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Protein

Nicotinamidase

Gene

PNC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Active sitei8Sequence analysis1
Metal bindingi51ZincCombined sources1 Publication1
Metal bindingi53ZincCombined sources1 Publication1
Metal bindingi94ZincCombined sources1 Publication1
Active sitei122Sequence analysis1
Active sitei167NucleophileSequence analysis1

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
  • nicotinamide metabolic process Source: GO_Central
  • nicotinate nucleotide salvage Source: SGD
  • replicative cell aging Source: SGD

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YGL037C-MONOMER
YEAST: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):
Nicotinamide 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002065581 – 216NicotinamidaseAdd BLAST216

Proteomic databases

MaxQBiP53184
PaxDbiP53184
PRIDEiP53184
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

Protein-protein interaction databases

BioGridi33210, 82 interactors
DIPiDIP-2070N
IntActiP53184, 12 interactors
MINTiP53184
STRINGi4932.YGL037C

Chemistry databases

BindingDBiP53184

Structurei

Secondary structure

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi11 – 14Combined sources4
Helixi25 – 28Combined sources4
Helixi29 – 37Combined sources9
Helixi39 – 41Combined sources3
Beta strandi43 – 51Combined sources9
Helixi61 – 63Combined sources3
Beta strandi72 – 76Combined sources5
Beta strandi85 – 89Combined sources5
Helixi100 – 102Combined sources3
Helixi106 – 115Combined sources10
Beta strandi118 – 122Combined sources5
Beta strandi132 – 135Combined sources4
Helixi145 – 151Combined sources7
Beta strandi156 – 162Combined sources7
Helixi164 – 168Combined sources5
Helixi169 – 177Combined sources9
Beta strandi181 – 190Combined sources10
Helixi196 – 208Combined sources13
Beta strandi212 – 214Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53184

Family & Domainsi

Sequence similaritiesi

Belongs to the isochorismatase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000064935
HOGENOMiHOG000078666
InParanoidiP53184
KOiK01440
OMAiTQDWHPP
OrthoDBiEOG092C4BU3

Family and domain databases

Gene3Di3.40.50.850, 1 hit
InterProiView protein in InterPro
IPR000868 Isochorismatase-like
IPR036380 Isochorismatase-like_sf
PfamiView protein in Pfam
PF00857 Isochorismatase, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiPNC1_YEAST
AccessioniPrimary (citable) accession number: P53184
Secondary accession number(s): D6VUA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health