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Nicotinamide mononucleotide adenylyltransferase (NMN adenylyltransferase) (NMNAT) (EC 2.7.7.1) (NMN-specific adenylyltransferase) (Promoter of filamentation protein 1)

 POF1_YEAST              Reviewed;         258 AA.
P25576; D6VQX0;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
12-SEP-2018, entry version 120.
RecName: Full=Nicotinamide mononucleotide adenylyltransferase {ECO:0000303|PubMed:24759102};
Short=NMN adenylyltransferase;
Short=NMNAT;
EC=2.7.7.1 {ECO:0000269|PubMed:24759102};
AltName: Full=NMN-specific adenylyltransferase {ECO:0000303|PubMed:24759102};
AltName: Full=Promoter of filamentation protein 1 {ECO:0000303|PubMed:21460040};
Name=POF1 {ECO:0000303|PubMed:21460040};
OrderedLocusNames=YCL047C {ECO:0000312|SGD:S000000552};
ORFNames=YCL47C;
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=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[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]
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).
[4]
INTERACTION WITH UBC7, AND DISRUPTION PHENOTYPE.
PubMed=22204397; DOI=10.1186/1471-2180-11-268;
Costa I.M., Nasser T.H., Demasi M., Nascimento R.M., Netto L.E.,
Miyamoto S., Prado F.M., Monteiro G.;
"The promoter of filamentation (POF1) protein from Saccharomyces
cerevisiae is an ATPase involved in the protein quality control
process.";
BMC Microbiol. 11:268-268(2011).
[5]
FUNCTION, AND INTERACTION WITH KSS1.
PubMed=21460040; DOI=10.1101/gad.1998811;
Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
Gerstein M., Snyder M.;
"Diverse protein kinase interactions identified by protein microarrays
reveal novel connections between cellular processes.";
Genes Dev. 25:767-778(2011).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[7]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND 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. Involved in the salvage pathway for
NAD(+) biosynthesis via NMN (PubMed:24759102). Involved in the
filamentation pathway. Suppresses the filamentation defect of a
KSS1 deletion (PubMed:21460040). {ECO:0000269|PubMed:21460040,
ECO:0000269|PubMed:24759102}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000269|PubMed:24759102}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.26 mM for nicotinamide mononucleotide
{ECO:0000269|PubMed:24759102};
Vmax=119 nmol/h/mg enzyme {ECO:0000269|PubMed:24759102};
pH dependence:
Optimum pH is 10. {ECO:0000269|PubMed:24759102};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
{ECO:0000305|PubMed:24759102}.
-!- SUBUNIT: Interacts with KSS1 (PubMed:21460040). Interacts with
UBC7 (PubMed:22204397). {ECO:0000269|PubMed:21460040,
ECO:0000269|PubMed:22204397}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24759102}.
Nucleus {ECO:0000269|PubMed:24759102}.
-!- INDUCTION: Expression is slightly induced in late log phase.
{ECO:0000269|PubMed:24759102}.
-!- DISRUPTION PHENOTYPE: Lowers cellular NAD(+) levels and decreases
the efficiency of nicotinamide riboside (NR) utilization,
resistance to oxidative stress, and NR-induced life span extension
(PubMed:24759102). Highly sensitive to heat shock and higher
sensitivity to ER stress agents than wild-type cells
(PubMed:22204397). {ECO:0000269|PubMed:22204397,
ECO:0000269|PubMed:24759102}.
-!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. POF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X59720; CAA42369.1; -; Genomic_DNA.
EMBL; BK006937; DAA07439.1; -; Genomic_DNA.
PIR; S19376; S19376.
RefSeq; NP_009883.1; NM_001178692.1.
ProteinModelPortal; P25576; -.
BioGrid; 30938; 59.
IntAct; P25576; 3.
MINT; P25576; -.
STRING; 4932.YCL047C; -.
MaxQB; P25576; -.
PaxDb; P25576; -.
PRIDE; P25576; -.
EnsemblFungi; CAA42369; CAA42369; CAA42369.
EnsemblFungi; YCL047C; YCL047C; YCL047C.
GeneID; 850310; -.
KEGG; sce:YCL047C; -.
EuPathDB; FungiDB:YCL047C; -.
SGD; S000000552; POF1.
InParanoid; P25576; -.
KO; K19785; -.
OMA; SVNNADK; -.
OrthoDB; EOG092C4S7J; -.
BioCyc; YEAST:G3O-29302-MONOMER; -.
UniPathway; UPA00253; UER00600.
PRO; PR:P25576; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:SGD.
GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
CDD; cd02165; NMNAT; 1.
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.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; NAD; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Pyridine nucleotide biosynthesis;
Reference proteome; Transferase.
CHAIN 1 258 Nicotinamide mononucleotide
adenylyltransferase.
/FTId=PRO_0000202549.
NP_BIND 34 36 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 138 140 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 224 227 ATP. {ECO:0000250|UniProtKB:Q96T66}.
BINDING 43 43 ATP. {ECO:0000250|UniProtKB:Q96T66}.
SEQUENCE 258 AA; 29673 MW; 1A55281FC19854C7 CRC64;
MKKTFEQFRK SNLLFQVLKG PQHLECQKLF VLDSSFNPPH LAHFQLLSQT IKNFKLKDTR
SHVLLLLAVN NADKLPKPAS FPTRLEMMCL FADYLQEKLP QSVVSVGLTV FSKFIDKDKI
LHEQFVKGCS ADIGYLVGFD TIARIFDEKY YHPLKISDVM ESFMSGSQLY CLARGDCHLS
AESQLRYASD ILEGKFEPVI PREWGARIHV MQNDYPALRN VSSSEIRNKL KNGQVESLKD
ELPLCIYDYL INNKTIFD


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