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Conserved domains on  [gi|491490555|ref|WP_005348291|]
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nicotinate-nucleotide adenylyltransferase [Aeromonas diversa]

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]; ...
5-211 3.39e-82

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: 243.10  E-value: 3.39e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   5 PLGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRA-SPFCTPEQRLAMVYLA-ANEFGLGVDERELRRDRP 82
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKhKPLASAEHRLAMLRLAiADNPRFEVSDIELERPGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  83 SWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEatapvqalLARHGTLrvddlhq 162
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDE--------LEELEAL------- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491490555 163 HRAGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
5-211 3.39e-82

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: 243.10  E-value: 3.39e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   5 PLGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRA-SPFCTPEQRLAMVYLA-ANEFGLGVDERELRRDRP 82
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKhKPLASAEHRLAMLRLAiADNPRFEVSDIELERPGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  83 SWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEatapvqalLARHGTLrvddlhq 162
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDE--------LEELEAL------- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491490555 163 HRAGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
6-211 3.34e-75

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: 225.20  E-value: 3.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   6 LGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRASPFCTPEQRLAMVYLAANEF-GLGVDERELRRDRPSW 84
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNpKFEVSDIEIKRDGPSY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALlarhgtlrvddlhqhR 164
Cdd:cd02165   81 TIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL---------------P 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491490555 165 AGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:cd02165  146 GGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
7-211 4.78e-71

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 215.08  E-value: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   7 GLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRA-SPFCTPEQRLAMVYLAANEF-GLGVDERELRRDRPSW 84
Cdd:PRK00071   7 GLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPqKPLAPLEHRLAMLELAIADNpRFSVSDIELERPGPSY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALLARHgtlrvddlhqhr 164
Cdd:PRK00071  87 TIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALQQLLEA------------ 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491490555 165 AGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:PRK00071 155 AGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
8-211 1.24e-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: 185.60  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555    8 LLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHR----ASPFctpEQRLAMVYLA-ANEFGLGVDERELRRDRP 82
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKktyeAASS---HHRLAMLKLAiEDNPKFEVDDFEIKRGGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   83 SWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALLARHgtlrvddlhq 162
Cdd:TIGR00482  78 SYTIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHH---------- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491490555  163 hraGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:TIGR00482 148 ---GNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
8-186 1.79e-18

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: 78.13  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555    8 LLGGTFDPIHLGHLKpalAARDALRLGELRL---LPNRVPPHR-ASPFCTPEQRLAMVYLAAnefglGVDERELRRDrps 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLR---LLEQAKELFDEDLivgVPSDEPPHKlKRPLFSAEERLEMLELAK-----WVDEVIVVAP--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   84 wtIETLEELRHEL-PDtplCFLMGMDSLLSLpsWHRWDELLSLAHLVVSVRPgwdaaeatapvqallarhgtlrvddlhq 162
Cdd:pfam01467  70 --WELTRELLKELnPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRP---------------------------- 114
                         170       180
                  ....*....|....*....|....
gi 491490555  163 hragHIWLAHNEPQPLSSTEIRAR 186
Cdd:pfam01467 115 ----VFFIPLKPTNGISSTDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
5-211 3.39e-82

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: 243.10  E-value: 3.39e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   5 PLGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRA-SPFCTPEQRLAMVYLA-ANEFGLGVDERELRRDRP 82
Cdd:COG1057    3 RIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKhKPLASAEHRLAMLRLAiADNPRFEVSDIELERPGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  83 SWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEatapvqalLARHGTLrvddlhq 162
Cdd:COG1057   83 SYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDE--------LEELEAL------- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491490555 163 HRAGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
6-211 3.34e-75

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: 225.20  E-value: 3.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   6 LGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRASPFCTPEQRLAMVYLAANEF-GLGVDERELRRDRPSW 84
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNpKFEVSDIEIKRDGPSY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALlarhgtlrvddlhqhR 164
Cdd:cd02165   81 TIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL---------------P 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491490555 165 AGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:cd02165  146 GGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
7-211 4.78e-71

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 215.08  E-value: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   7 GLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHRA-SPFCTPEQRLAMVYLAANEF-GLGVDERELRRDRPSW 84
Cdd:PRK00071   7 GLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPqKPLAPLEHRLAMLELAIADNpRFSVSDIELERPGPSY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALLARHgtlrvddlhqhr 164
Cdd:PRK00071  87 TIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEALALPALQQLLEA------------ 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491490555 165 AGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:PRK00071 155 AGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
8-211 1.24e-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: 185.60  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555    8 LLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVPPHR----ASPFctpEQRLAMVYLA-ANEFGLGVDERELRRDRP 82
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKktyeAASS---HHRLAMLKLAiEDNPKFEVDDFEIKRGGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   83 SWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALLARHgtlrvddlhq 162
Cdd:TIGR00482  78 SYTIDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAILRMHH---------- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491490555  163 hraGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:TIGR00482 148 ---GNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
6-211 2.30e-44

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 148.39  E-value: 2.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   6 LGLLGGTFDPIHLGHLkpALAAR--DALRLGELRLLPNRVPPHRASpfCTP-EQRLAMVYLAANEFGLG-----VDEREL 77
Cdd:PRK06973  24 IGILGGTFDPIHDGHL--ALARRfaDVLDLTELVLIPAGQPWQKAD--VSAaEHRLAMTRAAAASLVLPgvtvrVATDEI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  78 RRDRPSWTIETLEELRHEL-PDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEATAPVQALLA-RHGtl 155
Cdd:PRK06973 100 EHAGPTYTVDTLARWRERIgPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLGAASPAVAAEIAaRQA-- 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491490555 156 RVDDLHQHRAGHIWLAHNEPQPLSSTEIRARLAAGND--------PGELLPESVANYIRNNRLY 211
Cdd:PRK06973 178 DADVLQATPAGHLLIDTTLAFDLSATDIRAHLRACIArraqvpdaSAEHVPAAVWAYILQHRLY 241
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
6-212 9.89e-29

