NMA1_YEAST
ID NMA1_YEAST Reviewed; 401 AA.
AC Q06178; D6VYX0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
DE Short=NMN/NaMN adenylyltransferase 1;
DE EC=2.7.7.1 {ECO:0000269|PubMed:10428462, ECO:0000269|PubMed:4291828};
DE EC=2.7.7.18 {ECO:0000305|PubMed:11884393};
DE AltName: Full=NAD(+) diphosphorylase 1 {ECO:0000303|PubMed:4291828};
DE AltName: Full=NAD(+) pyrophosphorylase 1 {ECO:0000303|PubMed:4291828};
DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase 1 {ECO:0000303|PubMed:3013296};
DE Short=NMN adenylyltransferase 1;
DE Short=NMNAT 1;
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 1 {ECO:0000303|PubMed:11884393};
DE Short=NaMN adenylyltransferase 1;
DE Short=NaMNAT 1;
GN Name=NMA1 {ECO:0000303|PubMed:11884393};
GN OrderedLocusNames=YLR328W {ECO:0000312|SGD:S000004320}; ORFNames=L8543.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 1-22; 129-139 AND 256-265, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=10428462; DOI=10.1016/s0014-5793(99)00852-2;
RA Emanuelli M., Carnevali F., Lorenzi M., Raffaelli N., Amici A.,
RA Ruggieri S., Magni G.;
RT "Identification and characterization of YLR328W, the Saccharomyces
RT cerevisiae structural gene encoding NMN adenylyltransferase. Expression and
RT characterization of the recombinant enzyme.";
RL FEBS Lett. 455:13-17(1999).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=18098602;
RA Kornberg A.;
RT "The participation of inorganic pyrophosphate in the reversible enzymatic
RT synthesis of diphosphopyridine nucleotide.";
RL J. Biol. Chem. 176:1475-1476(1948).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4291828; DOI=10.1016/0003-9861(67)90262-7;
RA Dahmen W., Webb B., Preiss J.;
RT "The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide
RT pyrophosphorylases of Escherichia coli and yeast.";
RL Arch. Biochem. Biophys. 120:440-450(1967).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=3013296; DOI=10.1021/bi00360a037;
RA Natalini P., Ruggieri S., Raffaelli N., Magni G.;
RT "Nicotinamide mononucleotide adenylyltransferase. Molecular and enzymatic
RT properties of the homogeneous enzyme from baker's yeast.";
RL Biochemistry 25:3725-3729(1986).
RN [7]
RP FUNCTION.
RX PubMed=11884393; DOI=10.1074/jbc.m111773200;
RA Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Cohen H., Lin S.S.,
RA Manchester J.K., Gordon J.I., Sinclair D.A.;
RT "Manipulation of a nuclear NAD+ salvage pathway delays aging without
RT altering steady-state NAD+ levels.";
RL J. Biol. Chem. 277:18881-18890(2002).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12597897; DOI=10.1016/s1046-5928(02)00645-9;
RA Emanuelli M., Amici A., Carnevali F., Pierella F., Raffaelli N., Magni G.;
RT "Identification and characterization of a second NMN adenylyltransferase
RT gene in Saccharomyces cerevisiae.";
RL Protein Expr. Purif. 27:357-364(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95 AND SER-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95; SER-96 AND
RP SER-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP INDUCTION.
RC STRAIN=ATCC 201389 / BY4742;
RX PubMed=24759102; DOI=10.1074/jbc.m114.558643;
RA Kato M., Lin S.J.;
RT "YCL047C/POF1 is a novel nicotinamide mononucleotide adenylyltransferase
RT (NMNAT) in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 289:15577-15587(2014).
