POF1L_SCHPO
ID POF1L_SCHPO Reviewed; 249 AA.
AC Q9P7T7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative nicotinamide mononucleotide adenylyltransferase {ECO:0000250|UniProtKB:P25576};
DE Short=NMN adenylyltransferase {ECO:0000250|UniProtKB:P25576};
DE Short=NMNAT {ECO:0000250|UniProtKB:P25576};
DE EC=2.7.7.1 {ECO:0000250|UniProtKB:P25576};
DE AltName: Full=NMN-specific adenylyltransferase {ECO:0000250|UniProtKB:P25576};
DE AltName: Full=Protein POF1 homolog {ECO:0000250|UniProtKB:P25576};
GN ORFNames=SPAC694.03 {ECO:0000312|PomBase:SPAC694.03};
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 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).
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. {ECO:0000250|UniProtKB:P25576}.
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:P25576};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC {ECO:0000250|UniProtKB:P25576}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC POF1 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB71841.1; -; Genomic_DNA.
DR PIR; T50248; T50248.
DR RefSeq; NP_594483.1; NM_001019912.2.
DR AlphaFoldDB; Q9P7T7; -.
DR SMR; Q9P7T7; -.
DR BioGRID; 279491; 4.
DR STRING; 4896.SPAC694.03.1; -.
DR iPTMnet; Q9P7T7; -.
DR MaxQB; Q9P7T7; -.
DR PaxDb; Q9P7T7; -.
DR EnsemblFungi; SPAC694.03.1; SPAC694.03.1:pep; SPAC694.03.
DR GeneID; 2543057; -.
DR KEGG; spo:SPAC694.03; -.
DR PomBase; SPAC694.03; -.
DR VEuPathDB; FungiDB:SPAC694.03; -.
DR eggNOG; ENOG502RXY8; Eukaryota.
DR HOGENOM; CLU_032651_0_0_1; -.
DR InParanoid; Q9P7T7; -.
DR OMA; FNPKYYP; -.
DR PhylomeDB; Q9P7T7; -.
DR UniPathway; UPA00253; UER00600.
DR PRO; PR:Q9P7T7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; ISO:PomBase.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; ISO:PomBase.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..249
FT /note="Putative nicotinamide mononucleotide
FT adenylyltransferase"
FT /id="PRO_0000350758"
FT BINDING 39..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 129..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 214..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
SQ SEQUENCE 249 AA; 28274 MW; A7973EF384A7D55A CRC64;
MDQAKKYANL LDSFRSSTED ILLLERLEVS DKPIYVLDSS FNPPHFAHLG MCLSIPKGSQ
LLLLLSITNA DKPVAPAAFN ERILMMEKLK TLIHNCTVSV AICKHALFVD KCRSISNKLG
PREQVYLVGF DTLIRILDCK YYKEKAMQQV LQPFFSCSQI LCFSREVDGT TTDDQAQYLE
KIKKSLLPNI PSQWSEKIKL TKLKGNVGFG VSSTRARQAI ISGDEETQRK IIPQEILNVI
KVIQPYRHR
