ID A0A1G4JS31_9SACH Unreviewed; 561 AA.
AC A0A1G4JS31;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN ORFNames=LANO_0E04412G {ECO:0000313|EMBL:SCU93637.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU93637.1};
RN [1] {ECO:0000313|EMBL:SCU93637.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11611 {ECO:0000313|EMBL:SCU93637.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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)-
CC sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002593}.
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:0000256|ARBA:ARBA00029352};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT598451; SCU93637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4JS31; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000189911; Chromosome e.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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:SF30; DELTA 8-(E)-SPHINGOLIPID DESATURASE; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 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; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 211..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..77
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 561 AA; 65588 MW; F83F6C215F34350B CRC64;
MKHVMERSEV RERILKGQAI VIYDGHVLRL DKWIKFHPGG DKAIHHMIGR DATNEMKAYH
CDDTVDGFLK WRIGSISERW VNFLPPIQGG DFDEHSEVPD QWLVVTKQDE FEDIRSNKKM
CGEPDVKIYP KVPQGIIPSL DLKQAFERKV VSDPADISEN YDNELVRRDL ANLPSLDAET
QDWLSREYNI MHEKVINADL YKCNYLRYVK EVARIGTLFG ISFYLLFRVN HKFWSAIFLG
AAWQQLVFIA HDAGHISITH NYQVDNIIGM VIASCLGGLS LGWWKRNHNV HHLVTNDPIH
DPDIQHLPFF AVSTRLFNNI YSTYYERFIW FDKFAQKVIP LQNFLYYPIL SFGRFNLYRL
SWMHVLLGLG PRRGKAAWFR YFELAGLIFF NYWFFYLVCG KGLQSGWERF QYIMISHITT
MIVHVQITLS HFAMSTSDLG VAEGFPMRQL RTSMDVDCPR WLDFFHGGLH FQVVHHLFPR
LPRHNLRSAQ PFVIEFCEKV GLKYSIYGFK KGNTVVLNKL EEIAQQAKTM LECAKSMEQE
AVGRKNENYQ APVHEKQRKL A
//
