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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1

Gene

NMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD+ (NaAD). Key enzyme in both de novo and salvage pathways for NAD+ biosynthesis. Predominantly acts in the salvage pathways via NMN.4 Publications

Miscellaneous

Present with 5130 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.3 Publications
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.1 Publication

Cofactori

Ni2+1 PublicationNote: Divalent metal cation.1 Publication

Kineticsi

  1. KM=0.11 mM for ATP2 Publications
  2. KM=0.19 mM for NMN2 Publications
  3. KM=5 mM for NaMN1 Publication
  4. KM=0.073 mM for NAD+1 Publication
  5. KM=0.083 mM for diphosphate1 Publication

    pH dependencei

    Optimum pH is 7.2-8.4.2 Publications

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMA1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMA2)
    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.

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.2 Publications
    Proteins known to be involved in this subpathway in this organism are:
    1. Nicotinamide mononucleotide adenylyltransferase (POF1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMA1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMA2)
    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei181ATPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi172 – 174ATPBy similarity3
    Nucleotide bindingi288 – 290ATPBy similarity3
    Nucleotide bindingi356 – 359ATPBy similarity4

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionNucleotidyltransferase, Transferase
    Biological processPyridine nucleotide biosynthesis
    LigandATP-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:YLR328W-MONOMER
    YEAST:YLR328W-MONOMER
    ReactomeiR-SCE-196807 Nicotinate metabolism
    UniPathwayiUPA00253; UER00332
    UPA00253; UER00600

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Curated (EC:2.7.7.12 Publications, EC:2.7.7.181 Publication)
    Short name:
    NMN/NaMN adenylyltransferase 1
    Alternative name(s):
    NAD(+) diphosphorylase 11 Publication
    NAD(+) pyrophosphorylase 11 Publication
    Nicotinamide-nucleotide adenylyltransferase 11 Publication
    Short name:
    NMN adenylyltransferase 1
    Short name:
    NMNAT 1
    Nicotinate-nucleotide adenylyltransferase 11 Publication
    Short name:
    NaMN adenylyltransferase 1
    Short name:
    NaMNAT 1
    Gene namesi
    Name:NMA11 Publication
    Ordered Locus Names:YLR328WImported
    ORF Names:L8543.16
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XII

    Organism-specific databases

    EuPathDBiFungiDB:YLR328W
    SGDiS000004320 NMA1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001350181 – 401Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Add BLAST401

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei91PhosphoserineCombined sources1
    Modified residuei95PhosphoserineCombined sources1
    Modified residuei96PhosphoserineCombined sources1
    Modified residuei111PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ06178
    PaxDbiQ06178
    PRIDEiQ06178

    PTM databases

    iPTMnetiQ06178

    Expressioni

    Inductioni

    Expression is high in early log-phase and significantly drops as cells enter late log phase.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi31592, 40 interactors
    DIPiDIP-1228N
    IntActiQ06178, 13 interactors
    MINTiQ06178
    STRINGi4932.YLR328W

    Structurei

    3D structure databases

    ProteinModelPortaliQ06178
    SMRiQ06178
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni212 – 214Substrate bindingBy similarity3
    Regioni250 – 253Substrate bindingBy similarity4
    Regioni300 – 301Substrate bindingBy similarity2

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi61 – 67Poly-His7

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00530000063189
    HOGENOMiHOG000216047
    InParanoidiQ06178
    KOiK06210
    OMAiCLILERT
    OrthoDBiEOG092C3YJ3

    Family and domain databases

    Gene3Di3.40.50.620, 1 hit
    InterProiView protein in InterPro
    IPR004821 Cyt_trans-like
    IPR005248 NadD/NMNAT
    IPR014729 Rossmann-like_a/b/a_fold
    PfamiView protein in Pfam
    PF01467 CTP_transf_like, 1 hit
    TIGRFAMsiTIGR00482 TIGR00482, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q06178-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDPTRAPDFK PPSADEELIP PPDPESKIPK SIPIIPYVLA DANSSIDAPF
    60 70 80 90 100
    NIKRKKKHPK HHHHHHHSRK EGNDKKHQHI PLNQDDFQPL SAEVSSEDDD
    110 120 130 140 150
    ADFRSKERYG SDSTTESETR GVQKYQIADL EEVPHGIVRQ ARTLEDYEFP
    160 170 180 190 200
    SHRLSKKLLD PNKLPLVIVA CGSFSPITYL HLRMFEMALD AISEQTRFEV
    210 220 230 240 250
    IGGYYSPVSD NYQKQGLAPS YHRVRMCELA CERTSSWLMV DAWESLQPSY
    260 270 280 290 300
    TRTAKVLDHF NHEINIKRGG VATVTGEKIG VKIMLLAGGD LIESMGEPNV
    310 320 330 340 350
    WADADLHHIL GNYGCLIVER TGSDVRSFLL SHDIMYEHRR NILIIKQLIY
    360 370 380 390 400
    NDISSTKVRL FIRRAMSVQY LLPNSVIRYI QEHRLYVDQT EPVKQVLGNK

    E
    Length:401
    Mass (Da):45,859
    Last modified:November 1, 1996 - v1
    Checksum:iA176964E56A30DD8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U20618 Genomic DNA Translation: AAB64524.1
    BK006945 Genomic DNA Translation: DAA09636.1
    PIRiS53405
    RefSeqiNP_013432.1, NM_001182217.1

    Genome annotation databases

    EnsemblFungiiYLR328W; YLR328W; YLR328W
    GeneIDi851039
    KEGGisce:YLR328W

    Similar proteinsi

    Entry informationi

    Entry nameiNMA1_YEAST
    AccessioniPrimary (citable) accession number: Q06178
    Secondary accession number(s): D6VYX0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: March 28, 2018
    This is version 161 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health