ID   DEGS_KOMPG              Reviewed;         360 AA.
AC   C4R613; Q66VZ4;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000250|UniProtKB:Q5AJX2};
DE            EC=1.14.19.17 {ECO:0000305|PubMed:16339149};
DE   AltName: Full=Delta 4-(E)-sphingolipid desaturase {ECO:0000303|PubMed:16339149};
DE   AltName: Full=Dihydroceramide desaturase {ECO:0000250|UniProtKB:Q5AJX2};
GN   OrderedLocusNames=PAS_chr3_0939;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
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(4)-fatty-acid desaturase which introduces a double bond
CC       at the 4-position in the long-chain base (LCB) of ceramides. Required
CC       for the formation of the monounsaturated sphingoid base (E)-sphing-4-
CC       enine during glucosylceramide (GluCer) biosynthesis.
CC       {ECO:0000269|PubMed:16339149}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC         ChEBI:CHEBI:52639; EC=1.14.19.17;
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. DEGS
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAY70999.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY700778; AAU10085.1; -; Genomic_DNA.
DR   EMBL; FN392321; CAY70999.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_002493178.1; XM_002493133.1.
DR   AlphaFoldDB; C4R613; -.
DR   STRING; 644223.C4R613; -.
DR   EnsemblFungi; CAY70999; CAY70999; PAS_chr3_0939.
DR   GeneID; 8200290; -.
DR   KEGG; ppa:PAS_chr3_0939; -.
DR   eggNOG; KOG2987; Eukaryota.
DR   HOGENOM; CLU_032156_0_0_1; -.
DR   InParanoid; C4R613; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000000314; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR   CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR   InterPro; IPR011388; DES1/DES2.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   Pfam; PF08557; Lipid_DES; 1.
DR   PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR   SMART; SM01269; Lipid_DES; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW   Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="Sphingolipid delta(4)-desaturase"
FT                   /id="PRO_0000434802"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           109..113
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           146..150
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           288..292
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  41541 MW;  9F30B3DE73658A88 CRC64;
     MITHRSNNVQ YEVTPPSVEE DLGPQFEFYW TRQKDPHSIR RKLILAKHPE VAKLCGPEWR
     TKYIASAVVL LQLSIAYALK NTPVLSFKFL ALAYVVGATA NQNCFLCIHE LSHNLAFRKP
     LHNKLFAIWV NLPIGVPYSA SFQPYHQLHH KFLGDEVLDT DLPTPLEATV LSSLLGKAFF
     ATFQIFFYAL RPMMVTSIDM TFIHLLNVLV CLVSDFILIK FGSANSLWYL ILSSFFAGSL
     HPTAGHFIAE HYLLDPPKHY TQFQDVPPLE TYSYYGMLNL FTWNVGYHNE HHDFPFIAWS
     KLPLLRTIAH DFYQPLPKHT SWVRVIVDFI FDENVLMYNR VKRETAKDKS VDSKTTKTQS