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Database: UniProt
Entry: A0A395H6G5_9EURO
LinkDB: A0A395H6G5_9EURO
Original site: A0A395H6G5_9EURO 
ID   A0A395H6G5_9EURO        Unreviewed;       536 AA.
AC   A0A395H6G5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE            EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN   ORFNames=BO80DRAFT_422953 {ECO:0000313|EMBL:RAL03512.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL03512.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL03512.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL03512.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) 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; KZ824427; RAL03512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395H6G5; -.
DR   STRING; 1448316.A0A395H6G5; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_422953; -.
DR   OrthoDB; 294339at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000249402; 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:UP000249402};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        207..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..87
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   536 AA;  61960 MW;  AC6B4FDBD6D9C6FB CRC64;
     MQSISNFLPE KHPILSSRQI EGLIAAGQHI LIIHQKVLRV DSWIPYHPGG HKPIQHLVGK
     DATDEFTVFH SEETQKLIDR YQIGRIEGRW RNLVPPIQGG QFRPYDENIP SDGTKESTIL
     NGQNTDQDNR LDPVLAADLN STEAMTFLDS ETKKEISLTL TQYPPLDEIT QGDIIHKYHR
     LHEQIQAEGL YNCNYIAYAK EFTRCSLIFT TMLFFLHIGW YCTSALFLGF FWSQLVFAAH
     DAGHMAITHN FTIDSLIGMT IAAPIGGLSL GWWKRTHNVH HTVTNLPEHD PDNQHLPFLA
     VNHRFLGNLF SSYHERLMPY TKAARCLVPY QAYLYYPVLM FGRFNLYIQS WIFLLHGQGP
     RKGLAWWHRW YEIIGNILFW TWFGYGIVYR CIPTAWDRFV FVMISHMVTM PLHVQFTLSH
     FAMSTMDLGP SESFAQRMLR TTMDVDCPEW LDFIHGGLQF QAIHHLFPRV PRHNLRRTQK
     LVLEFCREVG IPYALYGFVS GNRKVVGSLA EVSRQAAILA QCQRTIARRG DFIHGH
//
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