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Protein

Probable acyl-CoA desaturase

Gene

SPCC1281.06c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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. 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.By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi110Iron 1By similarity1
Metal bindingi115Iron 1By similarity1
Metal bindingi147Iron 1By similarity1
Metal bindingi150Iron 2By similarity1
Metal bindingi151Iron 1By similarity1
Metal bindingi255Iron 2By similarity1
Metal bindingi284Iron 2By similarity1
Metal bindingi287Iron 1By similarity1
Metal bindingi288Iron 2By similarity1
Metal bindingi390Iron (heme axial ligand)1
Metal bindingi416Iron (heme axial ligand)1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-75105. Fatty acyl-CoA biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable acyl-CoA desaturase (EC:1.14.19.1By similarity)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase
Gene namesi
ORF Names:SPCC1281.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1281.06c.
PomBaseiSPCC1281.06c.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 61CytoplasmicCuratedAdd BLAST61
Transmembranei62 – 82HelicalSequence analysisAdd BLAST21
Topological domaini83 – 89LumenalCurated7
Transmembranei90 – 110HelicalSequence analysisAdd BLAST21
Topological domaini111 – 204CytoplasmicCuratedAdd BLAST94
Transmembranei205 – 225HelicalSequence analysisAdd BLAST21
Topological domaini226 – 229LumenalCurated4
Transmembranei230 – 250HelicalSequence analysisAdd BLAST21
Topological domaini251 – 479CytoplasmicCuratedAdd BLAST229

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854051 – 479Probable acyl-CoA desaturaseAdd BLAST479

Proteomic databases

MaxQBiO94523.
PRIDEiO94523.

PTM databases

iPTMnetiO94523.

Interactioni

Protein-protein interaction databases

MINTiMINT-4684891.
STRINGi4896.SPCC1281.06c.1.

Structurei

3D structure databases

ProteinModelPortaliO94523.
SMRiO94523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini357 – 433Cytochrome b5 heme-bindingAdd BLAST77

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi110 – 115Histidine box-1Curated6
Motifi147 – 151Histidine box-2Curated5
Motifi284 – 288Histidine box-3Curated5

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000270353.
InParanoidiO94523.
KOiK00507.
OMAiWAHRAYN.
OrthoDBiEOG092C2CE8.
PhylomeDBiO94523.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
Gene3Di3.10.120.10. 1 hit.
InterProiView 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.
IPR005804. FA_desaturase_dom.
IPR001522. FADS-1_CS.
PANTHERiPTHR11351. PTHR11351. 1 hit.
PfamiView protein in Pfam
PF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
PIRSFiPIRSF000345. OLE1. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
SMARTiView protein in SMART
SM01117. Cyt-b5. 1 hit.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiView protein in PROSITE
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.

Sequencei

Sequence statusi: Complete.

O94523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPSATAFS SATTQPTTEG NASMRKRTIP VVPSVPERKW DPKAPKHIQE
60 70 80 90 100
QPWTMQNWWR HLNWLHCMLI FGLPMIAIYG VFTTPLQTKT LIFAIIYYAY
110 120 130 140 150
SGLGITAGYH RLWSHRAYKA KKPLEYFLAA GGAAAFEGSI RWWSRDHRAH
160 170 180 190 200
HRYTDTDKDP YNVKKGFWYA HVGWMIILQN PRRIGRSDVS DLNSDPFVMF
210 220 230 240 250
NHRHFLPIAS FMAFIFPSLF CGLLWGDYRG GYFYAGVCRL VFVHHATFCV
260 270 280 290 300
NSLAHLIGSQ PFDDTNSARN HFITALVTLG EGNHNYHHAF PNDYRNGLRW
310 320 330 340 350
YEYDPTKIFI YIASLFGLAY NLNTFPDNEI QKGIVQQKQK VLDRWRAKLN
360 370 380 390 400
WGIPLEQLPV MEFEDFLEQS KTRPLVLING VVHDMTGFEH PGGQGLLRSA
410 420 430 440 450
FGKDATAAFN GGVYDHTNGA HNLLSTYRVA VVRGGMEVEV WKSGAGAQLP
460 470
MKDTQGQKIV RVGEQITRIQ PPIEAAAAN
Length:479
Mass (Da):54,438
Last modified:May 1, 1999 - v1
Checksum:iED5666E7B35EFCF2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54 – 59TMQNWW → GPCKTV (PubMed:10759889).Curated6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22827.1.
AB027859 Genomic DNA. Translation: BAA87163.1.
PIRiT40925.
RefSeqiNP_588170.1. NM_001023159.2.

Genome annotation databases

EnsemblFungiiSPCC1281.06c.1; SPCC1281.06c.1:pep; SPCC1281.06c.
GeneIDi2538753.
KEGGispo:SPCC1281.06c.

Similar proteinsi

Entry informationi

Entry nameiACO1_SCHPO
AccessioniPrimary (citable) accession number: O94523
Secondary accession number(s): Q9UU24
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: October 25, 2017
This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families