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Conserved domains on  [gi|446761631|ref|WP_000838887|]
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MULTISPECIES: nicotinate-nucleotide adenylyltransferase [Enterobacteriaceae]

Protein Classification

nicotinate-nucleotide adenylyltransferase( domain architecture ID 10011203)

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

EC:  2.7.7.18
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 PRK00071
nicotinate-nucleotide adenylyltransferase;
1-213 7.94e-91

nicotinate-nucleotide adenylyltransferase;


:

Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 7.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   1 MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQ-PEANSVQRKHMLELAIADKPLFTLDERELKR 79
Cdd:PRK00071   2 MMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  80 NAPSYTAQTLKEWRqEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLE-MAQPQYQQWLEDHlthnp 158
Cdd:PRK00071  82 PGPSYTIDTLRELR-ARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEaLALPALQQLLEAA----- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446761631 159 edlhlqpaGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:PRK00071 156 --------GAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-213 7.94e-91

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 7.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   1 MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQ-PEANSVQRKHMLELAIADKPLFTLDERELKR 79
Cdd:PRK00071   2 MMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  80 NAPSYTAQTLKEWRqEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLE-MAQPQYQQWLEDHlthnp 158
Cdd:PRK00071  82 PGPSYTIDTLRELR-ARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEaLALPALQQLLEAA----- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446761631 159 edlhlqpaGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:PRK00071 156 --------GAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 6-213 9.49e-90

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: 261.98  E-value: 9.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQ-PEANSVQRKHMLELAIADKPLFTLDERELKRNAPSY 84
Cdd:COG1057    5 GIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHkPLASAEHRLAMLRLAIADNPRFEVSDIELERPGPSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  85 TAQTLKEWRQEQgPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPL-EMAQPQyqqwledhlthnpedlHL 163
Cdd:COG1057   85 TIDTLRELREEY-PDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELdELEELE----------------AL 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446761631 164 QPAGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 7-212 8.30e-89

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: 259.56  E-value: 8.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631    7 LFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRP-QPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYT 85
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKtYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   86 AQTLKEWRQEQgPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWLEDHlthnpedlhlqp 165
Cdd:TIGR00482  81 IDTLKHLKKKY-PDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHH------------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446761631  166 aGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLY 212
Cdd:TIGR00482 148 -GNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 6-212 3.75e-80

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: 237.53  E-value: 3.75e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYT 85
Cdd:cd02165    2 ALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSYT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  86 AQTLKEWRQeQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWledhlthnpedlhlqP 165
Cdd:cd02165   82 IDTLEELRE-RYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL---------------P 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446761631 166 AGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLY 212
Cdd:cd02165  146 GGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 7-187 2.72e-32

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: 113.57  E-value: 2.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631    7 LFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHR-PQPEANSVQRKHMLELAIADKPLFTLDERELKRnapsyt 85
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   86 aqtlkEWRQEQGPDVplaFIIGQDSLLTFptWYEYETILDNAHLIVCRRPGYplemaqpqyqqwledhlthnpedlhlqp 165
Cdd:pfam01467  75 -----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRPVF---------------------------- 116

                         170       180
                  ....*....|....*....|..
gi 446761631  166 agkiYLAETPWFNISATIIRER 187
Cdd:pfam01467 117 ----FIPLKPTNGISSTDIRER 134
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-213 7.94e-91

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 7.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   1 MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQ-PEANSVQRKHMLELAIADKPLFTLDERELKR 79
Cdd:PRK00071   2 MMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  80 NAPSYTAQTLKEWRqEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLE-MAQPQYQQWLEDHlthnp 158
Cdd:PRK00071  82 PGPSYTIDTLRELR-ARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEaLALPALQQLLEAA----- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446761631 159 edlhlqpaGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:PRK00071 156 --------GAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 6-213 9.49e-90

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: 261.98  E-value: 9.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQ-PEANSVQRKHMLELAIADKPLFTLDERELKRNAPSY 84
Cdd:COG1057    5 GIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHkPLASAEHRLAMLRLAIADNPRFEVSDIELERPGPSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  85 TAQTLKEWRQEQgPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPL-EMAQPQyqqwledhlthnpedlHL 163
Cdd:COG1057   85 TIDTLRELREEY-PDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELdELEELE----------------AL 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446761631 164 QPAGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 7-212 8.30e-89

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: 259.56  E-value: 8.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631    7 LFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRP-QPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYT 85
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKtYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   86 AQTLKEWRQEQgPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWLEDHlthnpedlhlqp 165
Cdd:TIGR00482  81 IDTLKHLKKKY-PDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHH------------ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446761631  166 aGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLY 212
Cdd:TIGR00482 148 -GNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 6-212 3.75e-80

