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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: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi172 – 1743ATPBy similarity
    Nucleotide bindingi288 – 2903ATPBy similarity
    Nucleotide bindingi356 – 3594ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    ATP-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

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1PRO_0000135018Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei91 – 911PhosphoserineCombined sources
    Modified residuei95 – 951PhosphoserineCombined sources
    Modified residuei96 – 961PhosphoserineCombined sources
    Modified residuei111 – 1111PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ06178.

    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

    WithEntry#Exp.IntActNotes
    itself4EBI-11803,EBI-11803
    NMA2P532046EBI-11803,EBI-23073

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi31592. 28 interactions.
    DIPiDIP-1228N.
    IntActiQ06178. 8 interactions.
    MINTiMINT-403505.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06178.
    SMRiQ06178. Positions 163-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni212 – 2143Substrate bindingBy similarity
    Regioni250 – 2534Substrate bindingBy similarity
    Regioni300 – 3012Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi61 – 677Poly-His

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00530000063189.
    HOGENOMiHOG000216047.
    InParanoidiQ06178.
    KOiK06210.
    OMAiPIIPYVL.
    OrthoDBiEOG75QRFD.

    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.

    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.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliQ06178.
    SMRiQ06178. Positions 163-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31592. 28 interactions.
    DIPiDIP-1228N.
    IntActiQ06178. 8 interactions.
    MINTiMINT-403505.

    PTM databases

    iPTMnetiQ06178.

    Proteomic databases

    MaxQBiQ06178.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR328W; YLR328W; YLR328W.
    GeneIDi851039.
    KEGGisce:YLR328W.

    Organism-specific databases

    EuPathDBiFungiDB:YLR328W.
    SGDiS000004320. NMA1.

    Phylogenomic databases

    GeneTreeiENSGT00530000063189.
    HOGENOMiHOG000216047.
    InParanoidiQ06178.
    KOiK06210.
    OMAiPIIPYVL.
    OrthoDBiEOG75QRFD.

    Enzyme and pathway databases

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

    Miscellaneous databases

    PROiQ06178.

    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Identification and characterization of YLR328W, the Saccharomyces cerevisiae structural gene encoding NMN adenylyltransferase. Expression and characterization of the recombinant enzyme."
      Emanuelli M., Carnevali F., Lorenzi M., Raffaelli N., Amici A., Ruggieri S., Magni G.
      FEBS Lett. 455:13-17(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-22; 129-139 AND 256-265, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
    4. "The participation of inorganic pyrophosphate in the reversible enzymatic synthesis of diphosphopyridine nucleotide."
      Kornberg A.
      J. Biol. Chem. 176:1475-1476(1948) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    5. "The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast."
      Dahmen W., Webb B., Preiss J.
      Arch. Biochem. Biophys. 120:440-450(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    6. "Nicotinamide mononucleotide adenylyltransferase. Molecular and enzymatic properties of the homogeneous enzyme from baker's yeast."
      Natalini P., Ruggieri S., Raffaelli N., Magni G.
      Biochemistry 25:3725-3729(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    7. "Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels."
      Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Cohen H., Lin S.S., Manchester J.K., Gordon J.I., Sinclair D.A.
      J. Biol. Chem. 277:18881-18890(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Identification and characterization of a second NMN adenylyltransferase gene in Saccharomyces cerevisiae."
      Emanuelli M., Amici A., Carnevali F., Pierella F., Raffaelli N., Magni G.
      Protein Expr. Purif. 27:357-364(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95; SER-96 AND SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "YCL047C/POF1 is a novel nicotinamide mononucleotide adenylyltransferase (NMNAT) in Saccharomyces cerevisiae."
      Kato M., Lin S.J.
      J. Biol. Chem. 289:15577-15587(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: ATCC 201389 / BY4742.

    Entry informationi

    Entry nameiNMA1_YEAST
    AccessioniPrimary (citable) accession number: Q06178
    Secondary accession number(s): D6VYX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 148 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    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.