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Protein

Acyl-CoA desaturase 1

Gene

OLE1

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

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:1978720, PubMed:7947684). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:1978720). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:1978720, PubMed:7947684, PubMed:16443825).3 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.3 Publications

Cofactori

Fe2+By similarityNote: Expected to bind 2 Fe2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi161Iron 1By similarity1
Metal bindingi166Iron 1By similarity1
Metal bindingi198Iron 1By similarity1
Metal bindingi201Iron 2By similarity1
Metal bindingi202Iron 1By similarity1
Metal bindingi306Iron 2By similarity1
Metal bindingi335Iron 2By similarity1
Metal bindingi338Iron 1By similarity1
Metal bindingi339Iron 2By similarity1
Metal bindingi444Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi470Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

  • electron transfer activity Source: SGD
  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • stearoyl-CoA 9-desaturase activity Source: SGD

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YGL055W-MONOMER
YEAST:YGL055W-MONOMER
ReactomeiR-SCE-75105 Fatty acyl-CoA biosynthesis

Chemistry databases

SwissLipidsiSLP:000000512
SLP:000000875

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 1 (EC:1.14.19.12 Publications)
Alternative name(s):
Delta 9 fatty acid desaturase1 Publication
Fatty acid desaturase 1
Stearoyl-CoA desaturase 1
Gene namesi
Name:OLE1
Ordered Locus Names:YGL055W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL055W
SGDiS000003023 OLE1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 112CytoplasmicSequence analysisAdd BLAST112
Transmembranei113 – 133HelicalSequence analysisAdd BLAST21
Topological domaini134 – 138LumenalSequence analysis5
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21
Topological domaini160 – 255CytoplasmicSequence analysisAdd BLAST96
Transmembranei256 – 276HelicalSequence analysisAdd BLAST21
Topological domaini277 – 280LumenalSequence analysis4
Transmembranei281 – 301HelicalSequence analysisAdd BLAST21
Topological domaini302 – 510CytoplasmicSequence analysisAdd BLAST209

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854061 – 510Acyl-CoA desaturase 1Add BLAST510

Proteomic databases

MaxQBiP21147
PaxDbiP21147
PRIDEiP21147

Interactioni

Protein-protein interaction databases

BioGridi33192, 196 interactors
DIPiDIP-5026N
IntActiP21147, 41 interactors
MINTiP21147
STRINGi4932.YGL055W

Structurei

3D structure databases

ProteinModelPortaliP21147
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini409 – 487Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST79

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi161 – 166Histidine box-1Curated6
Motifi198 – 202Histidine box-2Curated5
Motifi335 – 339Histidine box-3Curated5

Domaini

The histidine box domains are involved in binding the catalytic metal ions.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063158
HOGENOMiHOG000270353
InParanoidiP21147
KOiK00507
OMAiFNGGVYF
OrthoDBiEOG092C2CE8

Family and domain databases

CDDicd03505 Delta9-FADS-like, 1 hit
Gene3Di3.10.120.10, 1 hit
InterProiView protein in InterPro
IPR009160 Acyl-CoA_deSatase_haem/ster-bd
IPR015876 Acyl-CoA_DS
IPR001199 Cyt_B5-like_heme/steroid-bd
IPR036400 Cyt_B5-like_heme/steroid_sf
IPR018506 Cyt_B5_heme-BS
IPR005804 FA_desaturase_dom
IPR001522 FADS-1_CS
PANTHERiPTHR11351 PTHR11351, 1 hit
PfamiView protein in Pfam
PF00173 Cyt-b5, 1 hit
PF00487 FA_desaturase, 1 hit
PIRSFiPIRSF000345 OLE1, 1 hit
PRINTSiPR00075 FACDDSATRASE
SMARTiView protein in SMART
SM01117 Cyt-b5, 1 hit
SUPFAMiSSF55856 SSF55856, 1 hit
PROSITEiView protein in PROSITE
PS00191 CYTOCHROME_B5_1, 1 hit
PS50255 CYTOCHROME_B5_2, 1 hit
PS00476 FATTY_ACID_DESATUR_1, 1 hit

Sequencei

Sequence statusi: Complete.

P21147-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPTSGTTIEL IDDQFPKDDS ASSGIVDEVD LTEANILATG LNKKAPRIVN
60 70 80 90 100
GFGSLMGSKE MVSVEFDKKG NEKKSNLDRL LEKDNQEKEE AKTKIHISEQ
110 120 130 140 150
PWTLNNWHQH LNWLNMVLVC GMPMIGWYFA LSGKVPLHLN VFLFSVFYYA
160 170 180 190 200
VGGVSITAGY HRLWSHRSYS AHWPLRLFYA IFGCASVEGS AKWWGHSHRI
210 220 230 240 250
HHRYTDTLRD PYDARRGLWY SHMGWMLLKP NPKYKARADI TDMTDDWTIR
260 270 280 290 300
FQHRHYILLM LLTAFVIPTL ICGYFFNDYM GGLIYAGFIR VFVIQQATFC
310 320 330 340 350
INSLAHYIGT QPFDDRRTPR DNWITAIVTF GEGYHNFHHE FPTDYRNAIK
360 370 380 390 400
WYQYDPTKVI IYLTSLVGLA YDLKKFSQNA IEEALIQQEQ KKINKKKAKI
410 420 430 440 450
NWGPVLTDLP MWDKQTFLAK SKENKGLVII SGIVHDVSGY ISEHPGGETL
460 470 480 490 500
IKTALGKDAT KAFSGGVYRH SNAAQNVLAD MRVAVIKESK NSAIRMASKR
510
GEIYETGKFF
Length:510
Mass (Da):58,403
Last modified:October 1, 1996 - v2
Checksum:iA6CC78DD4210ECCA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti67D → G in AAT93029 (PubMed:17322287).Curated1
Sequence conflicti304L → M in AAA34826 (PubMed:1978720).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05676 Genomic DNA Translation: AAA34826.1
Z72577 Genomic DNA Translation: CAA96757.1
AY693010 Genomic DNA Translation: AAT93029.1
BK006941 Genomic DNA Translation: DAA08047.1
PIRiS64059
RefSeqiNP_011460.3, NM_001180920.3

Genome annotation databases

EnsemblFungiiYGL055W; YGL055W; YGL055W
GeneIDi852825
KEGGisce:YGL055W

Similar proteinsi

Entry informationi

Entry nameiACO1_YEAST
AccessioniPrimary (citable) accession number: P21147
Secondary accession number(s): D6VU86, E9P911
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1996
Last modified: September 12, 2018
This is version 179 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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