ACO1_YEAST
ID ACO1_YEAST Reviewed; 510 AA.
AC P21147; D6VU86; E9P911;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Acyl-CoA desaturase 1;
DE EC=1.14.19.1 {ECO:0000269|PubMed:1978720, ECO:0000269|PubMed:7947684};
DE AltName: Full=Delta 9 fatty acid desaturase {ECO:0000303|PubMed:1978720};
DE AltName: Full=Fatty acid desaturase 1;
DE AltName: Full=Stearoyl-CoA desaturase 1;
GN Name=OLE1; OrderedLocusNames=YGL055W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1978720; DOI=10.1016/s0021-9258(17)30481-7;
RA Stukey J.E., McDonough V.M., Martin C.E.;
RT "The OLE1 gene of Saccharomyces cerevisiae encodes the delta 9 fatty acid
RT desaturase and can be functionally replaced by the rat stearoyl-CoA
RT desaturase gene.";
RL J. Biol. Chem. 265:20144-20149(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2674136; DOI=10.1016/s0021-9258(19)84740-3;
RA Stukey J.E., McDonough V.M., Martin C.E.;
RT "Isolation and characterization of OLE1, a gene affecting fatty acid
RT desaturation from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 264:16537-16544(1989).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7947684; DOI=10.1021/bi00209a009;
RA Shanklin J., Whittle E., Fox B.G.;
RT "Eight histidine residues are catalytically essential in a membrane-
RT associated iron enzyme, stearoyl-CoA desaturase, and are conserved in
RT alkane hydroxylase and xylene monooxygenase.";
RL Biochemistry 33:12787-12794(1994).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16443825; DOI=10.1194/jlr.c500025-jlr200;
RA Miyazaki M., Bruggink S.M., Ntambi J.M.;
RT "Identification of mouse palmitoyl-coenzyme A Delta9-desaturase.";
RL J. Lipid Res. 47:700-704(2006).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [10]
RP FUNCTION.
RX PubMed=22323296; DOI=10.1091/mbc.e11-07-0624;
RA De Smet C.H., Vittone E., Scherer M., Houweling M., Liebisch G.,
RA Brouwers J.F., de Kroon A.I.;
RT "The yeast acyltransferase Sct1p regulates fatty acid desaturation by
RT competing with the desaturase Ole1p.";
RL Mol. Biol. Cell 23:1146-1156(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates (PubMed:1978720, PubMed:7947684). Catalyzes
CC the insertion of a cis double bond at the delta-9 position into fatty
CC acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA
CC (PubMed:1978720, PubMed:2674136). Required for the biosynthesis of
CC membrane phospholipids, cholesterol esters and triglycerides
CC (PubMed:1978720, PubMed:7947684, PubMed:16443825). Regulates fatty acid
CC desaturation, that is, the ratio of unsaturated versus saturated fatty
CC acyl chains, by competing with the acyltransferase STC1 for the common
CC substrate C16:0-CoA. SCT1 sequesters C16:0-CoA into lipids, thereby
CC shielding it from desaturation by OLE1 (PubMed:22323296).
CC {ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:1978720,
CC ECO:0000269|PubMed:22323296, ECO:0000269|PubMed:2674136,
CC ECO:0000269|PubMed:7947684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:16443825, ECO:0000269|PubMed:1978720,
CC ECO:0000269|PubMed:2674136, ECO:0000269|PubMed:7947684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
CC Evidence={ECO:0000305|PubMed:2674136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:2674136};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000305|PubMed:2674136};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26928762}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; J05676; AAA34826.1; -; Genomic_DNA.
DR EMBL; Z72577; CAA96757.1; -; Genomic_DNA.
DR EMBL; AY693010; AAT93029.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08047.1; -; Genomic_DNA.
DR PIR; S64059; S64059.
DR RefSeq; NP_011460.3; NM_001180920.3.
DR AlphaFoldDB; P21147; -.
DR SMR; P21147; -.
DR BioGRID; 33192; 206.
DR DIP; DIP-5026N; -.
DR IntAct; P21147; 41.
DR MINT; P21147; -.
DR STRING; 4932.YGL055W; -.
DR SwissLipids; SLP:000000512; -.
DR SwissLipids; SLP:000000875; -.
DR iPTMnet; P21147; -.
DR MaxQB; P21147; -.
DR PaxDb; P21147; -.
DR PRIDE; P21147; -.
DR EnsemblFungi; YGL055W_mRNA; YGL055W; YGL055W.
DR GeneID; 852825; -.
DR KEGG; sce:YGL055W; -.
DR SGD; S000003023; OLE1.
DR VEuPathDB; FungiDB:YGL055W; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000176523; -.
DR HOGENOM; CLU_027359_3_2_1; -.
DR InParanoid; P21147; -.
DR OMA; WAHKSYN; -.
DR BioCyc; MetaCyc:YGL055W-MON; -.
DR BioCyc; YEAST:YGL055W-MON; -.
DR PRO; PR:P21147; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P21147; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IGI:SGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR GO; GO:0045471; P:response to ethanol; IDA:SGD.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:SGD.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF000345; OLE1; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Acyl-CoA desaturase 1"
FT /id="PRO_0000185406"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..138
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..280
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT DOMAIN 409..487
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 161..166
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 198..202
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 335..339
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 339
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 444
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 470
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT CONFLICT 67
FT /note="D -> G (in Ref. 5; AAT93029)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="L -> M (in Ref. 1; AAA34826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 58403 MW; A6CC78DD4210ECCA CRC64;
MPTSGTTIEL IDDQFPKDDS ASSGIVDEVD LTEANILATG LNKKAPRIVN GFGSLMGSKE
MVSVEFDKKG NEKKSNLDRL LEKDNQEKEE AKTKIHISEQ PWTLNNWHQH LNWLNMVLVC
GMPMIGWYFA LSGKVPLHLN VFLFSVFYYA VGGVSITAGY HRLWSHRSYS AHWPLRLFYA
IFGCASVEGS AKWWGHSHRI HHRYTDTLRD PYDARRGLWY SHMGWMLLKP NPKYKARADI
TDMTDDWTIR FQHRHYILLM LLTAFVIPTL ICGYFFNDYM GGLIYAGFIR VFVIQQATFC
INSLAHYIGT QPFDDRRTPR DNWITAIVTF GEGYHNFHHE FPTDYRNAIK WYQYDPTKVI
IYLTSLVGLA YDLKKFSQNA IEEALIQQEQ KKINKKKAKI NWGPVLTDLP MWDKQTFLAK
SKENKGLVII SGIVHDVSGY ISEHPGGETL IKTALGKDAT KAFSGGVYRH SNAAQNVLAD
MRVAVIKESK NSAIRMASKR GEIYETGKFF
