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P21147

- ACO1_YEAST

UniProt

P21147 - ACO1_YEAST

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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: 5 out of 5- Experimental evidence at protein leveli

Functioni

Utilizes O2 and electrons from the reduced cytochrome b5 domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates.Curated

Catalytic activityi

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

Cofactori

Iron.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi444 – 4441Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi470 – 4701Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. electron carrier activity Source: SGD
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro
  4. stearoyl-CoA 9-desaturase activity Source: SGD

GO - Biological processi

  1. 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:MONOMER-17617.
YEAST:YGL055W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase 1 (EC:1.14.19.1)
Alternative name(s):
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
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL055w.
SGDiS000003023. OLE1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Acyl-CoA desaturase 1PRO_0000185406Add
BLAST

Proteomic databases

MaxQBiP21147.
PaxDbiP21147.
PeptideAtlasiP21147.

Expressioni

Gene expression databases

GenevestigatoriP21147.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-2098,EBI-2098
AGP1P253761EBI-2098,EBI-2357
CAB3P360761EBI-2098,EBI-26778
CHO1P084561EBI-2098,EBI-14055
EMC2P471331EBI-2098,EBI-25568
ERG11P106141EBI-2098,EBI-5127
ERG5P547811EBI-2098,EBI-6563
ERV25P548371EBI-2098,EBI-6642
GAP1P191451EBI-2098,EBI-7314
GSF2Q046971EBI-2098,EBI-27807
KRE27P405401EBI-2098,EBI-24977
MID2P360271EBI-2098,EBI-10901
OST1P415431EBI-2098,EBI-12651
PGA3Q127461EBI-2098,EBI-27973
PHO84P252971EBI-2098,EBI-13320
PHO88P382641EBI-2098,EBI-13350
PMP2P409751EBI-2098,EBI-2043041
PPZ1P265701EBI-2098,EBI-13807
RTN1Q049471EBI-2098,EBI-38020
SAC1P323681EBI-2098,EBI-16210
SEC63P149061EBI-2098,EBI-16636
SPF1P399861EBI-2098,EBI-3128
TPO4Q122561EBI-2098,EBI-37213
UBP1P250371EBI-2098,EBI-19819
VRG4P401071EBI-2098,EBI-7764
YDR476CQ033621EBI-2098,EBI-2057915
YET1P357231EBI-2098,EBI-26730

Protein-protein interaction databases

BioGridi33192. 104 interactions.
DIPiDIP-5026N.
IntActiP21147. 40 interactions.
MINTiMINT-563591.
STRINGi4932.YGL055W.

Structurei

3D structure databases

ProteinModelPortaliP21147.
SMRiP21147. Positions 407-491.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 112112CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini134 – 1385LumenalSequence Analysis
Topological domaini160 – 25596CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini277 – 2804LumenalSequence Analysis
Topological domaini302 – 510209CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei113 – 13321HelicalSequence AnalysisAdd
BLAST
Transmembranei139 – 15921HelicalSequence AnalysisAdd
BLAST
Transmembranei256 – 27621HelicalSequence AnalysisAdd
BLAST
Transmembranei281 – 30121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini409 – 48779Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi161 – 1666Histidine box-1
Motifi198 – 2025Histidine box-2
Motifi335 – 3395Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1398.
GeneTreeiENSGT00530000063158.
HOGENOMiHOG000270353.
InParanoidiP21147.
KOiK00507.
OMAiFNGGVYF.
OrthoDBiEOG7S2277.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF000345. OLE1. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
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 [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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671D → G in AAT93029. (PubMed:17322287)Curated
Sequence conflicti304 – 3041L → M in AAA34826. (PubMed:1978720)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S64059.
RefSeqi NP_011460.3. NM_001180920.3.

3D structure databases

ProteinModelPortali P21147.
SMRi P21147. Positions 407-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33192. 104 interactions.
DIPi DIP-5026N.
IntActi P21147. 40 interactions.
MINTi MINT-563591.
STRINGi 4932.YGL055W.

Proteomic databases

MaxQBi P21147.
PaxDbi P21147.
PeptideAtlasi P21147.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL055W ; YGL055W ; YGL055W .
GeneIDi 852825.
KEGGi sce:YGL055W.

Organism-specific databases

CYGDi YGL055w.
SGDi S000003023. OLE1.

Phylogenomic databases

eggNOGi COG1398.
GeneTreei ENSGT00530000063158.
HOGENOMi HOG000270353.
InParanoidi P21147.
KOi K00507.
OMAi FNGGVYF.
OrthoDBi EOG7S2277.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17617.
YEAST:YGL055W-MONOMER.

Miscellaneous databases

NextBioi 972381.

Gene expression databases

Genevestigatori P21147.

Family and domain databases

Gene3Di 3.10.120.10. 1 hit.
InterProi IPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view ]
Pfami PF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000345. OLE1. 1 hit.
PRINTSi PR00075. FACDDSATRASE.
SUPFAMi SSF55856. SSF55856. 1 hit.
PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The OLE1 gene of Saccharomyces cerevisiae encodes the delta 9 fatty acid desaturase and can be functionally replaced by the rat stearoyl-CoA desaturase gene."
    Stukey J.E., McDonough V.M., Martin C.E.
    J. Biol. Chem. 265:20144-20149(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

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: October 29, 2014
This is version 146 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

External Data

Dasty 3