ID A0A1E4TQ57_PACTA Unreviewed; 589 AA.
AC A0A1E4TQ57;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Delta 8-(E)-sphingolipid desaturase {ECO:0000256|ARBA:ARBA00016939};
DE EC=1.14.19.18 {ECO:0000256|ARBA:ARBA00012019};
GN ORFNames=PACTADRAFT_45547 {ECO:0000313|EMBL:ODV93883.1};
OS Pachysolen tannophilus NRRL Y-2460.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV93883.1, ECO:0000313|Proteomes:UP000094236};
RN [1] {ECO:0000313|Proteomes:UP000094236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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)-
CC sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002593}.
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:0000256|ARBA:ARBA00029352};
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; KV454017; ODV93883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TQ57; -.
DR STRING; 669874.A0A1E4TQ57; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000094236; 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 Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000094236};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..101
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 589 AA; 67978 MW; B75F113562CB01D1 CRC64;
MVAFPVVTTT TIPKKKNKVS IVGNKNDVLS PRQIEHLIAI GYAIVIYEQY VLKLNGWLAK
HPGGDLAIFH MIGRDASDEM NAYHCDETVV TFKKYAIGRI DYKWENMLPP IQGGIYKKID
GLDENLTNKD VSMKPVGTAE FLITPRIPQG EILSLDKPNL FTSENPTSIR DPKLIIENYD
NNLVKLDLLS IPSLDYKTQR YLSHKYNLLH ENIISQGFYK CPYIEYFKEF CRIGSLFLWC
LIFLKLKYFK LSAFCLGCAW QQAVFSVHDA GHISITHNYT IDNVIGMLIA SFFGGLSLGW
WKRNHNVHHL IPNDPVHDPD IQHLPFFAVS SRLMGNVYST YYKKRLWFDK AAKILVRVQR
YTYYLILAFG RFNLYRLSME HLILGLGPRK GKAAWFRYFE LLGLVFFSYW FCYLIMTKTL
TNWQDRLIYL MISHVTTMLV HVQITLSHFA MSTSDLGTSE SFVSRQIRTT MDVDCPEWFD
YFHGGLQFQA IHHLFPRLPR HNFRKVQPLV IKFCEEVGLK YSIYGFVVGN GVVLDKMGDI
GQQVGILRDC LKNMKSEKID GANYYEKKLQ TAINEGKPCS SQSLEITSS
//
