ID A0A1E3PJT9_9ASCO Unreviewed; 374 AA.
AC A0A1E3PJT9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=NADFUDRAFT_46359 {ECO:0000313|EMBL:ODQ65716.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ65716.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ65716.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ65716.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454409; ODQ65716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PJT9; -.
DR STRING; 857566.A0A1E3PJT9; -.
DR OrthoDB; 5485164at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000095009; 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:UP000095009};
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 79..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..77
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 374 AA; 42638 MW; 3958E1791CF2E423 CRC64;
MATADTTGLG RSTNKDIYLP ESSSQIAEKP VVEQQEELGN PNSFLWTFQE EPHRSRRRAI
VKAHPEVTKL CGHEPLTKYV IFFVVGLQFL CAYLLRNTPF LSWKFFLVAY IIGATCSQNV
FLAIHEMSHN LAFKKPLHNK LFSIFTNLPI GVPYSAGFGP YHLLHHKHLG DAKYDTDLPT
NIEAVFLSNV AGKAFFATFQ LLFYAIRPIC VAQLPFTYIH FLNIVTIILA DVALVHFWGK
NALFYFLLSS FLAGSLHPLA GHFIAEHYVM ERPEVHSKTG IAAPETFSYY GILNFFVYNV
GLHNEHHDFP FVPWTRLHKL NEIAKEFYDP LPSHTSWSMV IVNFVFDPKV SLWCRVKREK
SARDVTDTPE TAGN
//
