ID   NMA1_YEAST              Reviewed;         401 AA.
AC   Q06178;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 78.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase 1;
DE            EC=2.7.7.1;
DE   AltName: Full=NAD(+) pyrophosphorylase 1;
DE   AltName: Full=NAD(+) diphosphorylase 1;
DE   AltName: Full=NMN adenylyltransferase 1;
GN   Name=NMA1; OrderedLocusNames=YLR328W; ORFNames=L8543.16;
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 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   MEDLINE=99355416; PubMed=10428462; DOI=10.1016/S0014-5793(99)00852-2;
RA   Emanuelli M., Carnevali F., Lorenzi M., Raffaelli N., Amici A.,
RA   Ruggieri S., Magni G.;
RT   "Identification and characterization of YLR328W, the Saccharomyces
RT   cerevisiae structural gene encoding NMN adenylyltransferase.
RT   Expression and characterization of the recombinant enzyme.";
RL   FEBS Lett. 455:13-17(1999).
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-91; SER-95 AND SER-96,
RP   AND MASS 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-44; SER-95 AND SER-96,
RP   AND MASS 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   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-11803, EBI-11803;
CC       P53204:NMA2; NbExp=1; IntAct=EBI-11803, EBI-23073;
CC       P47149:NNF1; NbExp=1; IntAct=EBI-11803, EBI-12098;
CC       P39986:SPF1; NbExp=1; IntAct=EBI-11803, EBI-3128;
CC       Q02821:SRP1; NbExp=1; IntAct=EBI-11803, EBI-1797;
CC       P38987:TEM1; NbExp=1; IntAct=EBI-11803, EBI-19113;
CC   -!- MISCELLANEOUS: Present with 5130 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; U20618; AAB64524.1; -; Genomic_DNA.
DR   PIR; S53405; S53405.
DR   RefSeq; NP_013432.1; -.
DR   HSSP; Q9HAN9; 1KR2.
DR   DIP; DIP:1228N; -.
DR   IntAct; Q06178; 13.
DR   Ensembl; YLR328W; Saccharomyces cerevisiae.
DR   GeneID; 851039; -.
DR   GenomeReviews; Y13138_GR; YLR328W.
DR   KEGG; sce:YLR328W; -.
DR   NMPDR; fig|4932.3.peg.4452; -.
DR   CYGD; YLR328w; -.
DR   SGD; S000004320; NMA1.
DR   HOGENOM; Q06178; -.
DR   OMA; Q06178; EPNVWAD.
DR   BioCyc; MetaCyc:YLR328W-MON; -.
DR   BRENDA; 2.7.7.1; 250.
DR   NextBio; 967639; -.
DR   GermOnline; YLR328W; Saccharomyces cerevisiae.
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:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase...; IDA:SGD.
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; Direct protein sequencing; NAD;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    401       Nicotinamide-nucleotide
FT                                adenylyltransferase 1.
FT                                /FTId=PRO_0000135018.
FT   COMPBIAS     61     67       Poly-His.
FT   MOD_RES      44     44       Phosphoserine.
FT   MOD_RES      91     91       Phosphoserine.
FT   MOD_RES      95     95       Phosphoserine.
FT   MOD_RES      96     96       Phosphoserine.
SQ   SEQUENCE   401 AA;  45859 MW;  A176964E56A30DD8 CRC64;
     MDPTRAPDFK PPSADEELIP PPDPESKIPK SIPIIPYVLA DANSSIDAPF NIKRKKKHPK
     HHHHHHHSRK EGNDKKHQHI PLNQDDFQPL SAEVSSEDDD ADFRSKERYG SDSTTESETR
     GVQKYQIADL EEVPHGIVRQ ARTLEDYEFP SHRLSKKLLD PNKLPLVIVA CGSFSPITYL
     HLRMFEMALD AISEQTRFEV IGGYYSPVSD NYQKQGLAPS YHRVRMCELA CERTSSWLMV
     DAWESLQPSY TRTAKVLDHF NHEINIKRGG VATVTGEKIG VKIMLLAGGD LIESMGEPNV
     WADADLHHIL GNYGCLIVER TGSDVRSFLL SHDIMYEHRR NILIIKQLIY NDISSTKVRL
     FIRRAMSVQY LLPNSVIRYI QEHRLYVDQT EPVKQVLGNK E
//