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Database: UniProt
Entry: G2XGZ9_VERDV
LinkDB: G2XGZ9_VERDV
Original site: G2XGZ9_VERDV 
ID   G2XGZ9_VERDV            Unreviewed;       553 AA.
AC   G2XGZ9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE            EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN   ORFNames=VDAG_09431 {ECO:0000313|EMBL:EGY19097.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY19097.1};
RN   [1] {ECO:0000313|EMBL:EGY19097.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY19097.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) 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; DS572720; EGY19097.1; -; Genomic_DNA.
DR   RefSeq; XP_009656687.1; XM_009658392.1.
DR   AlphaFoldDB; G2XGZ9; -.
DR   STRING; 498257.G2XGZ9; -.
DR   EnsemblFungi; EGY19097; EGY19097; VDAG_09431.
DR   GeneID; 20710894; -.
DR   KEGG; vda:VDAG_09431; -.
DR   eggNOG; KOG4232; Eukaryota.
DR   HOGENOM; CLU_016265_3_1_1; -.
DR   InParanoid; G2XGZ9; -.
DR   OMA; LYNCNYF; -.
DR   OrthoDB; 294339at2759; -.
DR   UniPathway; UPA00222; -.
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   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        230..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..84
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          94..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  63383 MW;  ED325A3AA67507A9 CRC64;
     MDARKHRDLP LLSRRQVEGL IASGRTIIIV DNYVLKVDAW LKYHPGGDKA IMHMVGRDAT
     DEVTVLHSPE AREQMMRYRI GRVGGRWENF LPPIQGGSFR DMATEAPEDE EQTSTSSDTD
     SREASPVFDA EKPLAHRRYN TTTTNTRGHS SSASSVSSHD DDHKMTPTGF LDAQTKKEIS
     LDLDRYPSLD INTQHEIVIK YRLLNKRIQA EGLYDCNYLS YAIEMVRYSL LFSGMLLFLS
     RGWYVPSAMC LGIFWHQLVF AAHDAGHMGI THNFHIDTCI GIFIADFLGG LSLGWWKRSH
     NVHHIVTNSP EHDPDIEHMP FFAVSHRLLG NLYSTYYDRL MKYDAFAKVM LSVQSKTYYP
     IMLFGRFNLY VLSWDHLIAG RAPRHGPAWW HRWLEVVGQA FFWAWFGYGI VYRCIPTAWD
     RVVFVIVSHM LQAPLHIQIT LSHFAMSTAD LGPAESFPQK MLRTTMDVDC PTWLDFFHGG
     LQFQAIHHLY PRIPRHNLRR TQKLVQEFCV DVGIPYALYG FVDGNKTVIG KLAEVSRQAA
     ILAECQKHVA SHE
//
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