SLD1_KLULC
ID SLD1_KLULC Reviewed; 573 AA.
AC Q8NKG8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000303|PubMed:12402089};
DE EC=1.14.19.18 {ECO:0000269|PubMed:12402089};
GN Name=SLD {ECO:0000303|PubMed:12402089};
OS Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=28985;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 56498 / CBS 683 / DSM 4394 / NBRC 1090 / NRRL Y-8279;
RX PubMed=12402089; DOI=10.1007/s00284-002-3860-0;
RA Takakuwa N., Kinoshita M., Oda Y., Ohnishi M.;
RT "Isolation and characterization of the genes encoding delta(8)-sphingolipid
RT desaturase from Saccharomyces kluyveri and Kluyveromyces lactis.";
RL Curr. Microbiol. 45:459-461(2002).
CC -!- FUNCTION: Delta(8)-fatty-acid desaturase which introduces a double bond
CC at the 8-position in the long-chain base (LCB) of ceramides. Required
CC for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-
CC 4,8-dienine during glucosylceramide (GluCer) biosynthesis.
CC {ECO:0000269|PubMed:12402089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = a (4E,8E)-4-sphinga-4,8-dienine ceramide + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46280, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:85953; EC=1.14.19.18;
CC Evidence={ECO:0000269|PubMed:12402089};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:12402089}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB085690; BAB93118.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NKG8; -.
DR SMR; Q8NKG8; -.
DR KEGG; ag:BAB93118; -.
DR VEuPathDB; FungiDB:KLLA0_E19471g; -.
DR BioCyc; MetaCyc:MON-14475; -.
DR BRENDA; 1.14.19.18; 2825.
DR BRENDA; 1.14.19.4; 2825.
DR UniPathway; UPA00222; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..573
FT /note="Delta 8-(E)-sphingolipid desaturase"
FT /id="PRO_0000418889"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..77
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 260..264
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 297..301
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 481..485
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 37
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 573 AA; 67065 MW; 9383EBA4323F1A57 CRC64;
MSRVLSRRDI ADRIAKGQTI VIYEDSVLNL DKWIKFHPGG DKSIYHMIGR DATDEMNAYH
DDQTITKFKI WKIGRIDYPW ENMLPPIQGG RFSKIDERDD IGDYDINLTS KWRSVDESNQ
YTKIPKNDRL ASEAEVKIYP KIPQGVVPSL DLKEAYEKKI VVDPAIVSEN YDNERVYEDL
TNFPSLDVKN QEWIASEYRK LHGEITAAGL YQCNYVRYLR EFLRIGTLFG ISFYLLSLKW
FAISAICLGF AWQQLVFIAH DAGHISITHN YQVDNIIGMT VASWIGGLSL GWWKRNHDVH
HLVTNDPVHD PDIQHLPFFA VSTRLFHNVY STYYDKFLWF DKFAQKVVPI QHYLYYPILC
FGRFNLYRLS WMHVLLGQGP RRGKAAWFRY YELAELSFFN YWFFYLIIYK QMPTNAERFK
YVMISHIATM IVHVQITLSH FAMSTSDLGV TESFPMRQLR TSMDVDCPRW LDFFHGGLQF
QVIHHLFPRL PRHNLKDAQS LVIKFCDKVG IKYSIYGFAA GNDVVISHLQ QIAQQAHTML
ECAKTMKKEA TDTEFHTNKH VLAANVNEKR KQE
