Nmnat

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0034355 NAD+ biosynthetic process via the salvage pathway	IBA GO_REF:0000033	ACCEPT	Summary: Nmnat catalyzes the formation of NAD+ from NMN and ATP, the penultimate step in the NAD+ salvage pathway. This is its primary enzymatic function, confirmed by multiple experimental studies (PMID:17132048, PMID:19403820, PMID:26616331, PMID:36476387). The IBA annotation is well supported by phylogenetic inference across eukaryotic NMNATs. Reason: The NAD+ salvage pathway role is the core enzymatic function of Nmnat. Phylogenetic inference is fully consistent with extensive direct experimental evidence in Drosophila. Supporting Evidence: PMID:36476387 NMN-D delays neurodegeneration caused by loss of the sole NMN-consuming and NAD+-synthesizing enzyme dNmnat file:DROME/Nmnat/Nmnat-deep-research-falcon.md these mutation–activity relationships experimentally support that the enzyme’s primary biochemical role is NMN adenylyltransferase activity in NAD\(^+\) biosynthesis/salvage.
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: GO:0000309 represents the core molecular function of Nmnat: catalyzing the reaction NMN + ATP -> NAD+ + PPi. This has been directly demonstrated by multiple IDA-level experiments (PMID:17132048, PMID:19403820, PMID:36476387). The IBA annotation is consistent with the phylogenetic analysis showing this activity across the NMNAT family. Reason: This is the primary molecular function of Nmnat, confirmed experimentally and by phylogenetic inference. The IBA annotation is at the correct level of specificity. Supporting Evidence: PMID:19403820 Nmnat enzymes with diverse sequences and structures from various species PMID:36476387 the sole NMN-consuming and NAD+-synthesizing enzyme dNmnat file:DROME/Nmnat/Nmnat-deep-research-falcon.md recombinant dNmnat protein exhibits NMNAT activity comparable to human NMNAT3 in an in vitro coupled assay, and mutations in conserved catalytic/substrate-binding motifs sharply reduce enzymatic activity, confirming that CG13645 encodes a bona fide NMNAT enzyme.
GO:0004515 nicotinate-nucleotide adenylyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: GO:0004515 represents the NaMN adenylyltransferase activity (EC 2.7.7.18), converting nicotinate ribonucleotide + ATP to deamido-NAD+ + PPi. UniProt assigns EC 2.7.7.18 to Nmnat based on RuleBase evidence. The IBA annotation is phylogenetically inferred from orthologs across the NMNAT family, several of which have dual-substrate specificity. Reason: NMNAT family members characteristically possess dual-substrate specificity for both NMN (GO:0000309) and NaMN (GO:0004515). The IBA annotation is consistent with the known biochemistry of this enzyme family and the UniProt-assigned EC 2.7.7.18. Supporting Evidence: PMID:36476387 the sole NMN-consuming and NAD+-synthesizing enzyme dNmnat
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation from UniProtKB keyword KW-0547 (Nucleotide-binding). Nmnat binds ATP as a substrate for its adenylyltransferase reaction. This is a very broad parent term that is subsumed by the more specific GO:0005524 (ATP binding) and the specific catalytic activities already annotated. Reason: While very general, this IEA annotation is not wrong. It is subsumed by more specific annotations (ATP binding, nicotinamide-nucleotide adenylyltransferase activity) but acceptable as an IEA-level annotation from keyword mapping.
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation from InterPro/EC mapping. Consistent with the experimentally validated IDA annotations and the IBA annotation for the same term. Reason: Redundant with IBA and IDA annotations for the same term, but IEA annotations are expected to exist alongside higher-evidence annotations. The mapping is correct.
GO:0003824 catalytic activity	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation from InterPro domain IPR004821 (CTP_transf_like). This is a very broad parent term. The more specific catalytic activities (GO:0000309, GO:0004515) are already annotated with stronger evidence. Reason: Broad but not wrong. This InterPro-based IEA annotation is consistent with the known enzymatic function. More specific child terms are annotated at IDA level.
