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Protein

Delta 8-(E)-sphingolipid desaturase

Gene

SLD

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Delta8-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.By similarity

Catalytic activityi

A (4E)-sphing-4-enine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E)-sphing-4,8-dienine ceramide + 2 ferricytochrome b5 + 2 H2O.By similarity

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi37Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi60Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Lipid metabolism, Sphingolipid metabolism, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta 8-(E)-sphingolipid desaturaseBy similarity (EC:1.14.19.18By similarity)
Gene namesi
Name:SLDBy similarity
Ordered Locus Names:KLLA0E19471g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome E

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei228 – 248HelicalSequence analysisAdd BLAST21
Transmembranei273 – 293HelicalSequence analysisAdd BLAST21
Transmembranei353 – 372HelicalSequence analysisAdd BLAST20
Transmembranei393 – 413HelicalSequence analysisAdd BLAST21
Transmembranei422 – 442HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004188901 – 573Delta 8-(E)-sphingolipid desaturaseAdd BLAST573

Interactioni

Protein-protein interaction databases

STRINGi284590.XP_454832.1.

Structurei

3D structure databases

ProteinModelPortaliQ6CMK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi260 – 264Histidine box-1Curated5
Motifi297 – 301Histidine box-2Curated5
Motifi481 – 485Histidine box-3Curated5

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4232. Eukaryota.
ENOG410XVSZ. LUCA.
HOGENOMiHOG000184828.
InParanoidiQ6CMK7.
KOiK13076.
OMAiMESIAWF.
OrthoDBiEOG092C19C2.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiView protein in InterPro
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR036400. Cyt_B5-like_heme/steroid_sf.
IPR005804. FA_desaturase_dom.
IPR012171. Fatty_acid_desaturase.
PfamiView protein in Pfam
PF00173. Cyt-b5. 1 hit.
PF00487. FA_desaturase. 1 hit.
PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
SMARTiView protein in SMART
SM01117. Cyt-b5. 1 hit.
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiView protein in PROSITE
PS50255. CYTOCHROME_B5_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6CMK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVLSRRDI ADRIAKGQTI VIYEDSVLNL DKWIKFHPGG DKSIYHMIGR
60 70 80 90 100
DATDEMNAYH DDQTITKFKI WKIGRIDYPW ENMLPPIQGG RFSKIDERDD
110 120 130 140 150
IGDYDINLTS KWRSVDESNQ YTKIPKNDRL ASEAEVKIYP KIPQGVVPSL
160 170 180 190 200
DLKEAYEKKI VVDPAIVSEN YDNERVYEDL TNFPSLDVKN QEWIASEYRK
210 220 230 240 250
LHGEITAAGL YQCNYVRYLK EFLRIGTLFG ISFYLLSLKW FAISAICLGF
260 270 280 290 300
AWQQLVFIAH DAGHISITHN YQVDNIIGMT VASWIGGLSL GWWKRNHNVH
310 320 330 340 350
HLVTNDPVHD PDIQHLPFFA VSTRLFHNVY STYYDKFLWF DKFAQKVVPI
360 370 380 390 400
QHYLYYPILC FGRFNLYRLS WMHVLLGQGP RRGKAAWFRY YELAGLSFFN
410 420 430 440 450
YWFFYLIIYK QMPTNAERFK YVMISHIATM IVHVQITLSH FAMSTSDLGV
460 470 480 490 500
TESFPMRQLR TSMDVDCPRW LDFFHGGLQF QVIHHLFPRL PRHNLRDAQS
510 520 530 540 550
LVIKFCDKVG IKYSIYGFAA GNDVVISHLQ QIAQQAHTML ECAKTMKKEA
560 570
TDTEFHTNKH VLAANVNEKR KQE
Length:573
Mass (Da):66,992
Last modified:August 16, 2004 - v1
Checksum:i60F8BF781CDDF44A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382125 Genomic DNA. Translation: CAG99919.1.
RefSeqiXP_454832.1. XM_454832.1.

Genome annotation databases

EnsemblFungiiCAG99919; CAG99919; KLLA0_E19471g.
GeneIDi2893963.
KEGGikla:KLLA0E19471g.

Similar proteinsi

Entry informationi

Entry nameiSLD1_KLULA
AccessioniPrimary (citable) accession number: Q6CMK7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: August 16, 2004
Last modified: October 25, 2017
This is version 89 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families