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O94523 (ACO1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable acyl-CoA desaturase

EC=1.14.19.1
Alternative name(s):
Delta(9)-desaturase
Short name=Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase
Gene names
ORF Names:SPCC1281.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Utilizes O2 and electrons from the reduced cytochrome b5 domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates By similarity.

Catalytic activity

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

Cofactor

Iron By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Ref.2.

Domain

The histidine box domains may contain the active site and/or be involved in metal ion binding By similarity.

Sequence similarities

Belongs to the fatty acid desaturase family.

Contains 1 cytochrome b5 heme-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Probable acyl-CoA desaturase
PRO_0000185405

Regions

Transmembrane62 – 8221Helical; Potential
Transmembrane90 – 11021Helical; Potential
Transmembrane205 – 22521Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane305 – 32521Helical; Potential
Domain357 – 43377Cytochrome b5 heme-binding
Motif110 – 1156Histidine box-1
Motif147 – 1515Histidine box-2
Motif284 – 2885Histidine box-3

Sites

Metal binding3901Iron (heme axial ligand) By similarity
Metal binding4161Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict54 – 596TMQNWW → GPCKTV Ref.2

Sequences

Sequence LengthMass (Da)Tools
O94523 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: ED5666E7B35EFCF2

FASTA47954,438
        10         20         30         40         50         60 
MTAPSATAFS SATTQPTTEG NASMRKRTIP VVPSVPERKW DPKAPKHIQE QPWTMQNWWR 

        70         80         90        100        110        120 
HLNWLHCMLI FGLPMIAIYG VFTTPLQTKT LIFAIIYYAY SGLGITAGYH RLWSHRAYKA 

       130        140        150        160        170        180 
KKPLEYFLAA GGAAAFEGSI RWWSRDHRAH HRYTDTDKDP YNVKKGFWYA HVGWMIILQN 

       190        200        210        220        230        240 
PRRIGRSDVS DLNSDPFVMF NHRHFLPIAS FMAFIFPSLF CGLLWGDYRG GYFYAGVCRL 

       250        260        270        280        290        300 
VFVHHATFCV NSLAHLIGSQ PFDDTNSARN HFITALVTLG EGNHNYHHAF PNDYRNGLRW 

       310        320        330        340        350        360 
YEYDPTKIFI YIASLFGLAY NLNTFPDNEI QKGIVQQKQK VLDRWRAKLN WGIPLEQLPV 

       370        380        390        400        410        420 
MEFEDFLEQS KTRPLVLING VVHDMTGFEH PGGQGLLRSA FGKDATAAFN GGVYDHTNGA 

       430        440        450        460        470 
HNLLSTYRVA VVRGGMEVEV WKSGAGAQLP MKDTQGQKIV RVGEQITRIQ PPIEAAAAN 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 54-257, SUBCELLULAR LOCATION.
Strain: ATCC 38364 / 968.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA22827.1.
AB027859 Genomic DNA. Translation: BAA87163.1.
PIRT40925.
RefSeqNP_588170.1. NM_001023159.2.

3D structure databases

ProteinModelPortalO94523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275336. 4 interactions.
MINTMINT-4684891.
STRING4896.SPCC1281.06c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1281.06c.1; SPCC1281.06c.1:pep; SPCC1281.06c.
GeneID2538753.
KEGGspo:SPCC1281.06c.

Organism-specific databases

PomBaseSPCC1281.06c.

Phylogenomic databases

eggNOGCOG1398.
HOGENOMHOG000270353.
KOK00507.
OMAHITETPL.
OrthoDBEOG7S2277.
PhylomeDBO94523.

Family and domain databases

Gene3D3.10.120.10. 1 hit.
InterProIPR009160. Acyl-CoA_deSatase_haem/ster-bd.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFPIRSF000345. OLE1. 1 hit.
PRINTSPR00075. FACDDSATRASE.
SUPFAMSSF55856. SSF55856. 1 hit.
PROSITEPS50255. CYTOCHROME_B5_2. 1 hit.
PS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20799937.

Entry information

Entry nameACO1_SCHPO
AccessionPrimary (citable) accession number: O94523
Secondary accession number(s): Q9UU24
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names