P40471 · AYR1_YEAST

Function

function

Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA) (PubMed:10617610, PubMed:1512203).
Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs (PubMed:24187129).
Required for spore germination (PubMed:10617610).
Plays a role in cell wall biogenesis, but this effect may be indirect by affecting the activities of cell wall synthesis enzymes (PubMed:23956635).
Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy (PubMed:26162625).
Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane (PubMed:28916712).

Miscellaneous

Present with 3671 molecules/cell in log phase SD medium.

Catalytic activity

Activity regulation

Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
20 μMNADPH
15 μMhexadecyl dihydroxyacetone-phosphate
3.5 mMp-nitrophenylacetate
1.52 mMp-nitrophenylbutyrate
61.21 μM1,2,3-tri-(9Z-octadecenoyl)-glycerol
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
3.8 nmol/min/mgfor hexadecyl dihydroxyacetone-phosphate
18.5 μmol/min/mgfor p-nitrophenylacetate
14.06 μmol/min/mgfor p-nitrophenylbutyrate
10.93 pmol/h/mgfor 1,2,3-tri-(9Z-octadecenoyl)-glycerol

pH Dependence

Optimum pH is 6.7-7.2.

Temperature Dependence

Optimum temperature is 40 degrees Celsius. Thermostable for 10 minutes up to 45 degrees Celsius.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site18Nucleophile; for lipase activity
Binding site21NADP+ (UniProtKB | ChEBI)
Binding site64NADP+ (UniProtKB | ChEBI)
Binding site93NADP+ (UniProtKB | ChEBI)
Binding site126NADP+ (UniProtKB | ChEBI)
Active site157Proton acceptor
Binding site157NADP+ (UniProtKB | ChEBI)
Active site161Lowers pKa of active site Tyr
Binding site161NADP+ (UniProtKB | ChEBI)
Binding site190NADP+ (UniProtKB | ChEBI)
Binding site192NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum
Cellular Componentlipid droplet
Cellular Componentmitochondrial outer membrane
Cellular Componentmitochondrion
Molecular Function1-acyl dihydroxyacetone phosphate reductase activity
Molecular Functionacylglycerone-phosphate reductase activity
Molecular Functiontriglyceride lipase activity
Biological Processphosphatidic acid biosynthetic process
Biological Processtriglyceride catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 1.A.115.1.1the pore-forming nadph-dependent 1-acyldihydroxyacetone phosphate reductase (ayr1) family

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
  • EC number
  • Short names
    ADR
  • Alternative names
    • 1-acyl DHAP reductase
    • Acyl/alkyl DHAP reductase
    • Acylglycerone-phosphate reductase
    • Triacylglycerol lipase AYR1
      (TAG lipase) (EC:3.1.1.3
      ) . EC:3.1.1.3 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      AYR1
    • Synonyms
      GBG1
    • Ordered locus names
      YIL124W

Organism names

Accessions

  • Primary accession
    P40471
  • Secondary accessions
    • D6VVG3

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Reduces the activities of beta-1,3-glucan synthase and chitin synthase III, while increasing chitin synthase I and II activities. Shows altered cell wall composition as well as susceptibility towards cell wall inhibitors such as zymolyase, calcofluor white, and nikkomycin Z.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis18Completely abolishes lipase activity.

Variants

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The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000545201-297NADPH-dependent 1-acyldihydroxyacetone phosphate reductase

Proteomic databases

PTM databases

Expression

Induction

Expressed during vegetative growth with a maximum level of transcription at G1 phase, after which it is decreased during the remainder of the cell cycle.

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif16-20GXSXG

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    297
  • Mass (Da)
    32,814
  • Last updated
    1995-02-01 v1
  • Checksum
    B614C0E0B1FB0CE0
MSELQSQPKKIAVVTGASGGIGYEVTKELARNGYLVYACARRLEPMAQLAIQFGNDSIKPYKLDISKPEEIVTFSGFLRANLPDGKLDLLYNNAGQSCTFPALDATDAAVEQCFKVNVFGHINMCRELSEFLIKAKGTIVFTGSLAGVVSFPFGSIYSASKAAIHQYARGLHLEMKPFNVRVINAITGGVATDIADKRPLPETSIYNFPEGREAFNSRKTMAKDNKPMPADAYAKQLVKDILSTSDPVDVYRGTFANIMRFVMIFVPYWLLEKGLSKKFKLDKVNNALKSKQKNKDD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z46833
EMBL· GenBank· DDBJ
CAA86868.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006942
EMBL· GenBank· DDBJ
DAA08429.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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