GO:0004515 nicotinate-nucleotide adenylyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation from InterPro/EC 2.7.7.18 mapping. Consistent with the IBA annotation and the ISS annotation for the same term. Reason: Redundant with IBA and ISS annotations for the same term. The mapping is correct.
GO:0005524 ATP binding	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation from UniProtKB keyword KW-0067 (ATP-binding). Nmnat uses ATP as a substrate in its adenylyltransferase reaction, so ATP binding is inherent to the enzymatic function. NMNAT also shares structural similarity with known chaperones and its chaperone function appears to involve the ATP-binding domain (PMID:18344983). Reason: ATP binding is an essential aspect of Nmnat's enzymatic mechanism and also relevant to its chaperone function. The IEA annotation is correct. Supporting Evidence: PMID:18344983 it shares significant structural similarity with known chaperones
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation from UniProt subcellular location mapping. Nuclear localization of Nmnat has been experimentally confirmed. Nmnat contains a C-terminal nuclear localization signal (KQKR at position 380-383; PMID:26616331). Isoform C is specifically nuclear-localized (PMID:26616331). Reason: Nuclear localization is experimentally validated by multiple studies including PMID:26616331 which characterized isoform-specific localization patterns. Supporting Evidence: file:DROME/Nmnat/Nmnat-deep-research-falcon.md Abundant in neuronal nuclei (brain and ventral nerve cord), persisting into adulthood.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation from UniProt subcellular location mapping. Cytoplasmic localization is experimentally confirmed by IDA (PMID:26616331). Nmnat localizes predominantly to the cytoplasm (PMID:19403820), and isoform D is specifically cytoplasmic (PMID:26616331). Reason: Cytoplasmic localization is confirmed by direct observation. Consistent with the IDA annotation from PMID:26616331.
GO:0009165 nucleotide biosynthetic process	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation from ARBA machine learning. NAD+ is a dinucleotide, so Nmnat's enzymatic activity directly contributes to nucleotide biosynthesis. This is a broad parent term that encompasses the more specific NAD+ biosynthetic process annotations. Reason: Broad but accurate. NAD+ is a dinucleotide and Nmnat catalyzes its synthesis. More specific terms (GO:0009435, GO:0034355) are annotated at higher evidence levels.
GO:0009435 NAD+ biosynthetic process	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation from InterPro/UniPathway mapping. NAD+ biosynthesis is the core biological process for Nmnat. The more specific child term GO:0034355 (NAD+ biosynthetic process via the salvage pathway) is annotated at IBA and IMP levels. Reason: This broader NAD+ biosynthesis term is correct and encompasses both de novo and salvage pathways. More specific annotations exist at higher evidence levels.
GO:0016740 transferase activity	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation from UniProtKB keyword KW-0808 (Transferase). Nmnat is indeed a nucleotidyltransferase. This is a very broad parent term subsumed by the specific adenylyltransferase activities already annotated. Reason: Very broad but correct. Subsumed by more specific child terms at higher evidence levels.
GO:0016779 nucleotidyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation from InterPro/keyword mapping. Nmnat is an adenylyltransferase, which is a type of nucleotidyltransferase. This is a parent term of the more specific GO:0070566 (adenylyltransferase activity) and the specific enzyme activities. Reason: Correct intermediate-level term. Consistent with the hierarchy of more specific annotations already present.
GO:0019363 pyridine nucleotide biosynthetic process	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation from UniProtKB keyword KW-0662 (Pyridine nucleotide biosynthesis). NAD+ is a pyridine nucleotide, so this annotation is accurate for the biosynthetic process Nmnat participates in. Reason: Correct. NAD+ is a pyridine nucleotide and Nmnat catalyzes a key step in its biosynthesis. Consistent with more specific annotations.
