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PNC1_SCHPO
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   03-AUG-2022, entry version 110.
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; 4896.SPBC365.20c.1; -.
DR   MaxQB; Q9USS0; -.
DR   PaxDb; Q9USS0; -.
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; IQHDFLP; -.
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; -; 1.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF52499; SSF52499; 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
 
 
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