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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2

Gene

NMA2

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 (PubMed:12597897). 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 (By similarity). Predominantly acts in the salvage pathways via NMN (PubMed:11884393).By similarity2 Publications

Miscellaneous

Present with 1430 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.By similarity1 Publication
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.1 Publication

Cofactori

Co2+1 PublicationNote: Divalent metal cation.1 Publication

Kineticsi

  1. KM=1.4 mM for ATP1 Publication
  2. KM=0.13 mM for NMN1 Publication
  3. KM=0.023 mM for NAD+1 Publication
  4. KM=5 mM for diphosphate1 Publication

    pH dependencei

    Optimum pH is 6.5-8.0.1 Publication

    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.1 Publication
    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 sitei175ATPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi166 – 168ATPBy similarity3
    Nucleotide bindingi282 – 284ATPBy similarity3
    Nucleotide bindingi350 – 353ATPBy 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:YGR010W-MONOMER
    YEAST:YGR010W-MONOMER
    BRENDAi2.7.7.1 984
    2.7.7.18 984
    ReactomeiR-SCE-196807 Nicotinate metabolism
    UniPathwayiUPA00253; UER00332
    UPA00253; UER00600

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2Curated (EC:2.7.7.11 Publication, EC:2.7.7.181 Publication)
    Short name:
    NMN/NaMN adenylyltransferase 2
    Alternative name(s):
    NAD(+) diphosphorylase 2
    NAD(+) pyrophosphorylase 2
    Nicotinamide-nucleotide adenylyltransferase 21 Publication
    Short name:
    NMN adenylyltransferase 2
    Short name:
    NMNAT 2
    Nicotinate-nucleotide adenylyltransferase 21 Publication
    Short name:
    NaMN adenylyltransferase 2
    Short name:
    NaMNAT 2
    Gene namesi
    Name:NMA21 Publication
    Ordered Locus Names:YGR010WImported
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VII

    Organism-specific databases

    EuPathDBiFungiDB:YGR010W
    SGDiS000003242 NMA2

    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

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001350191 – 395Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2Add BLAST395

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei85PhosphoserineCombined sources1
    Modified residuei89PhosphoserineCombined sources1
    Modified residuei90PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53204
    PaxDbiP53204
    PRIDEiP53204

    PTM databases

    iPTMnetiP53204

    Expressioni

    Inductioni

    Expression is slightly induced in late log phase.1 Publication

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NMA1Q061786EBI-23073,EBI-11803

    Protein-protein interaction databases

    BioGridi33254, 46 interactors
    DIPiDIP-1227N
    IntActiP53204, 3 interactors
    MINTiP53204
    STRINGi4932.YGR010W

    Structurei

    3D structure databases

    ProteinModelPortaliP53204
    SMRiP53204
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni206 – 208Substrate bindingBy similarity3
    Regioni244 – 247Substrate bindingBy similarity4
    Regioni294 – 295Substrate bindingBy similarity2

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00530000063189
    HOGENOMiHOG000216047
    InParanoidiP53204
    KOiK06210
    OMAiYKKQGLA
    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.

    P53204-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDPTKAPDFK PPQPNEELQP PPDPTHTIPK SGPIVPYVLA DYNSSIDAPF
    60 70 80 90 100
    NLDIYKTLSS RKKNANSSNR MDHIPLNTSD FQPLSRDVSS EEESEGQSNG
    110 120 130 140 150
    IDATLQDVTM TGNLGVLKSQ IADLEEVPHT IVRQARTIED YEFPVHRLTK
    160 170 180 190 200
    KLQDPEKLPL IIVACGSFSP ITYLHLRMFE MALDDINEQT RFEVVGGYFS
    210 220 230 240 250
    PVSDNYQKRG LAPAYHRVRM CELACERTSS WLMVDAWESL QSSYTRTAKV
    260 270 280 290 300
    LDHFNHEINI KRGGIMTVDG EKMGVKIMLL AGGDLIESMG EPHVWADSDL
    310 320 330 340 350
    HHILGNYGCL IVERTGSDVR SFLLSHDIMY EHRRNILIIK QLIYNDISST
    360 370 380 390
    KVRLFIRRGM SVQYLLPNSV IRYIQEYNLY INQSEPVKQV LDSKE
    Length:395
    Mass (Da):44,909
    Last modified:October 1, 1996 - v1
    Checksum:i4A358AF7885B6568
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z72795 Genomic DNA Translation: CAA96993.1
    BK006941 Genomic DNA Translation: DAA08108.1
    PIRiS64299
    RefSeqiNP_011524.1, NM_001181139.1

    Genome annotation databases

    EnsemblFungiiYGR010W; YGR010W; YGR010W
    GeneIDi852893
    KEGGisce:YGR010W

    Similar proteinsi

    Entry informationi

    Entry nameiNMA2_YEAST
    AccessioniPrimary (citable) accession number: P53204
    Secondary accession number(s): D6VUE7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: March 28, 2018
    This is version 142 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