GO:0048786 presynaptic active zone	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation from UniProt subcellular location mapping. Presynaptic active zone localization is experimentally supported. The IMP annotation from PMID:30692130 shows that excess dNmnat disrupts active zone ultrastructure, confirming its presence at this location. Reason: Presynaptic localization is experimentally validated. Consistent with the IMP annotation for the same term from PMID:30692130. Supporting Evidence: PMID:30692130 excess dNmnat is necessary in highwire mutants and sufficient in wild-type larvae to reduce quantal content, likely via disruption of active zone ultrastructure file:DROME/Nmnat/Nmnat-deep-research-falcon.md Present as punctate labeling at synapses/terminals, partially colocalizing with the active zone marker nc82, including in photoreceptor terminals of the adult lamina.
GO:0070566 adenylyltransferase activity	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation from ARBA machine learning. Nmnat is an adenylyltransferase that transfers the adenylyl group from ATP to NMN or NaMN. This is a parent term of the more specific GO:0000309 and GO:0004515. Reason: Correct intermediate-level term. Consistent with the known enzymatic mechanism and more specific annotations at higher evidence levels.
GO:0004515 nicotinate-nucleotide adenylyltransferase activity	IDA PMID:36476387 The NAD(+) precursor NMN activates dSarm to trigger axon deg...	ACCEPT	Summary: IDA annotation from the Llobet Rosell et al. 2022 study. This paper demonstrates that dNmnat is the sole NMN-consuming and NAD+-synthesizing enzyme in Drosophila. The study uses enzymatic assays and genetic manipulation to show that lowering NMN levels via NMN-Deamidase expression preserves axons, while loss of dNmnat causes neurodegeneration. The IDA evidence for NaMN adenylyltransferase activity (EC 2.7.7.18) is consistent with the dual-substrate specificity of NMNAT enzymes. Reason: Direct assay evidence for the NaMN adenylyltransferase activity. The study clearly demonstrates that Nmnat is the sole NAD+-synthesizing enzyme in Drosophila. Supporting Evidence: PMID:36476387 loss of the sole NMN-consuming and NAD+-synthesizing enzyme dNmnat
GO:1990535 neuron projection maintenance	IMP PMID:21596138 Nmnat exerts neuroprotective effects in dendrites and axons.	ACCEPT	Summary: IMP annotation from Wen et al. 2011. This study demonstrated that Nmnat is required for the maintenance of both axonal and dendritic integrity in Drosophila. Loss of Nmnat caused dendritic branches to show increased retraction and decreased growth, leading to progressive coverage defects. Sensory axons showed severe degeneration upon complete loss. Reason: Well-supported by mutant phenotype analysis. Neuron projection maintenance is a genuine biological process that Nmnat participates in, through its chaperone-like neuroprotective function. This is a well-established function (possibly core given the strong separation-of-function evidence), distinct from but coexisting with the enzymatic NAD+-synthesis role. Falcon deep research corroborates that this neuroprotective/maintenance activity is genuine and partially uncoupled from NAD+ synthesis, so it is retained as a real function rather than an over-annotation. Supporting Evidence: PMID:21596138 essential role for endogenous Nmnat function in the maintenance of both axonal and dendritic integrity file:DROME/Nmnat/Nmnat-deep-research-falcon.md A central, well-cited observation in Drosophila is that dNmnat’s neuroprotective/maintenance function can be partially uncoupled from its NAD\(^+\)-synthesis activity. Catalytically impaired mutants that retain <1% enzymatic activity (e.g., WR) can still strongly rescue neurodegeneration phenotypes in vivo (e.g., photoreceptor maintenance)
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity	IDA PMID:36476387 The NAD(+) precursor NMN activates dSarm to trigger axon deg...	ACCEPT	Summary: IDA annotation from the Llobet Rosell et al. 2022 study. The paper demonstrates that dNmnat is the sole NMN-consuming NAD+ synthase in Drosophila. While the primary focus is on NMN accumulation driving axon degeneration via dSarm activation, the study confirms the NMN adenylyltransferase activity of dNmnat through genetic manipulation of NMN levels. Reason: Direct experimental evidence confirming the primary catalytic function. Consistent with multiple other IDA annotations for the same activity from earlier studies. Supporting Evidence: PMID:36476387 NMN-D delays neurodegeneration caused by loss of the sole NMN-consuming and NAD+-synthesizing enzyme dNmnat
