ID A0A1Y2ERI5_PROLT Unreviewed; 338 AA.
AC A0A1Y2ERI5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000256|PIRNR:PIRNR017228};
DE EC=1.14.19.17 {ECO:0000256|PIRNR:PIRNR017228};
GN ORFNames=BCR37DRAFT_384610 {ECO:0000313|EMBL:ORY73894.1};
OS Protomyces lactucae-debilis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Protomycetaceae; Protomyces.
OX NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY73894.1, ECO:0000313|Proteomes:UP000193685};
RN [1] {ECO:0000313|EMBL:ORY73894.1, ECO:0000313|Proteomes:UP000193685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-1054 {ECO:0000313|EMBL:ORY73894.1,
RC ECO:0000313|Proteomes:UP000193685};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY73894.1}.
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DR EMBL; MCFI01000032; ORY73894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2ERI5; -.
DR STRING; 56484.A0A1Y2ERI5; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000193685; 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:UP000193685};
KW Sphingolipid metabolism {ECO:0000256|PIRNR:PIRNR017228};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..51
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 338 AA; 38755 MW; C390FA9B0B34A176 CRC64;
MATDMEVRTE AEQRLLDFHW SYSEEPHRTR RQAIIKAHPE VGALCGPEPL TKWLVLLVVF
VQTLAAVFLR DAPILSWRFM LTAYLLGGTC NQNIFLAIHE ISHNLAFKSM MANRYFAIVA
NLPIGLPYSA AFRPYHLEHH KHLGVDGIDT DLPTRFEALF LQNVLGKAFF ATFQIFFYAL
RPMMVKAMPF TPLHFANIFT QLSFDYILVS LFGWKPLLYL LFSSFFAGSL HPCAGHFIAE
HYVFENSMSD ETGVPAETYS YYGGLNALTY NVGYHNEHHD FPFVAWTRLP KLRAVASEFY
DDLPQHGSWT YVIFQFITDP KVGMFSRVKR TGSNVKKA
//
