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Protein

Acyl-CoA desaturase

Gene

OLE1

Organism
Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score: Annotation score: 3 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. 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi101Iron 1By similarity1
Metal bindingi106Iron 1By similarity1
Metal bindingi138Iron 1By similarity1
Metal bindingi141Iron 2By similarity1
Metal bindingi142Iron 1By similarity1
Metal bindingi246Iron 2By similarity1
Metal bindingi275Iron 2By similarity1
Metal bindingi278Iron 1By similarity1
Metal bindingi279Iron 2By similarity1
Metal bindingi384Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi410Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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-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
OrganismiAjellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri5037 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 54CytoplasmicCuratedAdd BLAST54
Transmembranei55 – 75HelicalSequence analysisAdd BLAST21
Topological domaini76 – 80LumenalCurated5
Transmembranei81 – 101HelicalSequence analysisAdd BLAST21
Topological domaini102 – 110CytoplasmicCurated9
Transmembranei111 – 131HelicalSequence analysisAdd BLAST21
Topological domaini132 – 199LumenalCuratedAdd BLAST68
Transmembranei200 – 220HelicalSequence analysisAdd BLAST21
Topological domaini221 – 476CytoplasmicCuratedAdd BLAST256

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854041 – 476Acyl-CoA desaturaseAdd BLAST476

Structurei

3D structure databases

ProteinModelPortaliQ12618.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini349 – 427Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST79

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi101 – 106Histidine box-1Curated6
Motifi138 – 142Histidine box-2Curated5
Motifi275 – 279Histidine 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

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.

Q12618-1 [UniParc]FASTAAdd 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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ12618.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17616.

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_AJECA
AccessioniPrimary (citable) accession number: Q12618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.