(data stored in SCRATCH zone)

SWISSPROT: Q6BM96_DEBHA

ID   Q6BM96_DEBHA            Unreviewed;       376 AA.
AC   Q6BM96;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Ceramide very long chain fatty acid hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE            EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN   OrderedLocusNames=DEHA2F07304g {ECO:0000313|EMBL:CAG89012.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89012.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89012.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Ceramide hydroxylase involved in the hydroxylation of
CC       sphingolipid-associated very long chain fatty acids. Postulated to
CC       hydroxylate the very long chain fatty acid of dihydroceramides and
CC       phytoceramides at C-2. {ECO:0000256|PIRNR:PIRNR005149}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR005149-50};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005149};
CC       Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic
CC       dimetal center. {ECO:0000256|PIRNR:PIRNR005149};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR005149}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7
CC       subfamily. {ECO:0000256|PIRNR:PIRNR005149}.
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DR   EMBL; CR382138; CAG89012.1; -; Genomic_DNA.
DR   RefSeq; XP_460675.1; XM_460675.1.
DR   STRING; 4959.XP_460675.1; -.
DR   EnsemblFungi; CAG89012; CAG89012; DEHA2F07304g.
DR   GeneID; 2903259; -.
DR   KEGG; dha:DEHA2F07304g; -.
DR   HOGENOM; HOG000023981; -.
DR   InParanoid; Q6BM96; -.
DR   KO; K19703; -.
DR   OMA; DMTHYFL; -.
DR   OrthoDB; 1049908at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IEA:EnsemblFungi.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006673; P:inositol phosphoceramide metabolic process; IEA:EnsemblFungi.
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; IPR006694; Fatty_acid_hydroxylase.
DR   InterPro; IPR014430; Scs7.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF04116; FA_hydroxylase; 1.
DR   PIRSF; PIRSF005149; IPC-B_HD; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM96.
DR   SWISS-2DPAGE; Q6BM96.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR005149};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR005149};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR005149};
KW   Heme {ECO:0000256|PIRSR:PIRSR005149-50};
KW   Iron {ECO:0000256|PIRNR:PIRNR005149, ECO:0000256|PIRSR:PIRSR005149-
KW   50}; Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR005149};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR005149};
KW   Membrane {ECO:0000256|PIRNR:PIRNR005149, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR005149,
KW   ECO:0000256|PIRSR:PIRSR005149-50};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR005149};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    194    213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    219    239       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    298    318       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        5     86       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   METAL        41     41       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR005149-50}.
FT   METAL        68     68       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR005149-50}.
SQ   SEQUENCE   376 AA;  43736 MW;  B5514FD40BC4D9A0 CRC64;
     MSRNLPLLAS AEVVKHNTQN DCWVTLYNRK VYNVSGFIDQ HPGGGDIILP YAGKDVTAIM
     ADTISHEHSE SAYEMLDDEM LVGYLATDEE ERELLNNKNN TPVEVRLEDS SSVDLYEFHD
     SLPPAEKLAI QTDYEEDIKK HKFLDLNKPL IPQMLCSTFS KEFYLDQVHR PRHYGKGSAP
     LFGNFLEPLS LTPWWVVPAV WLPPNFYIFY VGFVNQDKLV ALSFWVMGLF VWTLVEYCMH
     RFLFHLDGYL PEHPVALTLH FLLHGVHHYL PMDGYRLVLP PTLFVLLAYP FYKLVFAIFP
     FYMACSGFAG GTLGYILYDV IHYVIHHTKL PQFLQDIKTY HLEHHYKNYE MGFGVTSRFW
     DVIFETEITS TFQKRN
//

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