ID A0A2K1QGY1_9PEZI Unreviewed; 393 AA.
AC A0A2K1QGY1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000256|PIRNR:PIRNR017228};
DE EC=1.14.19.17 {ECO:0000256|PIRNR:PIRNR017228};
GN ORFNames=CAC42_6653 {ECO:0000313|EMBL:PNS14140.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS14140.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS14140.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS14140.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|PIRNR:PIRNR017228}.
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:0000256|PIRNR:PIRNR017228};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|PIRNR:PIRNR017228}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|ARBA:ARBA00006146,
CC ECO:0000256|PIRNR:PIRNR017228}.
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:PNS14140.1}.
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DR EMBL; NKHZ01000088; PNS14140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QGY1; -.
DR STRING; 2082308.A0A2K1QGY1; -.
DR InParanoid; A0A2K1QGY1; -.
DR OrthoDB; 5485164at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000243797; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
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 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Reference proteome {ECO:0000313|Proteomes:UP000243797};
KW Sphingolipid metabolism {ECO:0000256|PIRNR:PIRNR017228};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 35..73
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 393 AA; 44324 MW; DE1822F966158C2D CRC64;
MAPSMTATAI EAPAQPVLRL QSEFPVDQTS QQTETEKEDF FWTYTEEPHR TRRQAIIKAH
PEVLKLCGPE PLTIPVVVFV VSLQVLCAYL LQSTPFFSLQ FFLTAYIIGA TANQNLFLAI
HEISHNLAFK SGRANRLLAI FANLPIGIPY SASFRPYHLT HHKSLGVDGL DTDLPTSLEA
VFLDSVLGKA FFATFQILFY ALRPMFVYQL PFTNLHALNV AVQLLFDFFL VKTCGGQALK
YLIFSSFLAG SLHPCAGHFI AEHYVFDRDG VERKYTEDVR KASASKKEAL KSIEVPETFS
YYGPLNFFTY NVGLHNEHHD FPAIPWTRLP ELNRIAHEFY DDLPCHKSWV GVIWQFIMDE
QVGLWCRVKR AEGGRKVGAG GDTGVGRADP MIQ
//
