SLD1_EUGGR
ID SLD1_EUGGR Reviewed; 419 AA.
AC Q9SWQ9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Delta(8)-fatty-acid desaturase {ECO:0000303|PubMed:10328826};
DE Short=EFD1 {ECO:0000303|PubMed:10328826};
DE EC=1.14.19.4 {ECO:0000305|PubMed:10328826};
DE AltName: Full=Acyl-lipid (11-3)-desaturase;
DE AltName: Full=Delta(8)-sphingolipid desaturase;
GN Name=efd1;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10328826; DOI=10.1006/abbi.1999.1167;
RA Wallis J.G., Browse J.;
RT "The Delta8-desaturase of Euglena gracilis: an alternate pathway for
RT synthesis of 20-carbon polyunsaturated fatty acids.";
RL Arch. Biochem. Biophys. 365:307-316(1999).
RN [2]
RP MISCELLANEOUS.
RX PubMed=14216427;
RA Hulanicka D., Erwin J., Bloch K.;
RT "LIPID METABOLISM OF EUGLENA GRACILIS.";
RL J. Biol. Chem. 239:2778-2787(1964).
RN [3]
RP FUNCTION.
RX PubMed=22009657; DOI=10.1007/s11745-011-3617-2;
RA Meesapyodsuk D., Qiu X.;
RT "The front-end desaturase: structure, function, evolution and
RT biotechnological use.";
RL Lipids 47:227-237(2012).
CC -!- FUNCTION: Delta(8)-fatty-acid desaturase which introduces a double bond
CC at the 8-position in 20-carbon chain length fatty acids (C20) that have
CC an existing delta-11 unsaturation (double bond) (PubMed:10328826).
CC Whether it acts on CoA-linked substrates (as in animals) or
CC phospholipid-linked substrates (as in plants and fungi) is still not
CC clear (Probable). {ECO:0000269|PubMed:10328826,
CC ECO:0000305|PubMed:22009657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (11Z,14Z)-icosadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = an (8Z,11Z,14Z)-icosatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46792, 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:88252,
CC ChEBI:CHEBI:90076; EC=1.14.19.4;
CC Evidence={ECO:0000305|PubMed:10328826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46793;
CC Evidence={ECO:0000305|PubMed:10328826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (11Z,14Z,17Z)-icosatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an (8Z,11Z,14Z,17Z)-
CC eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46796, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88253,
CC ChEBI:CHEBI:90082; EC=1.14.19.4;
CC Evidence={ECO:0000305|PubMed:10328826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46797;
CC Evidence={ECO:0000305|PubMed:10328826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (11Z)-eicosenoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (8Z,11Z)-eicosadienoyl-containing
CC glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:67660, 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:172956,
CC ChEBI:CHEBI:172957; Evidence={ECO:0000305|PubMed:10328826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67661;
CC Evidence={ECO:0000305|PubMed:10328826};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10328826}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- MISCELLANEOUS: Euglena gracilis exhibits the metabolic behavior of a
CC plant in the light and of an animal in the dark. Grown in the dark,
CC this organism contains large amounts of 20-carbon chain length (C20)
CC polyunsaturated fatty acids (PUFA), including arachidonic acid (C20:4n-
CC 6), and little or no C18 PUFAs (such as linolenic acid, C18:3). On the
CC other hand, when grown under photoauxotrophic conditions, this organism
CC is rich in linolenic acid and contain relatively small amounts of the
CC C20 PUFAs. {ECO:0000303|PubMed:14216427}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF139720; AAD45877.1; -; mRNA.
DR AlphaFoldDB; Q9SWQ9; -.
DR SwissLipids; SLP:000000806; -.
DR KEGG; ag:AAD45877; -.
DR BioCyc; MetaCyc:MON-16975; -.
DR BRENDA; 1.14.19.4; 2197.
DR UniPathway; UPA00199; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102003; F:Delta8-sphingolipid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..419
FT /note="Delta(8)-fatty-acid desaturase"
FT /id="PRO_0000418894"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..64
FT /note="Cytochrome b5 heme-binding"
FT MOTIF 143..147
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 180..184
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 355..359
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 24
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 48457 MW; C2D8EDD092F27EB2 CRC64;
MKSKRQALSP LQLMEQTYDV VNFHPGGAEI IENYQGRDAT DAFMVMHFQE AFDKLKRMPK
INPSFELPPQ AAVNEAQEDF RKLREELIAT GMFDASPLWY SYKISTTLGL GVLGYFLMVQ
YQMYFIGAVL LGMHYQQMGW LSHDICHHQT FKNRNWNNLV GLVFGNGLQG FSVTCWKDRH
NAHHSATNVQ GHDPDIDNLP PLAWSEDDVT RASPISRKLI QFQQYYFLVI CILLRFIWCF
QCVLTVRSLK DRDNQFYRSQ YKKEAIGLAL HWTLKALFHL FFMPSILTSL LVFFVSELVG
GFGIAIVVFM NHYPLEKIGD PVWDGHGFSV GQIHETMNIR RGIITDWFFG GLNYQIEHHL
WPTLPRHNLT AVSYQVEQLC QKHNLPYRNP LPHEGLVILL RYLAVFARMA EKQPAGKAL
