P40471 · AYR1_YEAST
- ProteinNADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- GeneAYR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids297 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- a 1-acylglycerone 3-phosphate + H+ + NADPH = a 1-acyl-sn-glycero-3-phosphate + NADP+This reaction proceeds in the forward direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+This reaction proceeds in the forward direction.
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 μM | NADPH | |||||
15 μM | hexadecyl dihydroxyacetone-phosphate | |||||
3.5 mM | p-nitrophenylacetate | |||||
1.52 mM | p-nitrophenylbutyrate | |||||
61.21 μM | 1,2,3-tri-(9Z-octadecenoyl)-glycerol |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3.8 nmol/min/mg | for hexadecyl dihydroxyacetone-phosphate | ||||
18.5 μmol/min/mg | for p-nitrophenylacetate | ||||
14.06 μmol/min/mg | for p-nitrophenylbutyrate | ||||
10.93 pmol/h/mg | for 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 18 | Nucleophile; for lipase activity | ||||
Sequence: S | ||||||
Binding site | 21 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 64 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 126 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 157 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 157 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 161 | Lowers pKa of active site Tyr | ||||
Sequence: K | ||||||
Binding site | 161 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 190 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 192 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | lipid droplet | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Molecular Function | 1-acyl dihydroxyacetone phosphate reductase activity | |
Molecular Function | acylglycerone-phosphate reductase activity | |
Molecular Function | triglyceride lipase activity | |
Biological Process | phosphatidic acid biosynthetic process | |
Biological Process | triglyceride catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- EC number
- Short namesADR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40471
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 18 | Completely abolishes lipase activity. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054520 | 1-297 | NADPH-dependent 1-acyldihydroxyacetone phosphate reductase | |||
Sequence: MSELQSQPKKIAVVTGASGGIGYEVTKELARNGYLVYACARRLEPMAQLAIQFGNDSIKPYKLDISKPEEIVTFSGFLRANLPDGKLDLLYNNAGQSCTFPALDATDAAVEQCFKVNVFGHINMCRELSEFLIKAKGTIVFTGSLAGVVSFPFGSIYSASKAAIHQYARGLHLEMKPFNVRVINAITGGVATDIADKRPLPETSIYNFPEGREAFNSRKTMAKDNKPMPADAYAKQLVKDILSTSDPVDVYRGTFANIMRFVMIFVPYWLLEKGLSKKFKLDKVNNALKSKQKNKDD |
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.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 16-20 | GXSXG | ||||
Sequence: GASGG |
Sequence similarities
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length297
- Mass (Da)32,814
- Last updated1995-02-01 v1
- ChecksumB614C0E0B1FB0CE0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z46833 EMBL· GenBank· DDBJ | CAA86868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08429.1 EMBL· GenBank· DDBJ | Genomic DNA |