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SLD1_KLULA
ID   SLD1_KLULA              Reviewed;         573 AA.
AC   Q6CMK7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000250|UniProtKB:Q8NKG8};
DE            EC=1.14.19.18 {ECO:0000250|UniProtKB:Q8NKG8};
GN   Name=SLD {ECO:0000250|UniProtKB:Q8NKG8}; OrderedLocusNames=KLLA0E19471g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Delta(8)-fatty-acid desaturase which introduces a double bond
CC       at the 8-position in the long-chain base (LCB) of ceramides. Required
CC       for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-
CC       4,8-dienine during glucosylceramide (GluCer) biosynthesis.
CC       {ECO:0000250|UniProtKB:Q8NKG8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC         O2 = a (4E,8E)-4-sphinga-4,8-dienine ceramide + 2 Fe(III)-[cytochrome
CC         b5] + 2 H2O; Xref=Rhea:RHEA:46280, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:85953; EC=1.14.19.18;
CC         Evidence={ECO:0000250|UniProtKB:Q8NKG8};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000250|UniProtKB:Q8NKG8}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR382125; CAG99919.1; -; Genomic_DNA.
DR   RefSeq; XP_454832.1; XM_454832.1.
DR   AlphaFoldDB; Q6CMK7; -.
DR   SMR; Q6CMK7; -.
DR   STRING; 28985.XP_454832.1; -.
DR   EnsemblFungi; CAG99919; CAG99919; KLLA0_E19471g.
DR   GeneID; 2893963; -.
DR   KEGG; kla:KLLA0_E19471g; -.
DR   eggNOG; KOG4232; Eukaryota.
DR   HOGENOM; CLU_016265_3_1_1; -.
DR   InParanoid; Q6CMK7; -.
DR   OMA; MITFYIR; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
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; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353; PTHR19353; 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; SSF55856; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
KW   Oxidoreductase; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..573
FT                   /note="Delta 8-(E)-sphingolipid desaturase"
FT                   /id="PRO_0000418890"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..77
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   MOTIF           260..264
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           297..301
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           481..485
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
FT   BINDING         37
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         60
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ   SEQUENCE   573 AA;  66992 MW;  60F8BF781CDDF44A CRC64;
     MSRVLSRRDI ADRIAKGQTI VIYEDSVLNL DKWIKFHPGG DKSIYHMIGR DATDEMNAYH
     DDQTITKFKI WKIGRIDYPW ENMLPPIQGG RFSKIDERDD IGDYDINLTS KWRSVDESNQ
     YTKIPKNDRL ASEAEVKIYP KIPQGVVPSL DLKEAYEKKI VVDPAIVSEN YDNERVYEDL
     TNFPSLDVKN QEWIASEYRK LHGEITAAGL YQCNYVRYLK EFLRIGTLFG ISFYLLSLKW
     FAISAICLGF AWQQLVFIAH DAGHISITHN YQVDNIIGMT VASWIGGLSL GWWKRNHNVH
     HLVTNDPVHD PDIQHLPFFA VSTRLFHNVY STYYDKFLWF DKFAQKVVPI QHYLYYPILC
     FGRFNLYRLS WMHVLLGQGP RRGKAAWFRY YELAGLSFFN YWFFYLIIYK QMPTNAERFK
     YVMISHIATM IVHVQITLSH FAMSTSDLGV TESFPMRQLR TSMDVDCPRW LDFFHGGLQF
     QVIHHLFPRL PRHNLRDAQS LVIKFCDKVG IKYSIYGFAA GNDVVISHLQ QIAQQAHTML
     ECAKTMKKEA TDTEFHTNKH VLAANVNEKR KQE
 
 
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