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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (NAD( ) diphosphorylase 2) (NAD( ) pyrophosphorylase 2) (Nicotinamide-nucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (NMNAT 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) (NaMNAT 2)

 NMA2_YEAST              Reviewed;         395 AA.
P53204; D6VUE7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 138.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 2;
EC=2.7.7.1 {ECO:0000269|PubMed:12597897};
EC=2.7.7.18 {ECO:0000305|PubMed:11884393};
AltName: Full=NAD(+) diphosphorylase 2;
AltName: Full=NAD(+) pyrophosphorylase 2;
AltName: Full=Nicotinamide-nucleotide adenylyltransferase 2 {ECO:0000303|PubMed:12597897};
Short=NMN adenylyltransferase 2;
Short=NMNAT 2;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 2 {ECO:0000303|PubMed:11884393};
Short=NaMN adenylyltransferase 2;
Short=NaMNAT 2;
Name=NMA2 {ECO:0000303|PubMed:11884393};
OrderedLocusNames=YGR010W {ECO:0000312|SGD:S000003242};
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=9169869;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(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 1-15, FUNCTION, CATALYTIC ACTIVITY, AND
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).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-89 AND SER-90,
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).
[8]
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 (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). {ECO:0000250|UniProtKB:Q06178,
ECO:0000269|PubMed:11884393, ECO:0000269|PubMed:12597897}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000250|UniProtKB:Q06178,
ECO:0000269|PubMed:12597897}.
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+). {ECO:0000305|PubMed:11884393}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:12597897};
Note=Divalent metal cation. {ECO:0000269|PubMed:12597897};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.4 mM for ATP {ECO:0000269|PubMed:12597897};
KM=0.13 mM for NMN {ECO:0000269|PubMed:12597897};
KM=0.023 mM for NAD(+) {ECO:0000269|PubMed:12597897};
KM=5 mM for diphosphate {ECO:0000269|PubMed:12597897};
pH dependence:
Optimum pH is 6.5-8.0. {ECO:0000269|PubMed:12597897};
-!- 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:12597897}.
-!- INTERACTION:
Q06178:NMA1; NbExp=8; IntAct=EBI-23073, EBI-11803;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11884393}.
-!- INDUCTION: Expression is slightly induced in late log phase.
{ECO:0000269|PubMed:24759102}.
-!- MISCELLANEOUS: Present with 1430 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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EMBL; Z72795; CAA96993.1; -; Genomic_DNA.
EMBL; BK006941; DAA08108.1; -; Genomic_DNA.
PIR; S64299; S64299.
RefSeq; NP_011524.1; NM_001181139.1.
ProteinModelPortal; P53204; -.
SMR; P53204; -.
BioGrid; 33254; 43.
DIP; DIP-1227N; -.
IntAct; P53204; 7.
MINT; MINT-403491; -.
STRING; 4932.YGR010W; -.
iPTMnet; P53204; -.
MaxQB; P53204; -.
PRIDE; P53204; -.
EnsemblFungi; YGR010W; YGR010W; YGR010W.
GeneID; 852893; -.
KEGG; sce:YGR010W; -.
EuPathDB; FungiDB:YGR010W; -.
SGD; S000003242; NMA2.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
InParanoid; P53204; -.
KO; K06210; -.
OMA; YKKQGLA; -.
OrthoDB; EOG092C3YJ3; -.
BioCyc; MetaCyc:YGR010W-MONOMER; -.
BioCyc; YEAST:YGR010W-MONOMER; -.
BRENDA; 2.7.7.1; 984.
BRENDA; 2.7.7.18; 984.
Reactome; R-SCE-196807; Nicotinate metabolism.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
PRO; PR:P53204; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Direct protein sequencing; NAD;
Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
CHAIN 1 395 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 2.
/FTId=PRO_0000135019.
NP_BIND 166 168 ATP. {ECO:0000250|UniProtKB:Q96T66,
ECO:0000250|UniProtKB:Q9HAN9}.
NP_BIND 282 284 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 350 353 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 206 208 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 244 247 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 294 295 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
BINDING 175 175 ATP. {ECO:0000250|UniProtKB:Q96T66}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
SEQUENCE 395 AA; 44909 MW; 4A358AF7885B6568 CRC64;
MDPTKAPDFK PPQPNEELQP PPDPTHTIPK SGPIVPYVLA DYNSSIDAPF NLDIYKTLSS
RKKNANSSNR MDHIPLNTSD FQPLSRDVSS EEESEGQSNG IDATLQDVTM TGNLGVLKSQ
IADLEEVPHT IVRQARTIED YEFPVHRLTK KLQDPEKLPL IIVACGSFSP ITYLHLRMFE
MALDDINEQT RFEVVGGYFS PVSDNYQKRG LAPAYHRVRM CELACERTSS WLMVDAWESL
QSSYTRTAKV LDHFNHEINI KRGGIMTVDG EKMGVKIMLL AGGDLIESMG EPHVWADSDL
HHILGNYGCL IVERTGSDVR SFLLSHDIMY EHRRNILIIK QLIYNDISST KVRLFIRRGM
SVQYLLPNSV IRYIQEYNLY INQSEPVKQV LDSKE


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