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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (NAD( ) diphosphorylase 1) (NAD( ) pyrophosphorylase 1) (Nicotinamide-nucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (NMNAT 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1) (NaMNAT 1)

 NMA1_YEAST              Reviewed;         401 AA.
Q06178; D6VYX0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 164.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 1;
EC=2.7.7.1 {ECO:0000269|PubMed:10428462, ECO:0000269|PubMed:4291828};
EC=2.7.7.18 {ECO:0000305|PubMed:11884393};
AltName: Full=NAD(+) diphosphorylase 1 {ECO:0000303|PubMed:4291828};
AltName: Full=NAD(+) pyrophosphorylase 1 {ECO:0000303|PubMed:4291828};
AltName: Full=Nicotinamide-nucleotide adenylyltransferase 1 {ECO:0000303|PubMed:3013296};
Short=NMN adenylyltransferase 1;
Short=NMNAT 1;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 1 {ECO:0000303|PubMed:11884393};
Short=NaMN adenylyltransferase 1;
Short=NaMNAT 1;
Name=NMA1 {ECO:0000303|PubMed:11884393};
OrderedLocusNames=YLR328W {ECO:0000312|SGD:S000004320};
ORFNames=L8543.16;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 1-22; 129-139 AND 256-265, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, AND SUBUNIT.
PubMed=10428462; DOI=10.1016/S0014-5793(99)00852-2;
Emanuelli M., Carnevali F., Lorenzi M., Raffaelli N., Amici A.,
Ruggieri S., Magni G.;
"Identification and characterization of YLR328W, the Saccharomyces
cerevisiae structural gene encoding NMN adenylyltransferase.
Expression and characterization of the recombinant enzyme.";
FEBS Lett. 455:13-17(1999).
[4]
CATALYTIC ACTIVITY.
PubMed=18098602;
Kornberg A.;
"The participation of inorganic pyrophosphate in the reversible
enzymatic synthesis of diphosphopyridine nucleotide.";
J. Biol. Chem. 176:1475-1476(1948).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=4291828; DOI=10.1016/0003-9861(67)90262-7;
Dahmen W., Webb B., Preiss J.;
"The deamido-diphosphopyridine nucleotide and diphosphopyridine
nucleotide pyrophosphorylases of Escherichia coli and yeast.";
Arch. Biochem. Biophys. 120:440-450(1967).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=3013296; DOI=10.1021/bi00360a037;
Natalini P., Ruggieri S., Raffaelli N., Magni G.;
"Nicotinamide mononucleotide adenylyltransferase. Molecular and
enzymatic properties of the homogeneous enzyme from baker's yeast.";
Biochemistry 25:3725-3729(1986).
[7]
FUNCTION.
PubMed=11884393; DOI=10.1074/jbc.M111773200;
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.;
"Manipulation of a nuclear NAD+ salvage pathway delays aging without
altering steady-state NAD+ levels.";
J. Biol. Chem. 277:18881-18890(2002).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12597897; DOI=10.1016/S1046-5928(02)00645-9;
Emanuelli M., Amici A., Carnevali F., Pierella F., Raffaelli N.,
Magni G.;
"Identification and characterization of a second NMN
adenylyltransferase gene in Saccharomyces cerevisiae.";
Protein Expr. Purif. 27:357-364(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95 AND SER-96,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-95; SER-96 AND
SER-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[14]
INDUCTION.
STRAIN=ATCC 201389 / BY4742;
PubMed=24759102; DOI=10.1074/jbc.M114.558643;
Kato M., Lin S.J.;
"YCL047C/POF1 is a novel nicotinamide mononucleotide
adenylyltransferase (NMNAT) in Saccharomyces cerevisiae.";
J. Biol. Chem. 289:15577-15587(2014).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10428462,
ECO:0000269|PubMed:11884393, ECO:0000269|PubMed:3013296,
ECO:0000269|PubMed:4291828}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000269|PubMed:10428462,
ECO:0000269|PubMed:18098602, ECO:0000269|PubMed:3013296}.
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+). {ECO:0000305|PubMed:11884393}.
-!- COFACTOR:
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000269|PubMed:10428462};
Note=Divalent metal cation. {ECO:0000269|PubMed:10428462};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.11 mM for ATP {ECO:0000269|PubMed:12597897,
ECO:0000269|PubMed:3013296};
KM=0.19 mM for NMN {ECO:0000269|PubMed:12597897,
ECO:0000269|PubMed:3013296};
KM=5 mM for NaMN {ECO:0000269|PubMed:3013296};
KM=0.073 mM for NAD(+) {ECO:0000269|PubMed:12597897};
KM=0.083 mM for diphosphate {ECO:0000269|PubMed:12597897};
pH dependence:
Optimum pH is 7.2-8.4. {ECO:0000269|PubMed:12597897,
ECO:0000269|PubMed:3013296};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
{ECO:0000305|PubMed:11884393}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
{ECO:0000305|PubMed:3013296, ECO:0000305|PubMed:4291828}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10428462,
ECO:0000269|PubMed:3013296}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-11803, EBI-11803;
P53204:NMA2; NbExp=6; IntAct=EBI-11803, EBI-23073;
Q9HAN9:NMNAT1 (xeno); NbExp=3; IntAct=EBI-11803, EBI-3917542;
P63279:UBE2I (xeno); NbExp=3; IntAct=EBI-11803, EBI-80168;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: Expression is high in early log-phase and significantly
drops as cells enter late log phase.
{ECO:0000269|PubMed:24759102}.
-!- MISCELLANEOUS: Present with 5130 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U20618; AAB64524.1; -; Genomic_DNA.
EMBL; BK006945; DAA09636.1; -; Genomic_DNA.
PIR; S53405; S53405.
RefSeq; NP_013432.1; NM_001182217.1.
ProteinModelPortal; Q06178; -.
SMR; Q06178; -.
BioGrid; 31592; 42.
DIP; DIP-1228N; -.
IntAct; Q06178; 13.
MINT; Q06178; -.
STRING; 4932.YLR328W; -.
iPTMnet; Q06178; -.
MaxQB; Q06178; -.
PaxDb; Q06178; -.
PRIDE; Q06178; -.
EnsemblFungi; YLR328W; YLR328W; YLR328W.
GeneID; 851039; -.
KEGG; sce:YLR328W; -.
EuPathDB; FungiDB:YLR328W; -.
SGD; S000004320; NMA1.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
InParanoid; Q06178; -.
KO; K06210; -.
OMA; CLILERT; -.
OrthoDB; EOG092C3YJ3; -.
BioCyc; MetaCyc:YLR328W-MONOMER; -.
BioCyc; YEAST:YLR328W-MONOMER; -.
Reactome; R-SCE-196807; Nicotinate metabolism.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
PRO; PR:Q06178; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:SGD.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR005248; NadD/NMNAT.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00482; TIGR00482; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
NAD; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
Phosphoprotein; Pyridine nucleotide biosynthesis; Reference proteome;
Transferase.
CHAIN 1 401 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 1.
/FTId=PRO_0000135018.
NP_BIND 172 174 ATP. {ECO:0000250|UniProtKB:Q96T66,
ECO:0000250|UniProtKB:Q9HAN9}.
NP_BIND 288 290 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 356 359 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 212 214 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 250 253 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 300 301 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
COMPBIAS 61 67 Poly-His.
BINDING 181 181 ATP. {ECO:0000250|UniProtKB:Q96T66}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
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


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