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 110.04  E-value: 9.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   6 LGLLGGTFDPIHLGHLKPALAARDALRLGELRLLPNRVpphraSPFCT------PEQRLAMVYLAANEFG-LGVDERELR 78
Cdd:PRK07152   3 IAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYI-----NPFKKkqkasnGEHRLNMLKLALKNLPkMEVSDFEIK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  79 RDRPSWTIETLEELRHELPDTPLCFLMGMDSLLSLPSWHRWDELLSLAHLVVSVRPGWDAAEatapvqallarhgtlrvd 158
Cdd:PRK07152  78 RQNVSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKK------------------ 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491490555 159 DLHQHragHIWLAHNEPQPLSSTEIRarlaaGNDPGELLPESVANYIRNNRLYA 212
Cdd:PRK07152 140 NLKKY---NVLLLKNKNLNISSTKIR-----KGNLLGKLDPKVNDYINENFLYL 185
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
8-186 1.79e-18

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: 78.13  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555    8 LLGGTFDPIHLGHLKpalAARDALRLGELRL---LPNRVPPHR-ASPFCTPEQRLAMVYLAAnefglGVDERELRRDrps 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLR---LLEQAKELFDEDLivgVPSDEPPHKlKRPLFSAEERLEMLELAK-----WVDEVIVVAP--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555   84 wtIETLEELRHEL-PDtplCFLMGMDSLLSLpsWHRWDELLSLAHLVVSVRPgwdaaeatapvqallarhgtlrvddlhq 162
Cdd:pfam01467  70 --WELTRELLKELnPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRP---------------------------- 114
                         170       180
                  ....*....|....*....|....
gi 491490555  163 hragHIWLAHNEPQPLSSTEIRAR 186
Cdd:pfam01467 115 ----VFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
7-61 6.32e-08

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


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 48.07  E-value: 6.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491490555    7 GLLGGTFDPIHLGHLKpalAARDALRLGELRLLP----NRVPPHRASPFCTPEQRLAMV 61
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLD---LLERAKELFDELIVGvgsdQFVNPLKGEPVFSLEERLEML 57
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
11-211 2.63e-07

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 49.61  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  11 GTFDPIHLGHLKPALAARDALR-LGELRLLPNRVPP----HRASPFCTPEQRLAMVYLAANEFG-LGVDERELRRdrPSW 84
Cdd:cd09286    7 GSFNPITNMHLRMFELARDHLHeTGRYEVVGGIISPvndaYGKKGLASAKHRVAMCRLAVQSSDwIRVDDWESLQ--PEW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TiETLEELRHE------------------LPDTPLC----FLMGMDSLLSLPSWHRWD-----ELLSLAHLVVSVRPGWD 137
Cdd:cd09286   85 M-RTAKVLRHHreeinnkyggiegaakrvLDGSRREvkimLLCGADLLESFGIPGLWKdadleEILGEFGLVVVERTGSD 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491490555 138 aaeatapVQALLARHGTLRvddLHQHRaghIWLAHNEPQP-LSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:cd09286  164 -------PENFIASSDILR---KYQDN---IHLVKDWIPNdISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
11-211 4.42e-05

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 43.14  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  11 GTFDPIHLGHLKPALAARDALRLGELRLLPNRVPP-----HRASpFCTPEQRLAMVYLAANEFGL-GVDERELRRDRPSW 84
Cdd:PLN02945  29 GSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPvndayKKKG-LASAEHRIQMCQLACEDSDFiMVDPWEARQSTYQR 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491490555  85 TIETLEELRHEL------PDTPL--CFLMGMDSLLSL--PSWHRWDELLSLA--HLVVSVRpgwdaaEATAPVQALLARH 152
Cdd:PLN02945 108 TLTVLARVETSLnnnglaSEESVrvMLLCGSDLLESFstPGVWIPDQVRTICrdYGVVCIR------REGQDVEKLVSQD 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491490555 153 gtlrvDDLHQHRAGHIWLAHNEPQPLSSTEIRARLAAGNDPGELLPESVANYIRNNRLY 211
Cdd:PLN02945 182 -----EILNENRGNILVVDDLVPNSISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
178-206 7.33e-04

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 39.09  E-value: 7.33e-04
                         10        20
                 ....*....|....*....|....*....
gi 491490555 178 LSSTEIRARLAAGNDPGELLPESVANYIR 206
Cdd:PRK01153 127 YSGTEIRRRMIEGDPWEELVPKSVAEVIK 155
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
9-35 3.35e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 36.73  E-value: 3.35e-03
                         10        20
                 ....*....|....*....|....*..
gi 491490555   9 LGGTFDPIHLGHLKpaLAARdALRLGE 35
Cdd:PRK00777   6 VGGTFDPLHDGHRA--LLRK-AFELGK 29
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
9-35 7.16e-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: 35.94  E-value: 7.16e-03
                         10        20
                 ....*....|....*....|....*..
gi 491490555   9 LGGTFDPIHLGHLkpALAARdALRLGE 35
Cdd:COG1019    6 VGGTFDPLHDGHR--ALLER-AFELGG 29
 
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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