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YPR1 trifunctional aldehyde reductase/carbonyl reductase (NADPH)/glucose 1-dehydrogenase (NADP(+)) YPR1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851974, updated on 2-Nov-2024

Summary

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Official Symbol
YPR1
Official Full Name
trifunctional aldehyde reductase/carbonyl reductase (NADPH)/glucose 1-dehydrogenase (NADP(+)) YPR1
Primary source
SGD:S000002776
Locus tag
YDR368W
See related
AllianceGenome:SGD:S000002776; FungiDB:YDR368W; VEuPathDB:YDR368W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables aldose reductase (NADPH) activity; carbonyl reductase (NADPH) activity; and diacetyl reductase ((S)-acetoin forming) (NAD+) activity. Involved in acetoin metabolic process; cellular response to oxidative stress; and pentose catabolic process. Located in cytoplasm and nucleus. Human ortholog(s) of this gene implicated in several diseases, including 46,XY sex reversal 8; congenital bile acid synthesis defect 2; diabetic neuropathy; leukemia (multiple); and type 2 diabetes mellitus. Orthologous to several human genes including AKR1B1 (aldo-keto reductase family 1 member B) and AKR1B10 (aldo-keto reductase family 1 member B10). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See YPR1 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (1213904..1214842)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Mor1p Neighboring gene Kei1p Neighboring gene Xrs2p Neighboring gene Dxo1p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Characterization of Ypr1p from Saccharomyces cerevisiae as a 2-methylbutyraldehyde reductase. Ford G, et al. Yeast, 2002 Sep 15. PMID 12210903
  2. Amino acid sequence and characterization of aldo-keto reductase from bakers' yeast. Nakamura K, et al. Biosci Biotechnol Biochem, 1997 Feb. PMID 9058981
  3. Aldo-keto reductase enzymes detoxify glyphosate and improve herbicide resistance in plants. Vemanna RS, et al. Plant Biotechnol J, 2017 Jul. PMID 27611904, Free PMC Article
  4. Highly stereoselective reagents for beta-keto ester reductions by genetic engineering of baker's yeast. Rodríguez S, et al. J Am Chem Soc, 2001 Feb 28. PMID 11456752
  5. Simultaneous synthesis of 2-phenylethanol and L-homophenylalanine using aromatic transaminase with yeast Ehrlich pathway. Hwang JY, et al. Biotechnol Bioeng, 2009 Apr 1. PMID 19016485

See all (48) citations in PubMed

GeneRIFs: Gene References Into Functions

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables aldose reductase (NADPH) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aldose reductase (NADPH) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aldose reductase (NADPH) activity IEA
Inferred from Electronic Annotation
more info
  
enables carbonyl reductase (NADPH) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables diacetyl reductase ((S)-acetoin forming) (NAD+) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in D-xylose catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in D-xylose catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in acetoin metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in arabinose catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in arabinose catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in arabinose catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cellular response to oxidative stress IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular response to oxidative stress IGI
Inferred from Genetic Interaction
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm HDA PubMed 
located_in cytoplasm HDA PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in nucleus HDA PubMed 

General protein information

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Preferred Names
trifunctional aldehyde reductase/carbonyl reductase (NADPH)/glucose 1-dehydrogenase (NADP(+)) YPR1
NP_010656.1
  • NADPH-dependent aldo-keto reductase; reduces multiple substrates including 2-methylbutyraldehyde and D,L-glyceraldehyde, expression is induced by osmotic and oxidative stress; functionally redundant with other aldo-keto reductases; protein abundance increases in response to DNA replication stress; YPR1 has a paralog, GCY1, that arose from the whole genome duplication; human homolog AKR1B1 can complement yeast null mutant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001136.10 Reference assembly

    Range
    1213904..1214842
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180676.1 → NP_010656.1  TPA: trifunctional aldehyde reductase/carbonyl reductase (NADPH)/glucose 1-dehydrogenase (NADP(+)) YPR1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010656.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VSZ9, Q12458
    UniProtKB/TrEMBL
    B3LFT5, B5VGP8, C7GMG9, C8Z5S9, G2WBA4, N1PAI7
    Conserved Domains (1) summary
    cd19117
    Location:7 → 296
    AKR_AKR3A1-2; AKR3A family of aldo-keto reductase (AKR)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12458.1

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