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   08-NOV-2023, entry version 144.
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};
GN   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; 65.
DR   IntAct; P25576; 3.
DR   MINT; P25576; -.
DR   STRING; 4932.YCL047C; -.
DR   MaxQB; P25576; -.
DR   PaxDb; 4932-YCL047C; -.
DR   PeptideAtlas; P25576; -.
DR   EnsemblFungi; YCL047C_mRNA; YCL047C; YCL047C.
DR   GeneID; 850310; -.
DR   KEGG; sce:YCL047C; -.
DR   AGR; SGD:S000000552; -.
DR   SGD; S000000552; POF1.
DR   VEuPathDB; FungiDB:YCL047C; -.
DR   eggNOG; ENOG502RXY8; Eukaryota.
DR   HOGENOM; CLU_032651_0_0_1; -.
DR   InParanoid; P25576; -.
DR   OMA; RLVMMEL; -.
DR   OrthoDB; 1331302at2759; -.
DR   BioCyc; YEAST:G3O-29302-MONOMER; -.
DR   BRENDA; 2.7.7.1; 984.
DR   UniPathway; UPA00253; UER00600.
DR   BioGRID-ORCS; 850310; 0 hits in 10 CRISPR screens.
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; HUPs; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR31285; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR31285:SF0; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96T66"
FT   BINDING         224..227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
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
//