P40471 (AYR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
Short name=ADR
EC=1.1.1.101

Alternative name(s):
1-acyl DHAP reductase
Acyl/alkyl DHAP reductase
Acylglycerone-phosphate reductase

Gene names

Name:	AYR1
Ordered Locus Names:	YIL124W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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). Required for spore germination. Ref.6
Catalytic activity	1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH.
Enzyme regulation	Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions. Ref.4
Subcellular location	Lipid droplet. Endoplasmic reticulum Ref.5 Ref.6 Ref.7.
Miscellaneous	Present with 3671 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Biophysicochemical properties	Kinetic parameters: KM=20 µM for NADPH Ref.4 KM=15 µM for hexadecyl dihydroxyacetone-phosphate Vmax=3.8 nmol/min/mg enzyme for hexadecyl dihydroxyacetone-phosphate pH dependence: Optimum pH is 6.7-7.2. Temperature dependence: Optimum temperature is 40 degrees Celsius. Thermostable for 10 min up to 45 degrees Celsius.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Lipid droplet
Ligand	NAD NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidic acid biosynthetic process Inferred from mutant phenotype Ref.6. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.6. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD lipid particle Inferred from direct assay Ref.6. Source: SGD mitochondrial outer membrane Inferred from direct assay PubMed 16407407. Source: SGD
Molecular_function	acylglycerone-phosphate reductase activity Inferred from mutant phenotype Ref.6. Source: SGD nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 297	297	NADPH-dependent 1-acyldihydroxyacetone phosphate reductase		PRO_0000054520
Regions
	Nucleotide binding	13 – 37	25	NAD or NADP By similarity
Sites
	Active site	157	1	Proton acceptor By similarity
	Binding site	144	1	Substrate By similarity
Amino acid modifications
	Modified residue	243	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P40471 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: B614C0E0B1FB0CE0	FASTA	297	32,814
	10 20 30 40 50 60 MSELQSQPKK IAVVTGASGG IGYEVTKELA RNGYLVYACA RRLEPMAQLA IQFGNDSIKP 70 80 90 100 110 120 YKLDISKPEE IVTFSGFLRA NLPDGKLDLL YNNAGQSCTF PALDATDAAV EQCFKVNVFG 130 140 150 160 170 180 HINMCRELSE FLIKAKGTIV FTGSLAGVVS FPFGSIYSAS KAAIHQYARG LHLEMKPFNV 190 200 210 220 230 240 RVINAITGGV ATDIADKRPL PETSIYNFPE GREAFNSRKT MAKDNKPMPA DAYAKQLVKD 250 260 270 280 290 ILSTSDPVDV YRGTFANIMR FVMIFVPYWL LEKGLSKKFK LDKVNNALKS KQKNKDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46833 Genomic DNA. Translation: CAA86868.1. BK006942 Genomic DNA. Translation: DAA08429.1.
PIR	S49885.
RefSeq	NP_012142.3. NM_001179472.3.
3D structure databases
ProteinModelPortal	P40471.
SMR	P40471. Positions 9-238.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4614N.
IntAct	P40471. 11 interactions.
MINT	MINT-489020.
STRING	4932.YIL124W.
Proteomic databases
PaxDb	P40471.
PeptideAtlas	P40471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL124W; YIL124W; YIL124W.
GeneID	854682.
KEGG	sce:YIL119C. sce:YIL124W.
Organism-specific databases
CYGD	YIL124w.
SGD	S000001386. AYR1.
Phylogenomic databases
eggNOG	COG1028.
KO	K06123.
OMA	IANEARQ.
OrthoDB	EOG483HDK.
Enzyme and pathway databases
SABIO-RK	P40471.
Gene expression databases
ArrayExpress	P40471.
Genevestigator	P40471.
GermOnline	YIL124W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PIRSF	PIRSF000126. 11-beta-HSD1. 1 hit.
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977292.

Entry information

Entry name

AYR1_YEAST

Accession

Primary (citable) accession number: P40471
Secondary accession number(s): D6VVG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program