SLD1_KOMPG
ID SLD1_KOMPG Reviewed; 542 AA.
AC C4QVU3; Q66VZ5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000303|PubMed:16339149};
DE EC=1.14.19.18 {ECO:0000305|PubMed:16339149};
GN OrderedLocusNames=PAS_chr1-1_0013;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=16339149; DOI=10.1074/jbc.m512864200;
RA Ternes P., Sperling P., Albrecht S., Franke S., Cregg J.M., Warnecke D.,
RA Heinz E.;
RT "Identification of fungal sphingolipid C9-methyltransferases by
RT phylogenetic profiling.";
RL J. Biol. Chem. 281:5582-5592(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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:16339149}.
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:0000305|PubMed:16339149};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:16339149}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AY700777; AAU10084.1; -; Genomic_DNA.
DR EMBL; FN392319; CAY67366.1; -; Genomic_DNA.
DR RefSeq; XP_002489647.1; XM_002489602.1.
DR AlphaFoldDB; C4QVU3; -.
DR SMR; C4QVU3; -.
DR STRING; 644223.C4QVU3; -.
DR EnsemblFungi; CAY67366; CAY67366; PAS_chr1-1_0013.
DR GeneID; 8197530; -.
DR KEGG; ppa:PAS_chr1-1_0013; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_016265_3_1_1; -.
DR InParanoid; C4QVU3; -.
DR OMA; SITHGFH; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000314; Chromosome 1.
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 3: Inferred from homology;
KW Electron transport; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="Delta 8-(E)-sphingolipid desaturase"
FT /id="PRO_0000434804"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..75
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 235..239
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 272..276
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 455..459
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 35
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 58
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 542 AA; 63243 MW; 6C29D99FD8AF4226 CRC64;
MVVSREEVRE IIGRGNAIVI YEDHLLNLNG WLERHPGGEK AIHHMIGRDA SDEMNAYHDP
ETVKTFKRWS IGRVKLPWDN LVPPIQGGNY SFDKVDQRVI YKKLGIFPGV KIEPKVQENI
VLTEKSASKL LPVGGVRDPK TIIEDFDNKL VYEDIKQIPS LDHETQRNLS LQYNELHQTI
INRGYYQCDY WQYFKEFCRI SSLFLLFVLF LRSKWYTLSA ISIGLMWQQL VFIAHDAGHI
SITHNYQIDN IIGIIIANFI GGLSLGWWKR NHNVHHLVTN DPVHDPDIQH LPFFAVSSRL
LGNVFSTYYE KYLWFDKIAQ KMLQIQHKLY YPILSFGRFN LYRLSWSHLI MGLGPRKGKA
AWFRYLELIG LCFFSYWFFY KTMSYIPTKT LRFWFLLISH WTTMIVHVQI VLSHFAMSTS
DLGSTESFVS RQLRTTMDVD CPEWFDFFHG GLQFQAIHHL FPRLPRHNFR KVQPLVIEFC
KNTGLHYSIY GFVDGNGKVV NKMADVASQV VILNDCLHSI HLENTTGKNL YEAKVESVSI
KG
