ID K1WVH1_MARBU Unreviewed; 397 AA.
AC K1WVH1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000256|PIRNR:PIRNR017228};
DE EC=1.14.19.17 {ECO:0000256|PIRNR:PIRNR017228};
GN ORFNames=MBM_04946 {ECO:0000313|EMBL:EKD16477.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16477.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16477.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16477.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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}.
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DR EMBL; JH921438; EKD16477.1; -; Genomic_DNA.
DR RefSeq; XP_007292835.1; XM_007292773.1.
DR AlphaFoldDB; K1WVH1; -.
DR STRING; 1072389.K1WVH1; -.
DR GeneID; 18760881; -.
DR KEGG; mbe:MBM_04946; -.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_1_1; -.
DR InParanoid; K1WVH1; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000006753; 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:UP000006753};
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 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..96
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 397 AA; 45006 MW; B3860876C852E588 CRC64;
MPAVTSTITT ARLKNEAKIA RLRTDGEGEA REGEVKSKVV EGKAQVQVGI EKQETLETKE
HDFFWTYTEE PHRTRRMAII KAHPEVTKLC GPEPLTKYTV LLVVAVQVLA AYWLRDAAFF
SWRFFLTAYL VGATANQNLF LAIHEISHNL AFRSPRLNRA LAVFANLPIG VPYSASFRPY
HLTHHKSLGV DGLDTDLPTA LEAVFLDSIL GKAFFCTFQI LFYAIRPVFV YAVPFTTIHI
LNIAAQLAFD YVLVKTCSAH SLYYLIFSSF LAGSLHPCAG HFIAEHYVFE RQPTAAKDPL
TNTPVPETFS YYGALNMLTY NVGLHNEHHD FPAVPWTRLP VLHEIAKEFY ADLPRHESWV
GVIWQFVWDR EVGMTCRVKR KDGGRKVGGW TQQEMES
//
