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Protein

NADPH-dependent 1-acyldihydroxyacetone phosphate reductase

Gene

AYR1

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

Functioni

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). Required for spore germination.1 Publication

Catalytic activityi

1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH.

Enzyme regulationi

Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions.1 Publication

Kineticsi

  1. KM=20 µM for NADPH1 Publication
  2. KM=15 µM for hexadecyl dihydroxyacetone-phosphate1 Publication
  1. Vmax=3.8 nmol/min/mg enzyme for hexadecyl dihydroxyacetone-phosphate1 Publication

pH dependencei

Optimum pH is 6.7-7.2.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Thermostable for 10 min up to 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441SubstrateBy similarity
Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 3725NAD or NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • acylglycerone-phosphate reductase activity Source: SGD
  • triglyceride lipase activity Source: SGD

GO - Biological processi

  • phosphatidic acid biosynthetic process Source: SGD
  • triglyceride catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:YIL124W-MONOMER.
YEAST:YIL124W-MONOMER.
SABIO-RKP40471.

Chemistry

SwissLipidsiSLP:000000056.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH-dependent 1-acyldihydroxyacetone phosphate reductase (EC:1.1.1.101)
Short name:
ADR
Alternative name(s):
1-acyl DHAP reductase
Acyl/alkyl DHAP reductase
Acylglycerone-phosphate reductase
Gene namesi
Name:AYR1
Ordered Locus Names:YIL124W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL124W.
SGDiS000001386. AYR1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297NADPH-dependent 1-acyldihydroxyacetone phosphate reductasePRO_0000054520Add
BLAST

Proteomic databases

MaxQBiP40471.

PTM databases

iPTMnetiP40471.

Interactioni

Protein-protein interaction databases

BioGridi34867. 74 interactions.
DIPiDIP-4614N.
IntActiP40471. 9 interactions.
MINTiMINT-489020.

Structurei

3D structure databases

ProteinModelPortaliP40471.
SMRiP40471. Positions 12-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP40471.
KOiK06123.
OMAiFANIMRF.
OrthoDBiEOG78M0C3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40471-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELQSQPKK IAVVTGASGG IGYEVTKELA RNGYLVYACA RRLEPMAQLA
60 70 80 90 100
IQFGNDSIKP YKLDISKPEE IVTFSGFLRA NLPDGKLDLL YNNAGQSCTF
110 120 130 140 150
PALDATDAAV EQCFKVNVFG HINMCRELSE FLIKAKGTIV FTGSLAGVVS
160 170 180 190 200
FPFGSIYSAS KAAIHQYARG LHLEMKPFNV RVINAITGGV ATDIADKRPL
210 220 230 240 250
PETSIYNFPE GREAFNSRKT MAKDNKPMPA DAYAKQLVKD ILSTSDPVDV
260 270 280 290
YRGTFANIMR FVMIFVPYWL LEKGLSKKFK LDKVNNALKS KQKNKDD
Length:297
Mass (Da):32,814
Last modified:February 1, 1995 - v1
Checksum:iB614C0E0B1FB0CE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46833 Genomic DNA. Translation: CAA86868.1.
BK006942 Genomic DNA. Translation: DAA08429.1.
PIRiS49885.
RefSeqiNP_012142.3. NM_001179472.3.

Genome annotation databases

EnsemblFungiiYIL124W; YIL124W; YIL124W.
GeneIDi854682.
KEGGisce:YIL124W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46833 Genomic DNA. Translation: CAA86868.1.
BK006942 Genomic DNA. Translation: DAA08429.1.
PIRiS49885.
RefSeqiNP_012142.3. NM_001179472.3.

3D structure databases

ProteinModelPortaliP40471.
SMRiP40471. Positions 12-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34867. 74 interactions.
DIPiDIP-4614N.
IntActiP40471. 9 interactions.
MINTiMINT-489020.

Chemistry

SwissLipidsiSLP:000000056.

PTM databases

iPTMnetiP40471.

Proteomic databases

MaxQBiP40471.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL124W; YIL124W; YIL124W.
GeneIDi854682.
KEGGisce:YIL124W.

Organism-specific databases

EuPathDBiFungiDB:YIL124W.
SGDiS000001386. AYR1.

Phylogenomic databases

InParanoidiP40471.
KOiK06123.
OMAiFANIMRF.
OrthoDBiEOG78M0C3.

Enzyme and pathway databases

BioCyciMetaCyc:YIL124W-MONOMER.
YEAST:YIL124W-MONOMER.
SABIO-RKP40471.

Miscellaneous databases

PROiP40471.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 32-41; 63-79; 127-134; 224-235; 240-252 AND 261-273, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "The acyl dihydroxyacetone phosphate pathway enzymes for glycerolipid biosynthesis are present in the yeast Saccharomyces cerevisiae."
    Racenis P.V., Lai J.L., Das A.K., Mullick P.C., Hajra A.K., Greenberg M.L.
    J. Bacteriol. 174:5702-5710(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  5. "Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae."
    Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.
    J. Bacteriol. 181:6441-6448(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  6. "1-acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles."
    Athenstaedt K., Daum G.
    J. Biol. Chem. 275:235-240(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAYR1_YEAST
AccessioniPrimary (citable) accession number: P40471
Secondary accession number(s): D6VVG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 142 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 3671 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: 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.