POF1_YEAST
ID POF1_YEAST Reviewed; 258 AA.
AC P25576; D6VQX0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Nicotinamide mononucleotide adenylyltransferase {ECO:0000303|PubMed:24759102};
DE Short=NMN adenylyltransferase;
DE Short=NMNAT;
DE EC=2.7.7.1 {ECO:0000269|PubMed:24759102};
DE AltName: Full=NMN-specific adenylyltransferase {ECO:0000303|PubMed:24759102};
DE AltName: Full=Promoter of filamentation protein 1 {ECO:0000303|PubMed:21460040};
GN Name=POF1 {ECO:0000303|PubMed:21460040};
GN OrderedLocusNames=YCL047C {ECO:0000312|SGD:S000000552}; ORFNames=YCL47C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 [4]
RP INTERACTION WITH UBC7, AND DISRUPTION PHENOTYPE.
RX PubMed=22204397; DOI=10.1186/1471-2180-11-268;
RA Costa I.M., Nasser T.H., Demasi M., Nascimento R.M., Netto L.E.,
RA Miyamoto S., Prado F.M., Monteiro G.;
RT "The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae
RT is an ATPase involved in the protein quality control process.";
RL BMC Microbiol. 11:268-268(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH KSS1.
RX PubMed=21460040; DOI=10.1101/gad.1998811;
RA Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M.,
RA Gerstein M., Snyder M.;
RT "Diverse protein kinase interactions identified by protein microarrays
RT reveal novel connections between cellular processes.";
RL Genes Dev. 25:767-778(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND 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. Involved in the salvage pathway for
CC NAD(+) biosynthesis via NMN (PubMed:24759102). Involved in the
CC filamentation pathway. Suppresses the filamentation defect of a KSS1
CC deletion (PubMed:21460040). {ECO:0000269|PubMed:21460040,
CC ECO:0000269|PubMed:24759102}.
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:24759102};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.26 mM for nicotinamide mononucleotide
CC {ECO:0000269|PubMed:24759102};
CC Vmax=119 nmol/h/mg enzyme {ECO:0000269|PubMed:24759102};
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:24759102};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000305|PubMed:24759102}.
CC -!- SUBUNIT: Interacts with KSS1 (PubMed:21460040). Interacts with UBC7
CC (PubMed:22204397). {ECO:0000269|PubMed:21460040,
CC ECO:0000269|PubMed:22204397}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24759102}. Nucleus
CC {ECO:0000269|PubMed:24759102}.
CC -!- INDUCTION: Expression is slightly induced in late log phase.
CC {ECO:0000269|PubMed:24759102}.
CC -!- DISRUPTION PHENOTYPE: Lowers cellular NAD(+) levels and decreases the
CC efficiency of nicotinamide riboside (NR) utilization, resistance to
CC oxidative stress, and NR-induced life span extension (PubMed:24759102).
CC Highly sensitive to heat shock and higher sensitivity to ER stress
CC agents than wild-type cells (PubMed:22204397).
CC {ECO:0000269|PubMed:22204397, ECO:0000269|PubMed:24759102}.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC POF1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59720; CAA42369.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07439.1; -; Genomic_DNA.
DR PIR; S19376; S19376.
DR RefSeq; NP_009883.1; NM_001178692.1.
DR AlphaFoldDB; P25576; -.
DR SMR; P25576; -.
DR BioGRID; 30938; 64.
DR IntAct; P25576; 3.
DR MINT; P25576; -.
DR STRING; 4932.YCL047C; -.
DR MaxQB; P25576; -.
DR PaxDb; P25576; -.
DR PRIDE; P25576; -.
DR EnsemblFungi; YCL047C_mRNA; YCL047C; YCL047C.
DR GeneID; 850310; -.
DR KEGG; sce:YCL047C; -.
DR SGD; S000000552; POF1.
DR VEuPathDB; FungiDB:YCL047C; -.
DR eggNOG; ENOG502RXY8; Eukaryota.
DR HOGENOM; CLU_032651_0_0_1; -.
DR InParanoid; P25576; -.
DR OMA; FNPKYYP; -.
DR BioCyc; YEAST:G3O-29302-MON; -.
DR BRENDA; 2.7.7.1; 984.
DR UniPathway; UPA00253; UER00600.
DR PRO; PR:P25576; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25576; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..258
FT /note="Nicotinamide mononucleotide adenylyltransferase"
FT /id="PRO_0000202549"
FT BINDING 34..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 138..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 224..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
SQ 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
