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Protein

Delta(8)-fatty-acid desaturase

Gene

sld1

Organism
Helianthus annuus (Common sunflower)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role as delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides with or without a hydroxy group at the 4-position. The enzyme produces both the 8E and 8Z isomers. This structural modification contributes to the quantitative partitioning of ceramides between the two major sphingolipid classes, glucosylceramides and glycosylinositolphosphoryl ceramides. Sphingolipids are important membrane components involved in environmental stress responses, such as resistance to chilling, and act as cell signaling molecules.2 Publications

Catalytic activityi

A (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8E)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O.3 Publications
A (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8Z)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O.3 Publications

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi74 – 741Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Lipid metabolism, Sphingolipid metabolism, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(8)-fatty-acid desaturase (EC:1.14.19.293 Publications)
Alternative name(s):
Delta(8)-sphingolipid desaturase
Sphingolipid 8-(E/Z)-desaturase
Gene namesi
Name:sld1
OrganismiHelianthus annuus (Common sunflower)
Taxonomic identifieri4232 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceHeliantheaeHelianthus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence analysisAdd
BLAST
Transmembranei185 – 20521HelicalSequence analysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence analysisAdd
BLAST
Transmembranei293 – 31321HelicalSequence analysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Delta(8)-fatty-acid desaturasePRO_0000418893Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ43469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10085Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi169 – 1735Histidine box-1Curated
Motifi206 – 2105Histidine box-2Curated
Motifi383 – 3875Histidine box-3Curated

Domaini

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

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q43469-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSPSIEVLN SIADGKKYIT SKELKKHNNP NDLWISILGK VYNVTEWAKE
60 70 80 90 100
HPGGDAPLIN LAGQDVTDAF IAFHPGTAWK HLDKLFTGYH LKDYQVSDIS
110 120 130 140 150
RDYRKLASEF AKAGMFEKKG HGVIYSLCFV SLLLSACVYG VLYSGSFWIH
160 170 180 190 200
MLSGAILGLA WMQIAYLGHD AGHYQMMATR GWNKFAGIFI GNCITGISIA
210 220 230 240 250
WWKWTHNAHH IACNSLDYDP DLQHLPMLAV SSKLFNSITS VFYGRQLTFD
260 270 280 290 300
PLARFFVSYQ HYLYYPIMCV ARVNLYLQTI LLLISKRKIP DRGLNILGTL
310 320 330 340 350
IFWTWFPLLV SRLPNWPERV AFVLVSFCVT GIQHIQFTLN HFSGDVYVGP
360 370 380 390 400
PKGDNWFEKQ TRGTIDIACS SWMDWFFGGL QFQLEHHLFP RLPRCHLRSI
410 420 430 440 450
SPICRELCKK YNLPYVSLSF YDANVTTLKT LRTAALQARD LTNPAPQNLA

WEAFNTHG
Length:458
Mass (Da):52,231
Last modified:November 1, 1996 - v1
Checksum:iD182287AB0E99245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87143 mRNA. Translation: CAA60621.1.
PIRiS68358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87143 mRNA. Translation: CAA60621.1.
PIRiS68358.

3D structure databases

ProteinModelPortaliQ43469.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR012171. Fatty_acid_desaturase.
IPR005804. Fatty_acid_desaturase_dom.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
[Graphical view]
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A cytochrome-b5-containing fusion protein similar to plant acyl lipid desaturases."
    Sperling P., Schmidt H., Heinz E.
    Eur. J. Biochem. 232:798-805(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Further characterization of Delta(8)-sphingolipid desaturases from higher plants."
    Sperling P., Blume A., Zahringer U., Heinz E.
    Biochem. Soc. Trans. 28:638-641(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, REACTION MECHANISM.
  3. "Characterization of a Delta8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers."
    Beckmann C., Rattke J., Oldham N.J., Sperling P., Heinz E., Boland W.
    Angew. Chem. Int. Ed. 41:2298-2300(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  4. "Conformational studies on the Delta8(E,Z)-sphingolipid desaturase from Helianthus annuus with chiral fluoropalmitic acids as mechanistic probes."
    Habel A., Sperling P., Bartram S., Heinz E., Boland W.
    J. Org. Chem. 75:4975-4982(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.

Entry informationi

Entry nameiSLD1_HELAN
AccessioniPrimary (citable) accession number: Q43469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.