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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101Iron 1By similarity
Metal bindingi115 – 1151Iron 1By similarity
Metal bindingi147 – 1471Iron 1By similarity
Metal bindingi150 – 1501Iron 2By similarity
Metal bindingi151 – 1511Iron 1By similarity
Metal bindingi255 – 2551Iron 2By similarity
Metal bindingi284 – 2841Iron 2By similarity
Metal bindingi287 – 2871Iron 1By similarity
Metal bindingi288 – 2881Iron 2By similarity
Metal bindingi390 – 3901Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi416 – 4161Iron (heme axial ligand)PROSITE-ProRule annotation

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6161CytoplasmicCuratedAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Topological domaini83 – 897LumenalCurated
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 20494CytoplasmicCuratedAdd
BLAST
Transmembranei205 – 22521HelicalSequence analysisAdd
BLAST
Topological domaini226 – 2294LumenalCurated
Transmembranei230 – 25021HelicalSequence analysisAdd
BLAST
Topological domaini251 – 479229CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Probable acyl-CoA desaturasePRO_0000185405Add
BLAST

Proteomic databases

MaxQBiO94523.

Interactioni

Protein-protein interaction databases

MINTiMINT-4684891.

Structurei

3D structure databases

ProteinModelPortaliO94523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini357 – 43377Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1156Histidine box-1Curated
Motifi147 – 1515Histidine box-2Curated
Motifi284 – 2885Histidine box-3Curated

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

Phylogenomic databases

HOGENOMiHOG000270353.
InParanoidiO94523.
KOiK00507.
OMAiHITETPL.
OrthoDBiEOG092C2CE8.
PhylomeDBiO94523.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
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.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 596TMQNWW → GPCKTV (PubMed:10759889).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO94523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4684891.

Proteomic databases

MaxQBiO94523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

HOGENOMiHOG000270353.
InParanoidiO94523.
KOiK00507.
OMAiHITETPL.
OrthoDBiEOG092C2CE8.
PhylomeDBiO94523.

Enzyme and pathway databases

ReactomeiR-SPO-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiO94523.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
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.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACO1_SCHPO
AccessioniPrimary (citable) accession number: O94523
Secondary accession number(s): Q9UU24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 118 of the entry and version 1 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.