NMA2_YEAST
ID NMA2_YEAST Reviewed; 395 AA.
AC P53204; D6VUE7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
DE Short=NMN/NaMN adenylyltransferase 2;
DE EC=2.7.7.1 {ECO:0000269|PubMed:12597897};
DE EC=2.7.7.18 {ECO:0000305|PubMed:11884393};
DE AltName: Full=NAD(+) diphosphorylase 2;
DE AltName: Full=NAD(+) pyrophosphorylase 2;
DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase 2 {ECO:0000303|PubMed:12597897};
DE Short=NMN adenylyltransferase 2;
DE Short=NMNAT 2;
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 2 {ECO:0000303|PubMed:11884393};
DE Short=NaMN adenylyltransferase 2;
DE Short=NaMNAT 2;
GN Name=NMA2 {ECO:0000303|PubMed:11884393};
GN OrderedLocusNames=YGR010W {ECO:0000312|SGD:S000003242};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12597897; DOI=10.1016/s1046-5928(02)00645-9;
RA Emanuelli M., Amici A., Carnevali F., Pierella F., Raffaelli N., Magni G.;
RT "Identification and characterization of a second NMN adenylyltransferase
RT gene in Saccharomyces cerevisiae.";
RL Protein Expr. Purif. 27:357-364(2003).
RN [4]
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., Lin S.S.,
RA 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-89 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP 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 (PubMed:12597897). Can also use the
CC deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to
CC form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage
CC pathways for NAD(+) biosynthesis (By similarity). Predominantly acts in
CC the salvage pathways via NMN (PubMed:11884393).
CC {ECO:0000250|UniProtKB:Q06178, ECO:0000269|PubMed:11884393,
CC ECO:0000269|PubMed:12597897}.
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:0000250|UniProtKB:Q06178, ECO:0000269|PubMed:12597897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58437; EC=2.7.7.18;
CC Evidence={ECO:0000305|PubMed:11884393};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12597897};
CC Note=Divalent metal cation. {ECO:0000269|PubMed:12597897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for ATP {ECO:0000269|PubMed:12597897};
CC KM=0.13 mM for NMN {ECO:0000269|PubMed:12597897};
CC KM=0.023 mM for NAD(+) {ECO:0000269|PubMed:12597897};
CC KM=5 mM for diphosphate {ECO:0000269|PubMed:12597897};
CC pH dependence:
CC Optimum pH is 6.5-8.0. {ECO:0000269|PubMed:12597897};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000305|PubMed:11884393}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000305|PubMed:12597897}.
CC -!- INTERACTION:
CC P53204; Q06178: NMA1; NbExp=6; IntAct=EBI-23073, EBI-11803;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11884393}.
CC -!- INDUCTION: Expression is slightly induced in late log phase.
CC {ECO:0000269|PubMed:24759102}.
CC -!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z72795; CAA96993.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08108.1; -; Genomic_DNA.
DR PIR; S64299; S64299.
DR RefSeq; NP_011524.1; NM_001181139.1.
DR AlphaFoldDB; P53204; -.
DR SMR; P53204; -.
DR BioGRID; 33254; 52.
DR DIP; DIP-1227N; -.
DR IntAct; P53204; 2.
DR MINT; P53204; -.
DR STRING; 4932.YGR010W; -.
DR iPTMnet; P53204; -.
DR MaxQB; P53204; -.
DR PaxDb; P53204; -.
DR PRIDE; P53204; -.
DR EnsemblFungi; YGR010W_mRNA; YGR010W; YGR010W.
DR GeneID; 852893; -.
DR KEGG; sce:YGR010W; -.
DR SGD; S000003242; NMA2.
DR VEuPathDB; FungiDB:YGR010W; -.
DR eggNOG; KOG3199; Eukaryota.
DR GeneTree; ENSGT00950000183179; -.
DR HOGENOM; CLU_033366_5_0_1; -.
DR InParanoid; P53204; -.
DR OMA; PGLWARE; -.
DR BioCyc; MetaCyc:YGR010W-MON; -.
DR BioCyc; YEAST:YGR010W-MON; -.
DR BRENDA; 2.7.7.1; 984.
DR BRENDA; 2.7.7.18; 984.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR PRO; PR:P53204; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53204; protein.
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 activity; IDA:SGD.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
DR CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; NAD; Nucleotide-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase 2"
FT /id="PRO_0000135019"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66,
FT ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 244..247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 282..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 294..295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
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