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: 237.53  E-value: 3.75e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYT 85
Cdd:cd02165    2 ALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSYT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  86 AQTLKEWRQeQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWledhlthnpedlhlqP 165
Cdd:cd02165   82 IDTLEELRE-RYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL---------------P 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446761631 166 AGKIYLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQQGLY 212
Cdd:cd02165  146 GGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
7-213 2.05e-37

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 130.29  E-value: 2.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   7 LFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEAnSVQRKHMLELAIADKPL----FTLDERELKRNAP 82
Cdd:PRK06973  26 ILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSA-AEHRLAMTRAAAASLVLpgvtVRVATDEIEHAGP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  83 SYTAQTLKEWRQEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWLEDHLThNPEDLH 162
Cdd:PRK06973 105 TYTVDTLARWRERIGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLGAASPAVAAEIAARQA-DADVLQ 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446761631 163 LQPAGKIYLAETPWFNISATIIRERL--------QNGESCDDLLPEPVLTYINQQGLYR 213
Cdd:PRK06973 184 ATPAGHLLIDTTLAFDLSATDIRAHLraciarraQVPDASAEHVPAAVWAYILQHRLYH 242
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 7-187 2.72e-32

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: 113.57  E-value: 2.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631    7 LFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHR-PQPEANSVQRKHMLELAIADKPLFTLDERELKRnapsyt 85
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   86 aqtlkEWRQEQGPDVplaFIIGQDSLLTFptWYEYETILDNAHLIVCRRPGYplemaqpqyqqwledhlthnpedlhlqp 165
Cdd:pfam01467  75 -----ELLKELNPDV---LVIGADSLLDF--WYELDEILGNVKLVVVVRPVF---------------------------- 116

                         170       180
                  ....*....|....*....|..
gi 446761631  166 agkiYLAETPWFNISATIIRER 187
Cdd:pfam01467 117 ----FIPLKPTNGISSTDIRER 134
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
6-212 6.80e-32

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 118.13  E-value: 6.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQ-RKHMLELAIADKPLFTLDERELKRNAPSY 84
Cdd:PRK07152   4 AIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEhRLNMLKLALKNLPKMEVSDFEIKRQNVSY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  85 TAQTLKEWRQeQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYqqwledhlthnpedlhlq 164
Cdd:PRK07152  84 TIDTIKYFKK-KYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNLKKY------------------ 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446761631 165 pagKIYLAETPWFNISATIIRerlqNGEScDDLLPEPVLTYINQQGLY 212
Cdd:PRK07152 145 ---NVLLLKNKNLNISSTKIR----KGNL-LGKLDPKVNDYINENFLY 184
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 6-68 4.66e-13

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: 61.55  E-value: 4.66e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446761631    6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIP-NNVPPHRPQPEANSVQRKHMLELAIADKP 68
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSdQFVNPLKGEPVFSLEERLEMLKALKYVDE 65
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 10-212 1.39e-09

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: 55.77  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  10 GTFDPVHYGHLKPVEtLAN--LIGLTRVTIIPNNVPP----HRPQPEANSVQRKHMLELAIADKPLFTLDERELKRNAPS 83
Cdd:cd09286    7 GSFNPITNMHLRMFE-LARdhLHETGRYEVVGGIISPvndaYGKKGLASAKHRVAMCRLAVQSSDWIRVDDWESLQPEWM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  84 YTAQTLKEWRQE----------------QGPDVP--LAFIIGQDSLLTFPT---WYE--YETILDNAHLIVCRRPGyple 140
Cdd:cd09286   86 RTAKVLRHHREEinnkyggiegaakrvlDGSRREvkIMLLCGADLLESFGIpglWKDadLEEILGEFGLVVVERTG---- 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446761631 141 mAQPQYQQWLEDHLTHNPEDLHLQpagkiylaeTPWFN--ISATIIRERLQNGESCDDLLPEPVLTYINQQGLY 212
Cdd:cd09286  162 -SDPENFIASSDILRKYQDNIHLV---------KDWIPndISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 6-118 7.59e-08

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: 49.75  E-value: 7.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANlIGLTRVTIIPNNVPPHRPQPE--ANSVQRKHMLELAIADKP-LFTLDERELKrnaP 82
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALE-EALDEVIIIIVSNPPKKKRNKdpFSLHERVEMLKEILKDRLkVVPVDFPEVK---I 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446761631  83 SYTAQTLKEWRQEQGPDVplaFIIGQDSLLTFPTWY 118
Cdd:cd02039   78 LLAVVFILKILLKVGPDK---VVVGEDFAFGKNASY 110
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 55-213 4.86e-06

