OLE1

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. Has high specificity and catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides.1 Publication

Catalytic activityⁱ

Stearoyl-CoA + 2 ferrocytochrome b5 + O₂ + 2 H⁺ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H₂O.1 Publication

Cofactorⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	101	Iron 1By similarity	1
Metal bindingⁱ	106	Iron 1By similarity	1
Metal bindingⁱ	138	Iron 1By similarity	1
Metal bindingⁱ	141	Iron 2By similarity	1
Metal bindingⁱ	142	Iron 1By similarity	1
Metal bindingⁱ	246	Iron 2By similarity	1
Metal bindingⁱ	275	Iron 2By similarity	1
Metal bindingⁱ	278	Iron 1By similarity	1
Metal bindingⁱ	279	Iron 2By similarity	1
Metal bindingⁱ	384	Iron (heme axial ligand)PROSITE-ProRule annotation	1
Metal bindingⁱ	410	Iron (heme axial ligand)PROSITE-ProRule annotation	1

GO - Molecular functionⁱ

heme binding Source: InterPro
metal ion binding Source: UniProtKB-KW
stearoyl-CoA 9-desaturase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

unsaturated fatty acid biosynthetic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-17616

BioCycⁱ

MetaCyc:MONOMER-17616

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acyl-CoA desaturase (EC:1.14.19.11 Publication) Alternative name(s): Delta(9)-desaturaseCurated Short name: Delta-9 desaturaseCurated Fatty acid desaturaseCurated Stearoyl-CoA desaturaseCurated
Gene namesⁱ	Name:OLE11 Publication
Organismⁱ	Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifierⁱ	5037 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Histoplasma

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 54	CytoplasmicCuratedAdd BLAST	54
Transmembraneⁱ	55 – 75	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	76 – 80	LumenalCurated	5
Transmembraneⁱ	81 – 101	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	102 – 110	CytoplasmicCurated	9
Transmembraneⁱ	111 – 131	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	132 – 199	LumenalCuratedAdd BLAST	68
Transmembraneⁱ	200 – 220	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	221 – 476	CytoplasmicCuratedAdd BLAST	256

Keywords - Cellular componentⁱ

Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000185404	1 – 476	Acyl-CoA desaturaseAdd BLAST		476

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q12618
SMRⁱ	Q12618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	349 – 427	Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST		79

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	101 – 106	Histidine box-1Curated	6
Motifⁱ	138 – 142	Histidine box-2Curated	5
Motifⁱ	275 – 279	Histidine box-3Curated	5

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the fatty acid desaturase type 1 family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03505 Delta9-FADS-like, 1 hit
Gene3Dⁱ	3.10.120.10, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR11351 PTHR11351, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00173 Cyt-b5, 1 hit PF00487 FA_desaturase, 1 hit
PIRSFⁱ	PIRSF000345 OLE1, 1 hit
PRINTSⁱ	PR00075 FACDDSATRASE
SMARTⁱ	View protein in SMART SM01117 Cyt-b5, 1 hit
SUPFAMⁱ	SSF55856 SSF55856, 1 hit
PROSITEⁱ	View 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.

Q12618-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MALNEAPTAS PVAETAAGGK DVVTDAARRP NSEPKKVHIT DTPITLANWH 
        60         70         80         90        100
KHISWLNVTL IIAIPIYGLV QAYWVPLHLK TALWAVVYYF MTGLGITAGY 
       110        120        130        140        150
HRLWAHCSYS ATLPLKIYLA AVGGGAVEGS IRWWARGHRA HHRYTDTDKD 
       160        170        180        190        200
PYSVRKGLLY SHIGWMVMKQ NPKRIGRTEI TDLNEDPVVV WQHRNYLKVV 
       210        220        230        240        250
IFMGIVFPML VSGLGWGDWF GGFIYAGILR IFFVQQATFC VNSLAHWLGD 
       260        270        280        290        300
QPFDDRNSPR DHIVTALVTL GEGYHNFHHE FPSDYRNAIE WHQYDPTKWT 
       310        320        330        340        350
IWIWKQLGLA YDLKQFRANE IEKGRVQQLQ KKIDQRRAKL DWGIPLEQLP 
       360        370        380        390        400
VIEWDDYVDQ AKNGRGLIAI AGVVHDVTDF IKDHPGGKAM INSGIGKDAT 
       410        420        430        440        450
AMFNGGVYNH SNAAHNQLST MRVGVIRGGC EVEIWKRAQK ENKEVESVRD 
       460        470 
EYGNRIVRAG AQVTKIPEPI TTADAA

Length:476

Mass (Da):53,791

Last modified:November 1, 1996 - v1

Checksum:ⁱA91A9CE2A865CADB

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X85963 Genomic DNA Translation: CAA59939.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

X85963 Genomic DNA Translation: CAA59939.1

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q12618	Ole (Fragment)		AJECA		102	UniRef100_Q12618
Delta-9 fatty acid desaturase (Fragment)		AJECA		116

Protein	Similar proteins		Species	Score	Length	Source
Q12618	Ole (Fragment)		AJECA		102	UniRef90_Q12618
Acyl-CoA desaturase		Emmonsia crescens UAMH 3008		480
Acyl-CoA desaturase (Fragment)		Emmonsia sp. CAC-2015a		84
Acyl-CoA desaturase		Emmonsia crescens		479
Acyl-CoA desaturase		Blastomyces parvus		478
+24

Protein	Similar proteins		Species	Score	Length	Source
Q12618	Probable acyl-CoA desaturase		SCHPO		479	UniRef50_O94523
Acyl-CoA desaturase		Scedosporium apiospermum		475
Acyl-CoA desaturase		Sugiyamaella lignohabitans		492
Acyl-CoA desaturase		STACB		438
Acyl-CoA desaturase		HORWE		483
+334

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X85963 Genomic DNA Translation: CAA59939.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

X85963 Genomic DNA Translation: CAA59939.1

3D structure databases

ProteinModelPortalⁱ	Q12618
SMRⁱ	Q12618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-17616

BioCycⁱ

MetaCyc:MONOMER-17616

Family and domain databases

CDDⁱ	cd03505 Delta9-FADS-like, 1 hit
Gene3Dⁱ	3.10.120.10, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR11351 PTHR11351, 1 hit
Pfamⁱ	View protein in Pfam PF00173 Cyt-b5, 1 hit PF00487 FA_desaturase, 1 hit
PIRSFⁱ	PIRSF000345 OLE1, 1 hit
PRINTSⁱ	PR00075 FACDDSATRASE
SMARTⁱ	View protein in SMART SM01117 Cyt-b5, 1 hit
SUPFAMⁱ	SSF55856 SSF55856, 1 hit
PROSITEⁱ	View protein in PROSITE PS00191 CYTOCHROME_B5_1, 1 hit PS50255 CYTOCHROME_B5_2, 1 hit PS00476 FATTY_ACID_DESATUR_1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACO1_AJECA
Accessionⁱ	Q12618Primary (citable) accession number: Q12618
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
	Last sequence update:	November 1, 1996
	Last modified:	February 28, 2018
	This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Documents

SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q12618 (ACO1_AJECA)

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Acyl-CoA desaturase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Topology

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

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3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Family and domain databases

Sequence databases

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Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