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Database: UniProt
Entry: A0A0D7AGV2_9AGAR
LinkDB: A0A0D7AGV2_9AGAR
Original site: A0A0D7AGV2_9AGAR 
ID   A0A0D7AGV2_9AGAR        Unreviewed;       553 AA.
AC   A0A0D7AGV2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE            EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN   ORFNames=FISHEDRAFT_64725 {ECO:0000313|EMBL:KIY50521.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY50521.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY50521.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY50521.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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; KN881675; KIY50521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7AGV2; -.
DR   OrthoDB; 294339at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000054144; 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:UP000054144};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        230..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..85
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   553 AA;  62798 MW;  6FCF6AEA3E31CB98 CRC64;
     MVTDSKRPLN AIPRATVVAR ILDGEHLVIY KGLVLRIPHS WLDAHPGGNL SILHYVGRDA
     TDEVEVYHPD DVLQAIKCYA IGTVDEAELP WNPFIPPVEV GWVRKRVKAT EGSKPEGGKA
     SKYVWFKEAD AMRAPADSTD PLCPPSQILL VQKNTLLPEC DTPSLETLIA PPSTLSLQVQ
     VEHSVAFKDL HQRIIDAGLY KCRYISGYGP EIVRYSMFAF ASYWFYQKQW FLSSAFFLGL
     FWWQLVFFAH DLGHVGVTHC WEIDRLISIL IADFIGGLSI GWWVDNHNIH HLVTNHPSHD
     PDIEHLPFLA ISPVFFQSLW SSYYKRTMHF DAFAKVFITI QHYLFYVIML LARFNLYGLS
     YTFLVKKAFD TRRTKGGRWA WGLEIVGIIF FWCWFGRVLV GCGDWKTALG YLFVSHASTS
     ILHVQIVLSH FSMSTADLGP TESFPARQMR TTSDVICRPD LGWIHGGLHL QVTHHLFPRL
     PRHNLGEASK LVKEFAKERG LVYAEFGFVD GNMEMLGVLQ GVAEQLKIMK RVAKLEVQAA
     VDKKLAATDT KTE
//
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