSDLRR 169
Cdd:pfam01467 128 STDIRE 133
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 9-195 2.16e-12

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: 63.48  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   9 GSFDPPHYGHFALCTLTRELFSPE------KIILSISKNPLKGSANAPEAHQLAMAKLMAEelgkTGPVFEVSDWELRRA 82
Cdd:cd09286    7 GSFNPITNMHLRMFELARDHLHETgryevvGGIISPVNDAYGKKGLASAKHRVAMCRLAVQ----SSDWIRVDDWESLQP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  83 GFSYTIETLRHFH--------AIEPNAELLLCIGEDNYQI--------FEK------WKA--YQEILQLAHLVVFARSGT 138
Cdd:cd09286   83 EWMRTAKVLRHHReeinnkygGIEGAAKRVLDGSRREVKImllcgadlLESfgipglWKDadLEEILGEFGLVVVERTGS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254766685 139 QGEQ--QSSRIIPPERYT------WVQLDlpLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:cd09286  163 DPENfiASSDILRKYQDNihlvkdWIPND--ISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-195 5.92e-11

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 58.58  E-value: 5.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   1 MKKIALFGGSFDPPHYGHFalcTLTRELFSPEKIILSISKNPLKGSANAPEAHQLAMAKLMAEELGKtgPVFEVSDWE-- 78
Cdd:PRK08887   1 MKKIAVFGSAFNPPSLGHK---SVIESLSHFDLVLLVPSIAHAWGKTMLDYETRCQLVDAFIQDLGL--SNVQRSDIEqe 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  79 LRRAGFS-YTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILqlahlvvfarsgtqgeQQSSRIIPPERytwvq 157
Cdd:PRK08887  76 LYAPDESvTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEIT----------------QRWTVMACPEK----- 134

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 254766685 158 ldLPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:PRK08887 135 --VPIRSTDIRNALQNGKDISHLTTPGVARLLKEHQLY 170
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 9-195 3.45e-08

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 51.61  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   9 GSFDPPHYGHFALCTLTR-ELFSPEKIILSISKNPL----KGSANAPEAHQLAMAKLMAEElgktGPVFEVSDWELRRAG 83
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARdALMSEGYHVLGGYMSPVndayKKKGLASAEHRIQMCQLACED----SDFIMVDPWEARQST 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685  84 FSYTIETLRHFHAI---------EPNAELLLCiGEDNYQIFEK---WKAYQ--EILQLAHLVVFARSGTQGEQ--QSSRI 147
Cdd:PLN02945 105 YQRTLTVLARVETSlnnnglaseESVRVMLLC-GSDLLESFSTpgvWIPDQvrTICRDYGVVCIRREGQDVEKlvSQDEI 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254766685 148 IPPERYTWVQLD--LP--LSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLY 195
Cdd:PLN02945 184 LNENRGNILVVDdlVPnsISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-60 1.84e-07

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 46.53  E-value: 1.84e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254766685    4 IALFGGSFDPPHYGHFALCTLTRELFspEKIILSI----SKNPLKGSANAPEAHQLAMAKL 60
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVgsdqFVNPLKGEPVFSLEERLEMLKA 59
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-46 4.77e-06

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


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 44.57  E-value: 4.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 254766685    4 IALFGGSFDPPHYGHFALCTLTRELFspEKIILSISKNPLKGS 46
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALF--DEVIVAVAKNPSKKP 41
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-44 1.17e-04

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: 40.76  E-value: 1.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254766685   2 KKIALFGGSFDPPHYGHFALctLTR--ELFspEKIILSISKNPLK 44
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDI--IERaaKLF--DEVIVAVAVNPSK 41
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-147 2.90e-04

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: 39.35  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254766685   4 IALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLKGSANAPEAHQLAMAklMAEELGKtgPVFEVSDWELRRAG 83
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKKRNKDPFSLHERVE--MLKEILK--DRLKVVPVDFPEVK 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254766685  84 FSYT-IETLRHFHAIEPnaeLLLCIGEDNYQIFEKW--KAYQEILQLAHLVVFARSGTQGEQQSSRI 147
Cdd:cd02039   77 ILLAvVFILKILLKVGP---DKVVVGEDFAFGKNASynKDLKELFLDIEIVEVPRVRDGKKISSTLI 140
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-44 4.27e-04

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 38.99  E-value: 4.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 254766685   4 IALFGGSFDPPHYGHFALCTLTRELFspEKIILSISKNPLK 44
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLF--DEVIVAVAVNPSK 39
 
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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