GO:0034355 NAD+ biosynthetic process via the salvage pathway	IMP PMID:36476387 The NAD(+) precursor NMN activates dSarm to trigger axon deg...	ACCEPT	Summary: IMP annotation from Llobet Rosell et al. 2022. The study shows that dNmnat loss leads to neurodegeneration via NMN accumulation, and that expression of NMN-Deamidase (which converts NMN to NaMN, altering the metabolic flux) preserves axons. This demonstrates that dNmnat functions in the NAD+ salvage pathway by consuming NMN. Reason: Strong mutant phenotype evidence supporting the role in NAD+ salvage pathway biosynthesis. The study demonstrates the in vivo metabolic role of dNmnat. Supporting Evidence: PMID:36476387 NMN-D alters the NAD+ metabolic flux by lowering NMN, while NAD+ remains unchanged in vivo
GO:0004515 nicotinate-nucleotide adenylyltransferase activity	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation transferred from human NMNAT3 (UniProtKB:Q9HAN9) based on sequence similarity. The NaMN adenylyltransferase activity (EC 2.7.7.18) is a conserved function across the NMNAT family. This is consistent with the IBA and IDA annotations for the same term. Reason: Valid ISS transfer from a well-characterized ortholog. Consistent with the dual-substrate specificity known for the NMNAT family.
GO:0005739 mitochondrion	ISS GO_REF:0000024	UNDECIDED	Summary: ISS annotation transferred from human NMNAT3 (UniProtKB:Q96T66), which is known to localize to mitochondria. However, Drosophila has only a single Nmnat gene, unlike mammals which have three NMNAT isoenzymes with distinct subcellular localizations (NMNAT1: nuclear, NMNAT2: cytoplasmic/Golgi, NMNAT3: mitochondrial). The subcellular localization pattern of mammalian NMNAT3 may not directly transfer to the single Drosophila ortholog. Reason: The ISS transfer from human NMNAT3 is questionable because Drosophila has a single Nmnat that performs the functions of all three mammalian NMNAT isoenzymes. The experimentally determined localizations for Drosophila Nmnat include nucleus, cytoplasm, presynaptic active zone, and neuromuscular junction, but not specifically mitochondria. No direct experimental evidence for mitochondrial localization of dNmnat was found in the available publications.
GO:0031594 neuromuscular junction	IDA PMID:30692130 The E3 ligase Highwire promotes synaptic transmission by tar...	ACCEPT	Summary: IDA annotation from Russo et al. 2019. The study examines how the E3 ubiquitin ligase Highwire regulates dNmnat at the neuromuscular junction (NMJ). The study demonstrates that dNmnat is present at the NMJ and that its levels are regulated by Highwire-mediated ubiquitination. Excess dNmnat impairs evoked release by disrupting active zone ultrastructure. Reason: Direct observation of Nmnat at the neuromuscular junction. The study provides functional evidence for Nmnat's role at this location. Supporting Evidence: PMID:30692130 The ubiquitin ligase Highwire restrains synaptic growth and promotes evoked neurotransmission at NMJ synapses in Drosophila
GO:0048786 presynaptic active zone	IMP PMID:30692130 The E3 ligase Highwire promotes synaptic transmission by tar...	ACCEPT	Summary: IMP annotation from Russo et al. 2019. The study shows that excessive dNmnat impairs evoked release by disrupting active zone ultrastructure, providing functional evidence that Nmnat localizes to and affects the presynaptic active zone. This is consistent with the earlier observation of punctate presynaptic localization (PMID:17132048). Reason: Mutant phenotype evidence showing functional impact at the presynaptic active zone. Consistent with earlier direct localization data (PMID:17132048). Supporting Evidence: PMID:30692130 excess dNmnat is necessary in highwire mutants and sufficient in wild-type larvae to reduce quantal content, likely via disruption of active zone ultrastructure
GO:1900074 negative regulation of neuromuscular synaptic transmission	IDA PMID:30692130 The E3 ligase Highwire promotes synaptic transmission by tar...	KEEP AS NON CORE	Summary: IDA annotation from Russo et al. 2019. The study shows that excess dNmnat impairs evoked neurotransmitter release at the NMJ and that this requires catalytically active dNmnat. However, this effect appears to be a consequence of Nmnat overabundance when Highwire-mediated degradation is disrupted, rather than a normal physiological role. The negative regulation of synaptic transmission is an artifact of disrupted homeostatic regulation rather than a core function. Reason: While experimentally demonstrated, the negative regulation of neuromuscular synaptic transmission is a consequence of dNmnat overaccumulation when normal Highwire-mediated turnover is disrupted. This is not a core evolved function of Nmnat but rather reflects the need for tight regulation of its levels at the synapse. Supporting Evidence: PMID:30692130 Catalytically active dNmnat is required to drive defects in evoked release