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 45.83  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  55 QRKHMLELAIADKPLFTLDERELKRnaPSYTaQTL----------KEWRQEQGPDVPLAFIIGQDSLLTFPT---WY--E 119
Cdd:PLN02945  78 HRIQMCQLACEDSDFIMVDPWEARQ--STYQ-RTLtvlarvetslNNNGLASEESVRVMLLCGSDLLESFSTpgvWIpdQ 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631 120 YETILDNaHLIVC-RRPGYPLEmaqpqyqqwledHLTHNPEDLHLQPAGKIYLAETPWFNISATIIRERLQNGESCDDLL 198
Cdd:PLN02945 155 VRTICRD-YGVVCiRREGQDVE------------KLVSQDEILNENRGNILVVDDLVPNSISSTRVRECISRGLSVKYLT 221

                        170
                 ....*....|....*
gi 446761631 199 PEPVLTYINQQGLYR 213
Cdd:PLN02945 222 PDGVIDYIKEHGLYM 236
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 6-203 3.81e-05

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: 42.26  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631    6 ALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNnvpPHRpqpeansvqrkhmlelaiadKPLFTLDER-ELKRNAPSy 84
Cdd:TIGR01510   2 ALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKN---PSK--------------------KPLFSLEERvELIKDATK- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   85 taqtlkewrqeqgpDVPLAFIIGQDSLLTfptwyEYETILDNAHLIVCRRPG----YPLEMAqpqyqqWLEDHLTHNPED 160
Cdd:TIGR01510  58 --------------HLPNVRVDVFDGLLV-----DYAKELGATFIVRGLRAAtdfeYELQMA------LMNKHLAPEIET 112

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446761631  161 LHLqpagkiyLAETPWFNISATIIRERLQNGESCDDLLPEPVL 203
Cdd:TIGR01510 113 VFL-------MASPEYAFVSSSLVKEIASFGGDVSNLVPPAVA 148
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 6-208 6.14e-05

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: 41.68  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIglTRVTIipnnvpphrpqpeansvqrkhmlelAIAD----KPLFTLDER-ELKRn 80
Cdd:cd02163    2 AVYPGSFDPITNGHLDIIERASKLF--DEVIV-------------------------AVAVnpskKPLFSLEERvELIR- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  81 apsytaQTLKEWrqeqgPDVplaFIIGQDSLLTfptwyEYETILdNAHLIVcR--RPG----YPLEMAqpqyqqWLEDHL 154
Cdd:cd02163   54 ------EATKHL-----PNV---EVDGFDGLLV-----DFARKH-GANVIV-RglRAVsdfeYEFQMA------GMNRKL 106

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446761631 155 THNPEDLHLqpagkiyLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQ 208
Cdd:cd02163  107 APEIETVFL-------MASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 6-208 8.14e-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: 38.44  E-value: 8.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631   6 ALFGGTFDPVHYGHLKPVETLANLIGltRVTIipnnvpphrpqpeansvqrkhmlelAIAD----KPLFTLDER-ELKRn 80
Cdd:COG0669    4 AVYPGSFDPITNGHLDIIERAAKLFD--EVIV-------------------------AVAVnpskKPLFSLEERvELIR- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446761631  81 apsytaQTLKEWrqeqgPDVplaFIIGQDSLLTfptwyeyetilD-----NAHLIVcR--RPG----YPLEMAQpqyqqw 149
Cdd:COG0669   56 ------EALADL-----PNV---EVDSFDGLLV-----------DfarevGANVIV-RglRAVsdfeYEFQMAL------ 103

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446761631 150 LEDHLTHNPEDLHLqpagkiyLAETPWFNISATIIRERLQNGESCDDLLPEPVLTYINQ 208
Cdd:COG0669  104 MNRKLAPEIETVFL-------MTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKE 155
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
9-37 8.16e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 35.58  E-value: 8.16e-03
                         10        20
                 ....*....|....*....|....*....
gi 446761631   9 GGTFDPVHYGHLKPVETlANLIGlTRVTI 37
Cdd:PRK00777   7 GGTFDPLHDGHRALLRK-AFELG-KRVTI 33
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 9-33 9.45e-03

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


Pssm-ID: 440642  Cd Length: 154  Bit Score: 35.56  E-value: 9.45e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 446761631   9 GGTFDPVHYGHLKPVET---LAN--LIGLT 33
Cdd:COG1019    7 GGTFDPLHDGHRALLERafeLGGdvIIGLT 36
 
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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