ID   NMA2_YEAST              Reviewed;         395 AA.
AC   P53204;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase 2;
DE            EC=2.7.7.1;
DE   AltName: Full=NAD(+) pyrophosphorylase 2;
DE   AltName: Full=NAD(+) diphosphorylase 2;
DE   AltName: Full=NMN adenylyltransferase 2;
GN   Name=NMA2; OrderedLocusNames=YGR010W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313265; PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11884393; DOI=10.1074/jbc.M111773200;
RA   Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Cohen H.,
RA   Lin S.S., Manchester J.K., Gordon J.I., Sinclair D.A.;
RT   "Manipulation of a nuclear NAD+ salvage pathway delays aging without
RT   altering steady-state NAD+ levels.";
RL   J. Biol. Chem. 277:18881-18890(2002).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
CC       diphosphate + NAD(+).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide ribonucleotide: step 1/1.
CC   -!- INTERACTION:
CC       Q06178:NMA1; NbExp=1; IntAct=EBI-23073, EBI-11803;
CC       Q02821:SRP1; NbExp=1; IntAct=EBI-23073, EBI-1797;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z72795; CAA96993.1; -; Genomic_DNA.
DR   PIR; S64299; S64299.
DR   RefSeq; NP_011524.1; -.
DR   HSSP; Q9HAN9; 1KR2.
DR   DIP; DIP:1227N; -.
DR   IntAct; P53204; 7.
DR   Ensembl; YGR010W; Saccharomyces cerevisiae.
DR   GeneID; 852893; -.
DR   GenomeReviews; Y13135_GR; YGR010W.
DR   KEGG; sce:YGR010W; -.
DR   NMPDR; fig|4932.3.peg.2634; -.
DR   CYGD; YGR010w; -.
DR   SGD; S000003242; NMA2.
DR   HOGENOM; P53204; -.
DR   OMA; P53204; RGVKIML.
DR   BioCyc; MetaCyc:YGR010W-MON; -.
DR   BRENDA; 2.7.7.1; 250.
DR   NextBio; 972562; -.
DR   ArrayExpress; P53204; -.
DR   GermOnline; YGR010W; Saccharomyces cerevisiae.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase...; IEA:EC.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase a...; IGI:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR005248; NAMN_adtrnsfrase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR12039; NAMN_adtrnsfrase; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR00482; NAMN_adtrnsfrase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; NAD; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    395       Nicotinamide-nucleotide
FT                                adenylyltransferase 2.
FT                                /FTId=PRO_0000135019.
FT   MOD_RES      85     85       Phosphoserine.
SQ   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
//