NMAH_SCHPO
ID NMAH_SCHPO Reviewed; 368 AA.
AC Q9UT53;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE Short=NMN/NaMN adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE EC=2.7.7.1 {ECO:0000250|UniProtKB:Q06178};
DE EC=2.7.7.18 {ECO:0000250|UniProtKB:Q06178};
DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE Short=NMN adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE Short=NMNAT {ECO:0000250|UniProtKB:Q06178};
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE Short=NaMN adenylyltransferase {ECO:0000250|UniProtKB:Q06178};
DE Short=NaMNAT {ECO:0000250|UniProtKB:Q06178};
GN ORFNames=SPAC806.06c {ECO:0000312|PomBase:SPAC806.06c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-85, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
CC mononucleotide (NMN) and ATP. Can also use the deamidated form;
CC nicotinic acid mononucleotide (NaMN) as substrate to form deamido-
CC NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for
CC NAD(+) biosynthesis. {ECO:0000250|UniProtKB:Q06178}.
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};
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:0000250|UniProtKB:Q06178};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q06178};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000250|UniProtKB:Q06178}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC {ECO:0000250|UniProtKB:Q06178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB55285.2; -; Genomic_DNA.
DR PIR; T39098; T39098.
DR RefSeq; NP_592856.2; NM_001018257.2.
DR AlphaFoldDB; Q9UT53; -.
DR SMR; Q9UT53; -.
DR BioGRID; 279489; 7.
DR STRING; 4896.SPAC806.06c.1; -.
DR iPTMnet; Q9UT53; -.
DR MaxQB; Q9UT53; -.
DR PaxDb; Q9UT53; -.
DR PRIDE; Q9UT53; -.
DR EnsemblFungi; SPAC806.06c.1; SPAC806.06c.1:pep; SPAC806.06c.
DR GeneID; 2543055; -.
DR KEGG; spo:SPAC806.06c; -.
DR PomBase; SPAC806.06c; -.
DR VEuPathDB; FungiDB:SPAC806.06c; -.
DR eggNOG; KOG3199; Eukaryota.
DR HOGENOM; CLU_033366_5_0_1; -.
DR InParanoid; Q9UT53; -.
DR OMA; VPHGIQR; -.
DR Reactome; R-SPO-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR PRO; PR:Q9UT53; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; ISO:PomBase.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; ISM:PomBase.
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; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..368
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase"
FT /id="PRO_0000316624"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 174..176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 212..215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 250..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 262..263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 318..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 368 AA; 42149 MW; 4EE320D84D917DAE CRC64;
MHTMNGDNFA NSFPKNPLLS RNSSSSNVIQ YSDEFSPDED WLNEHAAKEH EERIRRPSVN
RAWQKNSTSG GPSVSLEKRE ADVASLGEVM DLEEVPRGIT RQARQLNEYI FPKHRFRNHL
VDEGKIPLVL VACGSFSPIT YLHLRMFEMA TDTIQEQTNM ELVAGYFSPV NDHYKKEGLA
PAYHRVRMCE LACERTSSWL MVDAWESLQP SYTCTARVLD HFDEEINQKR GGITLSDGTK
RPCKIMLLAG GDLIASMGEP GVWSDKDLHH ILGKFGCCIV ERTGSDVWAF LLAHDIMFAY
RGNILVIKQL IYNDISSTKV RLFIRRGMSI RYLLPNSVIQ YIERYALYRD AEPVKTIFYQ
SPFVRMEP
