ID A0A2J6TA44_9HELO Unreviewed; 577 AA.
AC A0A2J6TA44;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN ORFNames=K444DRAFT_589563 {ECO:0000313|EMBL:PMD59890.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD59890.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD59890.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD59890.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR EMBL; KZ613803; PMD59890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TA44; -.
DR STRING; 1095630.A0A2J6TA44; -.
DR InParanoid; A0A2J6TA44; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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:SF30; DELTA 8-(E)-SPHINGOLIPID DESATURASE; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..104
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 65848 MW; 7DC498A8AF59DA23 CRC64;
MHPEITRTPS CSRQSTMIPK EISPPREREA VLSSRKIEGL IANGKYIFIL DNKVIKADAW
LNYHPGGLKA IQHMIGKDAT DEVTALHSAE TRLRMTQYQI GTIEGRWKNF VPPIQGGTFR
KYPAVVQEDS DESEDESADS DSTRATSLIS DANGEEVRKR RGGSDTDRTS ITSMSSAAGS
AAPDDLTFLD SQTKQEMELD LEKYPALDSE VQEGIVQKYR LLNQRIRAEG LYDCNYTAYV
WEAARWVSLF LTMLFFLRIG WYCTSGAFLG MFWSQLVFAA HDAGHVAITH NFTIDTLIGM
IIAAPIGGLS LGWWKRTHNV HHIVTNSPEH DPDNQHLPVF AVNHRFLGNI WSTYHERLLP
YEAVAKFLVP FQAYMYYPVL TLGRFNLYVQ SWTFLLQGQG PRKGLAWWHR YFEIAGNLIF
WYWFGYLVVY KSIPKPSARF GFVMVSHMIN MPLHVQLTLS HFAMSTTDLG PDESFPQKML
RTTMDVDCPQ WLDFFHGGLQ FQAIHHLFPR IPRHNLRRTQ SLVQEFCEDV KIPYALYGFV
DGNREVIGKL GEVSRQAAIL AKCQKTVAER ADIFHGH
//
