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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1

Gene

Nmnat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP (PubMed:15381699). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency (By similarity). Can use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+ (By similarity). For the pyrophosphorolytic activity, prefers NAD+ and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively (By similarity). Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NaADP+ (By similarity). Protects against axonal degeneration following mechanical or toxic insults (PubMed:15310905, PubMed:16914673). Delays axonal degeneration after axotomy. Results in a >10-fold increase in intact neurites 72 hours after injury (PubMed:16914673).By similarity3 Publications

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.By similarity
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Cofactori

Zn2+By similarity, Mg2+By similarityNote: Divalent metal cations. Zn2+ confers higher activity as compared to Mg2+.By similarity

Enzyme regulationi

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).By similarity

Kineticsi

  1. KM=20.1 µM for nicotinamide mononucleotide (NMN)1 Publication
  1. Vmax=34.1 µmol/min/mg enzyme1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), Nicotinamide-nucleotide adenylyltransferase (Nmnat2), Nicotinamide-nucleotide adenylyltransferase (Nmnat2), Nicotinamide-nucleotide adenylyltransferase (Nmnat1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (Nmnat3), Nicotinamide-nucleotide adenylyltransferase
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (Nmnat2), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (Nmnat1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (Nmnat3)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei24ATPBy similarity1
Binding sitei58ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 17ATPBy similarity3
Nucleotide bindingi157 – 159ATPBy similarity3
Nucleotide bindingi225 – 228ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

  • 'de novo' NAD biosynthetic process from aspartate Source: GO_Central
  • ATP generation from poly-ADP-D-ribose Source: UniProtKB
  • NAD biosynthetic process Source: MGI
  • response to wounding Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.1. 3474.
ReactomeiR-MMU-196807. Nicotinate metabolism.
SABIO-RKQ9EPA7.
UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 1
Alternative name(s):
Nicotinamide mononucleotide adenylyltransferase 1
Short name:
NMN adenylyltransferase 1
Nicotinate-nucleotide adenylyltransferase 1
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:Nmnat1
Synonyms:D4Cole1e, Nmnat
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913704. Nmnat1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125 – 128RKRK → AAAA: Locates to the cytoplasm. Has no affect on enzyme activity or axonal protection. 1 Publication4
Mutagenesisi170W → A: Decrease in enzyme activity. Has no axonal protective effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001350131 – 285Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Add BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei117PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EPA7.
MaxQBiQ9EPA7.
PaxDbiQ9EPA7.
PRIDEiQ9EPA7.

PTM databases

iPTMnetiQ9EPA7.
PhosphoSitePlusiQ9EPA7.

Expressioni

Developmental stagei

Expressed throughout development and in adulthood.1 Publication

Inductioni

By neuronal injury.

Gene expression databases

BgeeiENSMUSG00000028992.
CleanExiMM_NMNAT1.
ExpressionAtlasiQ9EPA7. baseline and differential.
GenevisibleiQ9EPA7. MM.

Interactioni

Subunit structurei

Homohexamer. Interacts with ADPRT/PARP1.By similarity

Protein-protein interaction databases

IntActiQ9EPA7. 1 interactor.
STRINGi10090.ENSMUSP00000030845.

Structurei

3D structure databases

ProteinModelPortaliQ9EPA7.
SMRiQ9EPA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni55 – 57Substrate bindingBy similarity3
Regioni92 – 95Substrate bindingBy similarity4
Regioni169 – 170Substrate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi123 – 129Nuclear localization signalSequence analysis7

