Nicotinamidase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53184 (PNC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nicotinamidase
EC=3.5.1.19

Alternative name(s):
Nicotine deamidase
Short name=NAMase

Gene names

Name:	PNC1
Ordered Locus Names:	YGL037C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the deamidation of nicotinamide, an early step in the NAD⁺ salvage pathway. Positively regulates SIR2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide, an inhibitor of SIR2, during times of stress. Acts also on nicotinyl hydroxamate. Ref.4 Ref.7 Ref.10
Catalytic activity	Nicotinamide + H₂O = nicotinate + NH₃.
Enzyme regulation	Inhibited by N-ethylmaleimide, HgCl₂ and PCMB. Competitively inhibited by NAD, NMN and 3-acetylpyridine. Ref.5 Ref.6
Pathway	Cofactor biosynthesis; nicotinate biosynthesis; nicotinate from nicotinamide: step 1/1.
Subcellular location	Cytoplasm. Nucleus. Peroxisome. Note: Concentrates in peroxisomes. Ref.7 Ref.8
Induction	Induced during the stationary phase of growth, by calorie restriction, by various hyperosmotic shocks or by low-intensity stress (at protein level). Ref.4 Ref.5 Ref.6 Ref.7
Miscellaneous	Has a cis-peptide bond at 162-Val-Ala-163. Present with 7720 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the pncA family.
Biophysicochemical properties	Kinetic parameters: K_M=5.8 µM for nicotinamide Ref.5 Ref.6 Ref.12 K_M=32 µM for nicotinyl hydroxamate K_M=0.2 mM for pyrazinamide V_max=50.2 µmol/min/mg enzyme for nicotinamide V_max=59.4 µmol/min/mg enzyme for pyrazinamide pH dependence: Optimum pH is 6.5-7.5. Temperature dependence: Heating at 60 degrees Celsius inactivates the enzyme. Heating at 60 degrees Celsius in the presence of substrate prevents inactivation.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm Nucleus Peroxisome
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing at rDNA Inferred from mutant phenotype. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW replicative cell aging Inferred from expression pattern Ref.7. Source: SGD
Cellular component	nucleus Inferred from direct assay Ref.7. Source: SGD peroxisome Inferred from direct assay Ref.7. Source: SGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinamidase activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRP1	Q02821	1	EBI-23741,EBI-1797

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 216

216

Nicotinamidase

PRO_0000206558

Sites

Active site

122

Active site

167

Metal binding

Zinc

Metal binding

Zinc

Metal binding

Zinc

Amino acid modifications

Modified residue

174

Phosphoserine Ref.11

Secondary structure

216

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P53184 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C40B23C4228B6E3A
Show »

FASTA

216

24,993

        10         20         30         40         50         60 
MKTLIVVDMQ NDFISPLGSL TVPKGEELIN PISDLMQDAD RDWHRIVVTR DWHPSRHISF 

        70         80         90        100        110        120 
AKNHKDKEPY STYTYHSPRP GDDSTQEGIL WPVHCVKNTW GSQLVDQIMD QVVTKHIKIV 

       130        140        150        160        170        180 
DKGFLTDREY YSAFHDIWNF HKTDMNKYLE KHHTDEVYIV GVALEYCVKA TAISAAELGY 

       190        200        210 
KTTVLLDYTR PISDDPEVIN KVKEELKAHN INVVDK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Identification and functional analysis of the Saccharomyces cerevisiae nicotinamidase gene, PNC1." Ghislain M., Talla E., Francois J.M. Yeast 19:215-224(2002) [PubMed: 11816029] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11, FUNCTION, INDUCTION.
[5]	"Hydrolysis of nicotinyl hydroxamate by a yeast nicotinamidase." Bernheim M.L.C. Arch. Biochem. Biophys. 120:186-191(1967) [PubMed: 6058082] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[6]	"Inhibition of nicotinamidase by nicotinamide adenine dinucleotide." Calbreath D.F., Joshi J.G. J. Biol. Chem. 246:4334-4339(1971) [PubMed: 4326215] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[7]	"Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae." Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Sinclair D.A. Nature 423:181-185(2003) [PubMed: 12736687] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity." Gallo C.M., Smith D.L. Jr., Smith J.S. Mol. Cell. Biol. 24:1301-1312(2004) [PubMed: 14729974] [Abstract] Cited for: FUNCTION.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, MASS SPECTROMETRY.
[12]	"Crystal structure of the yeast nicotinamidase Pnc1p." Hu G., Taylor A.B., McAlister-Henn L., Hart P.J. Arch. Biochem. Biophys. 461:66-75(2007) [PubMed: 17382284] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z72559 Genomic DNA. Translation: CAA96739.1.
AY558481 Genomic DNA. Translation: AAS56807.1.
BK006941 Genomic DNA. Translation: DAA08063.1.

PIR

S64039.

RefSeq

NP_011478.1. NM_001180902.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H0R	X-ray	2.90	A/B/C/D/E/F/G	1-216	[»]

ProteinModelPortal

P53184.

SMR

P53184. Positions 1-216.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2070N.

IntAct

P53184. 9 interactions.

MINT

MINT-522829.

STRING

P53184.

Proteomic databases

PeptideAtlas

P53184.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL037C; YGL037C; YGL037C.

GeneID

852846.

KEGG

sce:YGL037C.

NMPDR

fig|4932.3.peg.2585.

Organism-specific databases

CYGD

YGL037c.

SGD

S000003005. PNC1.

Phylogenomic databases

eggNOG

fuNOG10585.

GeneTree

EFGT00050000006824.

HOGENOM

HBG752434.

OMA

IHCVANT.

OrthoDB

EOG4XSQ09.

Gene expression databases

ArrayExpress

P53184.

Genevestigator

P53184.

GermOnline

YGL037C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000868. Isochorismatase-like.
[Graphical view]

Gene3D

G3DSA:3.40.50.850. Isochorismatase_hydro. 1 hit.

K01440.

Pfam

PF00857. Isochorismatase. 1 hit.
[Graphical view]

SUPFAM

SSF52499. Iscrsm_hydrolase. 1 hit.

ProtoNet

Search...

Other

NextBio

972431.

Entry information

Entry name

PNC1_YEAST

Accession

Primary (citable) accession number: P53184
Secondary accession number(s): D6VUA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents