SLD1_LACK1
ID SLD1_LACK1 Reviewed; 568 AA.
AC Q8NKG9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=226302;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC / NRRL Y-12651;
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; AB085689; BAB93117.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NKG9; -.
DR SMR; Q8NKG9; -.
DR KEGG; ag:BAB93117; -.
DR BRENDA; 1.14.19.18; 6897.
DR BRENDA; 1.14.19.4; 6897.
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..568
FT /note="Delta 8-(E)-sphingolipid desaturase"
FT /id="PRO_0000418891"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
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 REGION 549..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 259..263
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 296..300
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 480..484
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 568 AA; 66466 MW; 1158BE7B876D68EC CRC64;
MDNIISRGEI EDRIARGQAI VIYEGLVLNL EKWIKFHPGG DKAIHHMIGR DATDEMKAYH
CDETVEIFRK WRIGRIDQEW ENFLPPIQGG VFRFLNQQHD STDLGLSNKW IAPNTSDQFK
FIKNEKHMCG EPDVKIYPKI PQGVIPSLNL KEAYEKKVVT DPATVADNYD NELVRQDLET
LPDLDPKTQE WLSKEYNKMH NEIIEAGLYQ CNYFRYVKEL TRIGLLFALS YYLLYHRDQK
FWSAFSMGCA WQQLVFIAHD AGHISITHHY QLDNIFGMII ASWVGGLSLG WWKRNHNVHH
LITNDPIHDP DIQHLPFFAV STRLFDNIYS TYYEKFLWFD AFAKKVVPWQ NYLYYPMLAF
GRFNLYRLSW MHVLLGLGPR RGKAGWFRYF ELCGLIFFNY WFFYLLVGCK LQTGWDRFQY
IMVSHITTML VHVQITLSHF AMSTSDLGVG EGFPMRQLRT SMDVDCPRWL DFLHGGLQFQ
VVHHLFPRLP RHNLRAAQPY VIEFCEKVGI KYSIYGFSKG NGVVLTKLQE IAVQAKTMLE
CASAMKKEAT GEREADEKTY RTKSIKNA