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9EPA7.
KOiK06210.
OMAiRVAMCQL.
OrthoDBiEOG091G0JTI.
PhylomeDBiQ9EPA7.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EPA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSSKKTEVV LLACGSFNPI TNMHLRLFEL AKDYMHATGK YSVIKGIISP
60 70 80 90 100
VGDAYKKKGL IPAHHRIIMA ELATKNSHWV EVDTWESLQK EWVETVKVLR
110 120 130 140 150
YHQEKLATGS CSYPQSSPAL EKPGRKRKWA DQKQDSSPQK PQEPKPTGVP
160 170 180 190 200
KVKLLCGADL LESFSVPNLW KMEDITQIVA NFGLICITRA GSDAQKFIYE
210 220 230 240 250
SDVLWRHQSN IHLVNEWITN DISSTKIRRA LRRGQSIRYL VPDLVQEYIE
260 270 280
KHELYNTESE GRNAGVTLAP LQRNAAEAKH NHSTL
Length:285
Mass (Da):32,355
Last modified:May 9, 2003 - v2
Checksum:i2769D42E894EB84F
GO

Sequence cautioni

The sequence AAG17285 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAG17286 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAG38490 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260924 mRNA. Translation: AAG17285.1. Different initiation.
AF260925 mRNA. Translation: AAG17286.1. Different initiation.
AF260927 Genomic DNA. Translation: AAG38490.1. Different initiation.
AY679721 mRNA. Translation: AAT76443.1.
CCDSiCCDS18960.1.
RefSeqiNP_597679.1. NM_133435.1.
XP_006539168.1. XM_006539105.3.
UniGeneiMm.76062.

Genome annotation databases

EnsembliENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992.
ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992.
GeneIDi66454.
KEGGimmu:66454.
UCSCiuc008vwj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260924 mRNA. Translation: AAG17285.1. Different initiation.
AF260925 mRNA. Translation: AAG17286.1. Different initiation.
AF260927 Genomic DNA. Translation: AAG38490.1. Different initiation.
AY679721 mRNA. Translation: AAT76443.1.
CCDSiCCDS18960.1.
RefSeqiNP_597679.1. NM_133435.1.
XP_006539168.1. XM_006539105.3.
UniGeneiMm.76062.

3D structure databases

ProteinModelPortaliQ9EPA7.
SMRiQ9EPA7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EPA7. 1 interactor.
STRINGi10090.ENSMUSP00000030845.

PTM databases

iPTMnetiQ9EPA7.
PhosphoSitePlusiQ9EPA7.

Proteomic databases

EPDiQ9EPA7.
MaxQBiQ9EPA7.
PaxDbiQ9EPA7.
PRIDEiQ9EPA7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030845; ENSMUSP00000030845; ENSMUSG00000028992.
ENSMUST00000105693; ENSMUSP00000101318; ENSMUSG00000028992.
GeneIDi66454.
KEGGimmu:66454.
UCSCiuc008vwj.1. mouse.

Organism-specific databases

CTDi64802.
MGIiMGI:1913704. Nmnat1.

Phylogenomic databases

eggNOGiKOG3199. Eukaryota.
COG1057. LUCA.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9EPA7.
KOiK06210.
OMAiRVAMCQL.
OrthoDBiEOG091G0JTI.
PhylomeDBiQ9EPA7.
TreeFamiTF315035.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.
BRENDAi2.7.7.1. 3474.
ReactomeiR-MMU-196807. Nicotinate metabolism.
SABIO-RKQ9EPA7.

Miscellaneous databases

PROiQ9EPA7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028992.
CleanExiMM_NMNAT1.
ExpressionAtlasiQ9EPA7. baseline and differential.
GenevisibleiQ9EPA7. MM.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNMNA1_MOUSE
AccessioniPrimary (citable) accession number: Q9EPA7
Secondary accession number(s): Q6B504
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 9, 2003
Last modified: November 2, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In strain C57BL/Ola, an 85 kb region on chromosome 4 containing Nmnat1 and Ube4b is triplicated. The N-terminal 70 residues of Ube4b becomes linked to the complete Nmnat1 protein and encodes a fusion protein located in the nucleus which is responsible for the Wallerian degeneration slow (Wlds) phenotype characterized by delayed Wallerian degeneration of injured axons.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.