GO:0005737 cytoplasm	IDA PMID:26616331 Alternative splicing of Drosophila Nmnat functions as a swit...	ACCEPT	Summary: IDA annotation from Ruan et al. 2015. The study demonstrates that isoform D is cytoplasmic and that the cytoplasmic localization is associated with the neuroprotective isoform. The K380R mutation in the nuclear localization signal shifts localization from nuclear to cytoplasmic. This study also confirmed earlier findings of cytoplasmic localization (PMID:19403820). Reason: Direct observation of cytoplasmic localization, specifically characterizing isoform-specific localization patterns. Core localization for the neuroprotective functions of Nmnat. Supporting Evidence: PMID:26616331 When expressed with a pan-neuronal driver nervana-GAL4, PC is highly enriched in the cell body, while cytPC and PD are predominantly cytoplasmic, consistent with the localization pattern in transfected cells.
GO:0043025 neuronal cell body	IDA PMID:26616331 Alternative splicing of Drosophila Nmnat functions as a swit...	ACCEPT	Summary: IDA annotation from Ruan et al. 2015. The study demonstrates neuronal localization of Nmnat and characterizes the alternative splicing that produces isoforms with distinct subcellular distributions in neurons. Earlier work (PMID:17132048) used the visual system of Drosophila as a model to study nmnat function in neurons. Reason: Direct observation of Nmnat in neuronal cell bodies. Consistent with the known expression pattern and functional role in neuroprotection. Supporting Evidence: PMID:17132048 we use the visual system of Drosophila as a model system to address these issues
GO:0051082 unfolded protein binding	IDA PMID:18344983 NAD synthase NMNAT acts as a chaperone to protect against ne...	MODIFY	Summary: IDA annotation from Zhai et al. 2008 (Nature). This landmark study demonstrated that NMNAT acts as a chaperone to protect against neurodegeneration. The study showed that NMNAT displays chaperone function in biochemical assays and cultured cells, shares structural similarity with known chaperones, is upregulated by proteotoxic stress, and is recruited with Hsp70 into protein aggregates. The chaperone function is independent of NAD+ synthesis activity (the H61A catalytic mutant retains chaperone activity). The follow-up study (PMID:26616331) further characterized the chaperone activity as holdase activity (preventing aggregation) rather than refoldase activity for isoform C, while isoform D shows both holdase and refoldase activity. GO:0051082 (unfolded protein binding) is now formally obsolete. The experimentally demonstrated activity is better described as misfolded protein binding (GO:0051787) since the studies show NMNAT preventing aggregation of misfolded proteins and being recruited to protein aggregates. Reason: GO:0051082 is now formally obsolete. The underlying experimental evidence is strong and well-characterized: Nmnat acts as a holdase chaperone that prevents toxic aggregation of misfolded proteins. The best replacement term is GO:0051787 (misfolded protein binding), which accurately captures NMNAT's demonstrated ability to bind to and prevent aggregation of misfolded/aggregation-prone proteins. The term GO:0140309 (unfolded protein carrier activity) is not appropriate because there is no evidence that NMNAT escorts proteins between cellular compartments. Note that the chaperone holdase activity is a secondary moonlighting function; the primary function is NAD+ synthesis. Proposed replacements: misfolded protein binding Supporting Evidence: PMID:18344983 NMNAT displays chaperone function both in biochemical assays and cultured cells, and it shares significant structural similarity with known chaperones PMID:18344983 it is upregulated in the brain upon overexpression of poly-glutamine expanded protein and recruited with the chaperone Hsp70 into protein aggregates file:DROME/Nmnat/Nmnat-deep-research-falcon.md dNmnat/NMNAT is described as binding misfolded species (e.g., Tau oligomers), promoting their ubiquitination/clearance, and that reduced endogenous NMNAT exacerbates Tau-induced degeneration, while NMNAT expression suppresses degeneration in Drosophila models.