CC -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
CC mononucleotide (NMN) and ATP. Can also use the deamidated form;
CC nicotinic acid mononucleotide (NaMN) as substrate to form deamido-
CC NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for
CC NAD(+) biosynthesis. Predominantly acts in the salvage pathways via
CC NMN. {ECO:0000269|PubMed:10428462, ECO:0000269|PubMed:11884393,
CC ECO:0000269|PubMed:3013296, ECO:0000269|PubMed:4291828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC Evidence={ECO:0000269|PubMed:10428462, ECO:0000269|PubMed:18098602,
CC ECO:0000269|PubMed:3013296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58437; EC=2.7.7.18;
CC Evidence={ECO:0000305|PubMed:11884393};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10428462};
CC Note=Divalent metal cation. {ECO:0000269|PubMed:10428462};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for ATP {ECO:0000269|PubMed:12597897,
CC ECO:0000269|PubMed:3013296};
CC KM=0.19 mM for NMN {ECO:0000269|PubMed:12597897,
CC ECO:0000269|PubMed:3013296};
CC KM=5 mM for NaMN {ECO:0000269|PubMed:3013296};
CC KM=0.073 mM for NAD(+) {ECO:0000269|PubMed:12597897};
CC KM=0.083 mM for diphosphate {ECO:0000269|PubMed:12597897};
CC pH dependence:
CC Optimum pH is 7.2-8.4. {ECO:0000269|PubMed:12597897,
CC ECO:0000269|PubMed:3013296};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000305|PubMed:11884393}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000305|PubMed:3013296,
CC ECO:0000305|PubMed:4291828}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10428462,
CC ECO:0000269|PubMed:3013296}.
CC -!- INTERACTION:
CC Q06178; Q06178: NMA1; NbExp=4; IntAct=EBI-11803, EBI-11803;
CC Q06178; P53204: NMA2; NbExp=6; IntAct=EBI-11803, EBI-23073;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is high in early log-phase and significantly
CC drops as cells enter late log phase. {ECO:0000269|PubMed:24759102}.
CC -!- MISCELLANEOUS: Present with 5130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U20618; AAB64524.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09636.1; -; Genomic_DNA.
DR PIR; S53405; S53405.
DR RefSeq; NP_013432.1; NM_001182217.1.
DR AlphaFoldDB; Q06178; -.
DR SMR; Q06178; -.
DR BioGRID; 31592; 45.
DR DIP; DIP-1228N; -.
DR IntAct; Q06178; 9.
DR MINT; Q06178; -.
DR STRING; 4932.YLR328W; -.
DR iPTMnet; Q06178; -.
DR MaxQB; Q06178; -.
DR PaxDb; Q06178; -.
DR PRIDE; Q06178; -.
DR EnsemblFungi; YLR328W_mRNA; YLR328W; YLR328W.
DR GeneID; 851039; -.
DR KEGG; sce:YLR328W; -.
DR SGD; S000004320; NMA1.
DR VEuPathDB; FungiDB:YLR328W; -.
DR eggNOG; KOG3199; Eukaryota.
DR GeneTree; ENSGT00950000183179; -.
DR HOGENOM; CLU_033366_5_0_1; -.
DR InParanoid; Q06178; -.
DR OMA; VPHGIQR; -.
DR BioCyc; MetaCyc:YLR328W-MON; -.
DR BioCyc; YEAST:YLR328W-MON; -.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR PRO; PR:Q06178; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06178; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:SGD.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
DR CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; NAD; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase 1"
FT /id="PRO_0000135018"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66,
FT ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 212..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 288..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 300..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 356..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 401 AA; 45859 MW; A176964E56A30DD8 CRC64;
MDPTRAPDFK PPSADEELIP PPDPESKIPK SIPIIPYVLA DANSSIDAPF NIKRKKKHPK
HHHHHHHSRK EGNDKKHQHI PLNQDDFQPL SAEVSSEDDD ADFRSKERYG SDSTTESETR
GVQKYQIADL EEVPHGIVRQ ARTLEDYEFP SHRLSKKLLD PNKLPLVIVA CGSFSPITYL
HLRMFEMALD AISEQTRFEV IGGYYSPVSD NYQKQGLAPS YHRVRMCELA CERTSSWLMV
DAWESLQPSY TRTAKVLDHF NHEINIKRGG VATVTGEKIG VKIMLLAGGD LIESMGEPNV
WADADLHHIL GNYGCLIVER TGSDVRSFLL SHDIMYEHRR NILIIKQLIY NDISSTKVRL
FIRRAMSVQY LLPNSVIRYI QEHRLYVDQT EPVKQVLGNK E
