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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: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei175 – 1751ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi166 – 1683ATPBy similarity
    Nucleotide bindingi282 – 2843ATPBy similarity
    Nucleotide bindingi350 – 3534ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • NAD biosynthetic process Source: SGD
    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: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

    GO - Cellular componenti

    • nucleus Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2PRO_0000135019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei85 – 851PhosphoserineCombined sources
    Modified residuei89 – 891PhosphoserineCombined sources
    Modified residuei90 – 901PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53204.

    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. 18 interactions.
    DIPiDIP-1227N.
    IntActiP53204. 3 interactions.
    MINTiMINT-403491.

    Structurei

    3D structure databases

    ProteinModelPortaliP53204.
    SMRiP53204. Positions 157-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 2083Substrate bindingBy similarity
    Regioni244 – 2474Substrate bindingBy similarity
    Regioni294 – 2952Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00530000063189.
    HOGENOMiHOG000216047.
    InParanoidiP53204.
    KOiK06210.
    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.

    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.

    Cross-referencesi

    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.

    3D structure databases

    ProteinModelPortaliP53204.
    SMRiP53204. Positions 157-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33254. 18 interactions.
    DIPiDIP-1227N.
    IntActiP53204. 3 interactions.
    MINTiMINT-403491.

    PTM databases

    iPTMnetiP53204.

    Proteomic databases

    MaxQBiP53204.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR010W; YGR010W; YGR010W.
    GeneIDi852893.
    KEGGisce:YGR010W.

    Organism-specific databases

    EuPathDBiFungiDB:YGR010W.
    SGDiS000003242. NMA2.

    Phylogenomic databases

    GeneTreeiENSGT00530000063189.
    HOGENOMiHOG000216047.
    InParanoidiP53204.
    KOiK06210.
    OrthoDBiEOG75QRFD.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00332.
    UPA00253; UER00600.
    BioCyciMetaCyc:YGR010W-MONOMER.
    YEAST:YGR010W-MONOMER.
    BRENDAi2.7.7.1. 984.
    2.7.7.18. 984.
    ReactomeiR-SCE-196807. Nicotinate metabolism.

    Miscellaneous databases

    NextBioi972562.
    PROiP53204.

    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 VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(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 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: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "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, SUBCELLULAR LOCATION.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "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-85; SER-89 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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 nameiNMA2_YEAST
    AccessioniPrimary (citable) accession number: P53204
    Secondary accession number(s): D6VUE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: May 11, 2016
    This is version 127 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 1430 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: 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.