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity	IDA PMID:19403820 Nicotinamide mononucleotide adenylyl transferase-mediated ax...	ACCEPT	Summary: IDA annotation from Sasaki et al. 2009. The study used Drosophila Nmnat among NMNAT enzymes from diverse species to demonstrate that enzymatic activity is important for axonal protection. The study showed that Nmnat enzymes with diverse sequences from various species all mediate robust axonal protection after axotomy, and that mutants with reduced enzymatic activity lacked axon protective activity. Reason: Direct assay evidence for the NMN adenylyltransferase activity. The study also demonstrated the importance of enzymatic activity for axonal protection, though steady-state NAD+ levels were not changed. Supporting Evidence: PMID:19403820 Nmnat1 enzymatic activity is important for axonal protection as mutants with reduced enzymatic activity lacked axon protective activity
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity	IDA PMID:17132048 Drosophila NMNAT maintains neural integrity independent of i...	ACCEPT	Summary: IDA annotation from the foundational Zhai et al. 2006 study. This study isolated the first nmnat mutations in a multicellular organism and demonstrated that Nmnat catalyzes the formation of NAD+ from NMN and ATP. The study showed that enzymatically inactive NMNAT (H61A mutant) retains strong neuroprotective effects, establishing the separation of enzymatic and neuroprotective functions. Reason: The foundational experimental demonstration of NMN adenylyltransferase activity in Drosophila Nmnat, using direct enzymatic assays and mutagenesis. Supporting Evidence: PMID:17132048 the NAD synthase NMNAT (nicotinamide mononucleotide adenylyltransferase 1) PMID:17132048 enzymatically inactive NMNAT protein retains strong neuroprotective effects
GO:0045494 photoreceptor cell maintenance	IMP PMID:17132048 Drosophila NMNAT maintains neural integrity independent of i...	KEEP AS NON CORE	Summary: IMP annotation from Zhai et al. 2006. The study used the Drosophila visual system as a model to demonstrate that loss of nmnat causes rapid and severe neurodegeneration in photoreceptor cells. The degeneration could be attenuated by blocking neuronal activity. Photoreceptor maintenance was rescued by enzymatically inactive NMNAT, indicating the neuroprotective function is NAD-independent. Reason: While experimentally well-supported, photoreceptor cell maintenance is a tissue-specific manifestation of the broader neuroprotective function of Nmnat. The core function is neuronal maintenance in general, and photoreceptor cells are one of many cell types where this is observed. This is a non-core annotation reflecting the specific experimental model used rather than a unique photoreceptor-specific function. Supporting Evidence: PMID:17132048 Loss of nmnat causes a rapid and severe neurodegeneration that can be attenuated by blocking neuronal activity file:DROME/Nmnat/Nmnat-deep-research-falcon.md Loss-of-function of nmnat causes rapid, progressive neurodegeneration in the visual system, including defective ERGs and ultrastructural synaptic abnormalities

Gene Description

Existing Annotations Review

Core Functions

Nmnat catalyzes the synthesis of NAD+ from nicotinamide mononucleotide (NMN) and ATP (EC 2.7.7.1, GO:0000309). This is the primary evolved enzymatic function. Nmnat is the sole NAD+-synthesizing enzyme in Drosophila, and this activity is essential for viability.

Nmnat also catalyzes the synthesis of deamido-NAD+ from nicotinate ribonucleotide and ATP (EC 2.7.7.18, GO:0004515), reflecting the dual-substrate specificity conserved across the NMNAT enzyme family.

References

Deep Research

Falcon

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