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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)DescriptionActionsGraphical viewLength
Metal bindingi51Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi74Iron (heme axial ligand)PROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Transmembranei147 – 167HelicalSequence analysisAdd BLAST21
Transmembranei185 – 205HelicalSequence analysisAdd BLAST21
Transmembranei264 – 284HelicalSequence analysisAdd BLAST21
Transmembranei293 – 313HelicalSequence analysisAdd BLAST21
Transmembranei320 – 340HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004188931 – 458Delta(8)-fatty-acid desaturaseAdd BLAST458

Structurei

3D structure databases

ProteinModelPortaliQ43469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 100Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST85

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi169 – 173Histidine box-1Curated5
Motifi206 – 210Histidine box-2Curated5
Motifi383 – 387Histidine box-3Curated5

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.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
[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.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
[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...

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: November 30, 2016
This is version 79 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.