SLD1_CANAL
ID SLD1_CANAL Reviewed; 584 AA.
AC Q5AEK8; A0A1D8PJJ1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000303|PubMed:19047747};
DE EC=1.14.19.18 {ECO:0000269|PubMed:19047747};
GN Name=SLD1 {ECO:0000303|PubMed:19047747};
GN OrderedLocusNames=CAALFM_C302680CA; ORFNames=CaO19.260;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=19047747; DOI=10.1099/mic.0.2008/018788-0;
RA Oura T., Kajiwara S.;
RT "Disruption of the sphingolipid delta(8)-desaturase gene causes a delay in
RT morphological changes in Candida albicans.";
RL Microbiology 154:3795-3803(2008).
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:19047747}.
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:19047747};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:19047747}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Has a decreased hyphal growth rate and is highly
CC sensitive to SDS and fluconazole. {ECO:0000269|PubMed:19047747}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; CP017625; AOW28301.1; -; Genomic_DNA.
DR RefSeq; XP_719958.2; XM_714865.2.
DR AlphaFoldDB; Q5AEK8; -.
DR SMR; Q5AEK8; -.
DR STRING; 237561.Q5AEK8; -.
DR GeneID; 3638406; -.
DR KEGG; cal:CAALFM_C302680CA; -.
DR CGD; CAL0000198953; SLD1.
DR VEuPathDB; FungiDB:C3_02680C_A; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_016265_3_1_1; -.
DR InParanoid; Q5AEK8; -.
DR OMA; MITFYIR; -.
DR OrthoDB; 1060606at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000559; Chromosome 3.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IMP:CGD.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IBA:GO_Central.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IMP:CGD.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IMP:CGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:CGD.
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; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..584
FT /note="Delta 8-(E)-sphingolipid desaturase"
FT /id="PRO_0000434805"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 7..82
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 109..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..297
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 330..334
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 514..518
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 42
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 65
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 584 AA; 67383 MW; 52EF576E04ED7538 CRC64;
MDVKRPKKIF TRSQIIDLIA DGKVIVIYKN NVLNLTSWIK KHPGGDKAAY HMVGKDATDE
MHAYHCDETV DTFTRFKIGE IEGPRWENLL PPIQGGIYAK GGHYGSLNNK NTSNKKTLDS
KLDNDSSNST SDLECLTTTN SCDSDISETE IANYKGIGFV PSVKPVVPQN QLVSKSNMDI
VFPIIDEETK KKVIRNPKTL LNNYDNKLSQ EDVMSLPALD YDSQQVLRDK YNELHQTIID
YGLYECDLWD YVREVTKIGS LFLYSLSFLK INQLFLSAVF MGMAWHQGTF IAHDAGHIGI
THNYQIDNIF GMLIADWFGG LSLGWWKRNH NVHHLITNDP VHDPDIQHLP FFAVSVRLFQ
NVYSTYYDKI LPFDKFSQFL IPLQKYLYYP ILCFGRFNLY RLSWTHVLCG QGPRQGKAAW
FRYFEFFGLS FFFYWFFYLL VFKTIEGGWN RFNYVMVSHI TTMLVHVQIT LSHFAMSTAD
LGVSESFPSR QVRTTMDVDC PEWLDFLHGG LQFQAIHHLF PRLPRHNLRK AQPFVIKFCE
EVGLSYSIYG FGEGNEIVIS RLADIGKQCS IFLDATKHYE GDLY
