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Conserved domains on  [gi|19115395|ref|NP_594483|]
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nicotinamide-nucleotide adenylyltransferase [Schizosaccharomyces pombe]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10114920)

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
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 34-246 2.65e-35

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: 124.28  E-value: 2.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395  34 IYVLDSSFNPPHFAHLGMCLSIPK---GSQLLLLLSITNADKPVAPAAFNERILMMEKLKTLIHNCTVSVAICKHALFVD 110
Cdd:cd02165   1 IALFGGSFDPPHLGHLAIAEEALEelgLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395 111 KCRSI---SNKLGPREQVYLVGFDTLIRIldCKYYKEkamqqvlQPFFSCSQILCFSREVDGTTTDDQAQYLEKIKKsll 187
Cdd:cd02165  81 TIDTLeelRERYPNAELYFIIGSDNLIRL--PKWYDW-------EELLSLVHLVVAPRPGYPIEDASLEKLLLPGGR--- 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19115395 188 pnipsqwsekiklTKLKGNVGFGVSSTRARQAIISGdeETQRKIIPQEILNVIKVIQPY 246
Cdd:cd02165 149 -------------IILLDNPLLNISSTEIRERLKNG--KSIRYLLPPAVADYIKEHGLY 192
 
Name Accession Description Interval E-value
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 34-246 2.65e-35

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: 124.28  E-value: 2.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395  34 IYVLDSSFNPPHFAHLGMCLSIPK---GSQLLLLLSITNADKPVAPAAFNERILMMEKLKTLIHNCTVSVAICKHALFVD 110
Cdd:cd02165   1 IALFGGSFDPPHLGHLAIAEEALEelgLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395 111 KCRSI---SNKLGPREQVYLVGFDTLIRIldCKYYKEkamqqvlQPFFSCSQILCFSREVDGTTTDDQAQYLEKIKKsll 187
Cdd:cd02165  81 TIDTLeelRERYPNAELYFIIGSDNLIRL--PKWYDW-------EELLSLVHLVVAPRPGYPIEDASLEKLLLPGGR--- 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19115395 188 pnipsqwsekiklTKLKGNVGFGVSSTRARQAIISGdeETQRKIIPQEILNVIKVIQPY 246
Cdd:cd02165 149 -------------IILLDNPLLNISSTEIRERLKNG--KSIRYLLPPAVADYIKEHGLY 192
 
Name Accession Description Interval E-value
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 34-246 2.65e-35

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: 124.28  E-value: 2.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395  34 IYVLDSSFNPPHFAHLGMCLSIPK---GSQLLLLLSITNADKPVAPAAFNERILMMEKLKTLIHNCTVSVAICKHALFVD 110
Cdd:cd02165   1 IALFGGSFDPPHLGHLAIAEEALEelgLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115395 111 KCRSI---SNKLGPREQVYLVGFDTLIRIldCKYYKEkamqqvlQPFFSCSQILCFSREVDGTTTDDQAQYLEKIKKsll 187
Cdd:cd02165  81 TIDTLeelRERYPNAELYFIIGSDNLIRL--PKWYDW-------EELLSLVHLVVAPRPGYPIEDASLEKLLLPGGR--- 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19115395 188 pnipsqwsekiklTKLKGNVGFGVSSTRARQAIISGdeETQRKIIPQEILNVIKVIQPY 246
Cdd:cd02165 149 -------------IILLDNPLLNISSTEIRERLKNG--KSIRYLLPPAVADYIKEHGLY 192
 
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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