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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: Annotation score: 5 out of 5-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 carrier activity Source: SGD
  • heme binding Source: InterPro
  • iron ion binding Source: GO_Central
  • stearoyl-CoA 9-desaturase activity Source: SGD

GO - Biological processi

  • long-chain fatty acid biosynthetic process Source: GO_Central
  • mitochondrion inheritance Source: SGD
  • unsaturated fatty acid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Keywords - Ligandi

Heme, 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

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

GO - Cellular componenti

  • integral component of endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

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.
PRIDEiP21147.

Interactioni

Protein-protein interaction databases

BioGridi33192. 103 interactors.
DIPiDIP-5026N.
IntActiP21147. 40 interactors.
MINTiMINT-563591.

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

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

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.
InterProiIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR015876. Acyl-CoA_DS.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF000345. OLE1. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP21147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33192. 103 interactors.
DIPiDIP-5026N.
IntActiP21147. 40 interactors.
MINTiMINT-563591.

Chemistry databases

SwissLipidsiSLP:000000512.
SLP:000000875.

Proteomic databases

MaxQBiP21147.
PRIDEiP21147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL055W; YGL055W; YGL055W.
GeneIDi852825.
KEGGisce:YGL055W.

Organism-specific databases

EuPathDBiFungiDB:YGL055W.
SGDiS000003023. OLE1.

Phylogenomic databases

GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270353.
InParanoidiP21147.
KOiK00507.
OMAiFNGGVYF.
OrthoDBiEOG092C2CE8.

Enzyme and pathway databases

BioCyciMetaCyc:YGL055W-MONOMER.
YEAST:YGL055W-MONOMER.
ReactomeiR-SCE-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiP21147.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
Gene3Di3.10.120.10. 1 hit.
InterProiIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR015876. Acyl-CoA_DS.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF000345. OLE1. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACO1_YEAST
AccessioniPrimary (citable) accession number: P21147
Secondary accession number(s): D6VU86, E9P911
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.