ID A0A367YIK7_9ASCO Unreviewed; 615 AA.
AC A0A367YIK7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN Name=SLD1_0 {ECO:0000313|EMBL:RCK65723.1};
GN ORFNames=Cantr_01448 {ECO:0000313|EMBL:RCK65723.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK65723.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK65723.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK65723.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCK65723.1}.
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DR EMBL; QLNQ01000019; RCK65723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YIK7; -.
DR STRING; 5486.A0A367YIK7; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000253472; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..126
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 71276 MW; 102366E195B95E51 CRC64;
MGRYSQHRSL RRKSNENQNI TKRTPSTIIH SLIPRERERD NCITMDGKRP KKILSRVQIT
DLIAEGKVIV IYENSVLNLT PWIKRHPGGE LAVYHMVGRD ATDEMNAYHS AETASVFKRY
KIGETDCTTW ENLLPPIQGG IYTKGSKSSG RSRLENKLDK DNSSSNSETE NFSDTSASDV
EPTEYKGIGY TERVQPVVPQ NQMVSKENKE LVFPIITDDT KKKVIRDPKT LMNNYDNELS
QNDVLNLPSL DYKTQRFLRD KYVELHEDII RMGLYDCNYW DYVREIVKIG SLFLYSLSFL
KLNYLFLSAV CMGMAWHQGT FIAHDAGHVS ISHNYQIDNL FGMIVADWFG GLSLGWWKRN
HNVHHLITND PVHDPDIQHL PFFAVSVRLF LNVYSTYYEK VLWFDKFAQF LIPFQQYLYY
PILCFGRFNL YRLSWAHLIN GDGPRQGKAA WFRYFELAGL SFFFYWFFYL LVFKTIEGGW
NRFNYVMVSH IATMLVHVQI TLSHFAMSTS DLGVSESFPS RQLRTTMDVD CPKWLDFLHG
GLQFQAIHHL FPRLPRHKLR SAQPFVIKFC EEVGLSYSIY GFGEGNDIII GKLADIGKQC
SILLDATKKY DGDLV
//
