ID PNC1_SCHPO Reviewed; 220 AA.
AC Q9USS0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Nicotinamidase;
DE EC=3.5.1.19;
DE AltName: Full=Nicotinamide deamidase;
DE Short=NAMase;
GN Name=pnc1; ORFNames=SPBC365.20c;
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 deamidation of nicotinamide, an early step in
CC the NAD(+) salvage pathway. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + nicotinamide = NH4(+) + nicotinate;
CC Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19;
CC -!- PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate
CC from nicotinamide: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}. Peroxisome
CC {ECO:0000250|UniProtKB:P53184}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB60673.2; -; Genomic_DNA.
DR RefSeq; NP_596029.2; NM_001021938.3.
DR AlphaFoldDB; Q9USS0; -.
DR SMR; Q9USS0; -.
DR BioGRID; 277422; 7.
DR STRING; 284812.Q9USS0; -.
DR iPTMnet; Q9USS0; -.
DR MaxQB; Q9USS0; -.
DR PaxDb; 4896-SPBC365-20c-1; -.
DR EnsemblFungi; SPBC365.20c.1; SPBC365.20c.1:pep; SPBC365.20c.
DR GeneID; 2540906; -.
DR KEGG; spo:SPBC365.20c; -.
DR PomBase; SPBC365.20c; pnc1.
DR VEuPathDB; FungiDB:SPBC365.20c; -.
DR eggNOG; KOG4003; Eukaryota.
DR HOGENOM; CLU_068979_13_0_1; -.
DR InParanoid; Q9USS0; -.
DR OMA; AKILYQN; -.
DR PhylomeDB; Q9USS0; -.
DR UniPathway; UPA00830; UER00790.
DR PRO; PR:Q9USS0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008936; F:nicotinamidase activity; ISO:PomBase.
DR GO; GO:0019358; P:nicotinate nucleotide salvage; ISO:PomBase.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR PANTHER; PTHR11080:SF2; LD05707P; 1.
DR PANTHER; PTHR11080; PYRAZINAMIDASE/NICOTINAMIDASE; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Peroxisome;
KW Pyridine nucleotide biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..220
FT /note="Nicotinamidase"
FT /id="PRO_0000371807"
FT ACT_SITE 11
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /evidence="ECO:0000255"
FT ACT_SITE 163
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P53184"
SQ SEQUENCE 220 AA; 24501 MW; 923BFD3507AF1275 CRC64;
MSFHPALIIV DVQNDFVHPV YISSGESALE VVPVINRLLE NDYKWDTVIA TKDVHPKDHL
SFTTSHSSTP KPSGTVVNIE AYGHVYKQTL WNSHCVENTP GCEFPDSLNG DRIEFVIPKG
SDRLVESYSG FYDAIGRDNG LKAILDKKGI TDVFIAGVAT DICVKETALH ARHWYNTYII
SEAVKGSSTE SHNQAIKDFR DAKIEVISEK DPILQSVRKV
//
