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Protein

Nicotinamidase

Gene

PNC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Nicotinamide + H2O = nicotinate + NH3.1 Publication

Enzyme regulationi

Inhibited by N-ethylmaleimide, HgCl2 and PCMB. Competitively inhibited by NAD, NMN and 3-acetylpyridine.2 Publications

Kineticsi

  1. KM=5.8 µM for nicotinamide3 Publications
  2. KM=32 µM for nicotinyl hydroxamate3 Publications
  3. KM=0.2 mM for pyrazinamide3 Publications
  1. Vmax=50.2 µmol/min/mg enzyme for nicotinamide3 Publications
  2. Vmax=59.4 µmol/min/mg enzyme for pyrazinamide3 Publications

pH dependencei

Optimum pH is 6.5-7.5.3 Publications

Temperature dependencei

Heating at 60 degrees Celsius inactivates the enzyme. Heating at 60 degrees Celsius in the presence of substrate prevents inactivation.3 Publications

Pathwayi: nicotinate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinate from nicotinamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinamidase (PNC1)
This subpathway is part of the pathway nicotinate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes nicotinate from nicotinamide, the pathway nicotinate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Sequence analysis
Metal bindingi51 – 511ZincCombined sources1 Publication
Metal bindingi53 – 531ZincCombined sources1 Publication
Metal bindingi94 – 941ZincCombined sources1 Publication
Active sitei122 – 1221Sequence analysis
Active sitei167 – 1671NucleophileSequence analysis

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • nicotinamidase activity Source: SGD

GO - Biological processi

  • chromatin silencing at rDNA Source: SGD
  • chromatin silencing at telomere Source: SGD
  • negative regulation of DNA amplification Source: SGD
  • nicotinate nucleotide salvage Source: SGD
  • replicative cell aging Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YGL037C-MONOMER.
BRENDAi3.5.1.19. 984.
UniPathwayiUPA00830; UER00790.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamidase (EC:3.5.1.191 Publication)
Alternative name(s):
Nicotine deamidase
Short name:
NAMase
Gene namesi
Name:PNC1
Ordered Locus Names:YGL037C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL037C.
SGDiS000003005. PNC1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • cytoplasm Source: SGD
  • nucleus Source: SGD
  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216NicotinamidasePRO_0000206558Add
BLAST

Proteomic databases

MaxQBiP53184.
PeptideAtlasiP53184.
TopDownProteomicsiP53184.

PTM databases

iPTMnetiP53184.

Expressioni

Inductioni

Induced during the stationary phase of growth, by calorie restriction, by various hyperosmotic shocks or by low-intensity stress (at protein level).2 Publications

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SRP1Q028211EBI-23741,EBI-1797

Protein-protein interaction databases

BioGridi33210. 43 interactions.
DIPiDIP-2070N.
IntActiP53184. 10 interactions.
MINTiMINT-522829.

Chemistry

BindingDBiP53184.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi11 – 144Combined sources
Helixi25 – 284Combined sources
Helixi29 – 379Combined sources
Helixi39 – 413Combined sources
Beta strandi43 – 519Combined sources
Helixi61 – 633Combined sources
Beta strandi72 – 765Combined sources
Beta strandi85 – 895Combined sources
Helixi100 – 1023Combined sources
Helixi106 – 11510Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi132 – 1354Combined sources
Helixi145 – 1517Combined sources
Beta strandi156 – 1627Combined sources
Turni164 – 1663Combined sources
Helixi167 – 17711Combined sources
Beta strandi181 – 19010Combined sources
Helixi196 – 20813Combined sources
Beta strandi212 – 2143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0RX-ray2.90A/B/C/D/E/F/G1-216[»]
3V8EX-ray2.71A/B/C/D/E/F/G1-216[»]
ProteinModelPortaliP53184.
SMRiP53184. Positions 1-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53184.

Family & Domainsi

Sequence similaritiesi

Belongs to the PncA family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000064935.
HOGENOMiHOG000078666.
InParanoidiP53184.
KOiK01440.
OMAiPIHCVAN.
OrthoDBiEOG7DJSZ0.

Family and domain databases

Gene3Di3.40.50.850. 1 hit.
InterProiIPR000868. Isochorismatase-like.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
[Graphical view]
SUPFAMiSSF52499. SSF52499. 1 hit.

Sequencei

Sequence statusi: Complete.

P53184-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLIVVDMQ NDFISPLGSL TVPKGEELIN PISDLMQDAD RDWHRIVVTR
60 70 80 90 100
DWHPSRHISF AKNHKDKEPY STYTYHSPRP GDDSTQEGIL WPVHCVKNTW
110 120 130 140 150
GSQLVDQIMD QVVTKHIKIV DKGFLTDREY YSAFHDIWNF HKTDMNKYLE
160 170 180 190 200
KHHTDEVYIV GVALEYCVKA TAISAAELGY KTTVLLDYTR PISDDPEVIN
210
KVKEELKAHN INVVDK
Length:216
Mass (Da):24,993
Last modified:October 1, 1996 - v1
Checksum:iC40B23C4228B6E3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72559 Genomic DNA. Translation: CAA96739.1.
AY558481 Genomic DNA. Translation: AAS56807.1.
BK006941 Genomic DNA. Translation: DAA08063.1.
PIRiS64039.
RefSeqiNP_011478.3. NM_001180902.3.

Genome annotation databases

EnsemblFungiiYGL037C; YGL037C; YGL037C.
GeneIDi852846.
KEGGisce:YGL037C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72559 Genomic DNA. Translation: CAA96739.1.
AY558481 Genomic DNA. Translation: AAS56807.1.
BK006941 Genomic DNA. Translation: DAA08063.1.
PIRiS64039.
RefSeqiNP_011478.3. NM_001180902.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0RX-ray2.90A/B/C/D/E/F/G1-216[»]
3V8EX-ray2.71A/B/C/D/E/F/G1-216[»]
ProteinModelPortaliP53184.
SMRiP53184. Positions 1-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33210. 43 interactions.
DIPiDIP-2070N.
IntActiP53184. 10 interactions.
MINTiMINT-522829.

Chemistry

BindingDBiP53184.

PTM databases

iPTMnetiP53184.

Proteomic databases

MaxQBiP53184.
PeptideAtlasiP53184.
TopDownProteomicsiP53184.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL037C; YGL037C; YGL037C.
GeneIDi852846.
KEGGisce:YGL037C.

Organism-specific databases

EuPathDBiFungiDB:YGL037C.
SGDiS000003005. PNC1.

Phylogenomic databases

GeneTreeiENSGT00530000064935.
HOGENOMiHOG000078666.
InParanoidiP53184.
KOiK01440.
OMAiPIHCVAN.
OrthoDBiEOG7DJSZ0.

Enzyme and pathway databases

UniPathwayiUPA00830; UER00790.
BioCyciYEAST:YGL037C-MONOMER.
BRENDAi3.5.1.19. 984.

Miscellaneous databases

EvolutionaryTraceiP53184.
NextBioi972431.
PROiP53184.

Family and domain databases

Gene3Di3.40.50.850. 1 hit.
InterProiIPR000868. Isochorismatase-like.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
[Graphical view]
SUPFAMiSSF52499. SSF52499. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPNC1_YEAST
AccessioniPrimary (citable) accession number: P53184
Secondary accession number(s): D6VUA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Has a cis-peptide bond at 162-Val-Ala-163.
Present with 7720 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.