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Protein

NADH pyrophosphatase

Gene

NPY1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

NAD(H) + H2O = AMP + NMN(H).

Cofactori

Mg2+, Mn2+Note: Divalent metal cations. Mg2+ or Mn2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi272 – 2721Divalent metal cationBy similarity
Metal bindingi276 – 2761Divalent metal cationBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • NAD+ diphosphatase activity Source: SGD

GO - Biological processi

  • NADH metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

BioCyciYEAST:YGL067W-MONOMER.
BRENDAi3.6.1.22. 984.
ReactomeiR-SCE-197264. Nicotinamide salvaging.
R-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH pyrophosphatase (EC:3.6.1.22)
Gene namesi
Name:NPY1
Ordered Locus Names:YGL067W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL067W.
SGDiS000003035. NPY1.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384NADH pyrophosphatasePRO_0000056961Add
BLAST

Proteomic databases

MaxQBiP53164.
PeptideAtlasiP53164.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi33180. 28 interactions.
IntActiP53164. 1 interaction.
MINTiMINT-2781196.

Structurei

3D structure databases

ProteinModelPortaliP53164.
SMRiP53164. Positions 162-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 351133Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi257 – 27822Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family. NudC subfamily.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063600.
HOGENOMiHOG000247937.
InParanoidiP53164.
KOiK03426.
OMAiTIAGFME.
OrthoDBiEOG7K3TW2.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR015376. Znr_NADH_PPase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
PF09297. zf-NADH-PPase. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTAVTFFGQ HVLNRVSFLR CSKEFIKKSL NHDSTVFIPF IEGEALISPE
60 70 80 90 100
NGDLVQLSNS VKSYKNILSA IVPLYTTLLN TTRSRSDESG INVTFLGLLE
110 120 130 140 150
GTDSAFNFEW SNISYKGTPY FGLDIRVTES TLFKKVDFEP IFSYPKVTRD
160 170 180 190 200
HIFKQTNEDA SLYSQGKMYL DWLAKYKFCP GCGSPLFPVE AGTKLQCSNE
210 220 230 240 250
NRNVYCNVRD ARINNVCFPR TDPTVIIALT NSDYSKCCLA RSKKRYGDFV
260 270 280 290 300
LYSTIAGFME PSETIEEACI REIWEETGIS CKNIDIVRSQ PWPYPCSLMI
310 320 330 340 350
GCLGIVQFNS KNEVINLNHD DELLDAQWFD TTEIIQALDK YAGGYRVPFK
360 370 380
NDINLPGSTT IAFQLINHVC ENYKNLRKTS SSHL
Length:384
Mass (Da):43,516
Last modified:October 1, 1996 - v1
Checksum:i96D6768CE2BC8F0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441E → D in AAT93207 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72589 Genomic DNA. Translation: CAA96771.1.
AY693188 Genomic DNA. Translation: AAT93207.1.
BK006941 Genomic DNA. Translation: DAA08035.1.
PIRiS64074.
RefSeqiNP_011448.3. NM_001180932.3.

Genome annotation databases

EnsemblFungiiYGL067W; YGL067W; YGL067W.
GeneIDi852813.
KEGGisce:YGL067W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72589 Genomic DNA. Translation: CAA96771.1.
AY693188 Genomic DNA. Translation: AAT93207.1.
BK006941 Genomic DNA. Translation: DAA08035.1.
PIRiS64074.
RefSeqiNP_011448.3. NM_001180932.3.

3D structure databases

ProteinModelPortaliP53164.
SMRiP53164. Positions 162-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33180. 28 interactions.
IntActiP53164. 1 interaction.
MINTiMINT-2781196.

Proteomic databases

MaxQBiP53164.
PeptideAtlasiP53164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL067W; YGL067W; YGL067W.
GeneIDi852813.
KEGGisce:YGL067W.

Organism-specific databases

EuPathDBiFungiDB:YGL067W.
SGDiS000003035. NPY1.

Phylogenomic databases

GeneTreeiENSGT00530000063600.
HOGENOMiHOG000247937.
InParanoidiP53164.
KOiK03426.
OMAiTIAGFME.
OrthoDBiEOG7K3TW2.

Enzyme and pathway databases

BioCyciYEAST:YGL067W-MONOMER.
BRENDAi3.6.1.22. 984.
ReactomeiR-SCE-197264. Nicotinamide salvaging.
R-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

PROiP53164.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR015376. Znr_NADH_PPase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
PF09297. zf-NADH-PPase. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
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. "Cloning and characterization of the NADH pyrophosphatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a Nudix hydrolase subfamily."
    Xu W., Dunn C.A., Bessman M.J.
    Biochem. Biophys. Res. Commun. 273:753-758(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNPY1_YEAST
AccessioniPrimary (citable) accession number: P53164
Secondary accession number(s): D6VU74, E9P928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 846 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.