ID A0A0K3CMC0_RHOTO Unreviewed; 372 AA.
AC A0A0K3CMC0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Ceramide very long chain fatty acid hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN Name=FGENESH: predicted gene_10.318 {ECO:0000313|EMBL:CTR09620.1};
GN ORFNames=AAT19DRAFT_9664 {ECO:0000313|EMBL:PRQ72325.1}, BN2166_0054810
GN {ECO:0000313|EMBL:CTR09620.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09620.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR09620.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR09620.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ72325.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ72325.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7 subfamily.
CC {ECO:0000256|ARBA:ARBA00005747, ECO:0000256|PIRNR:PIRNR005149}.
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DR EMBL; CWKI01000010; CTR09620.1; -; Genomic_DNA.
DR EMBL; LCTV02000010; PRQ72325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CMC0; -.
DR STRING; 5286.A0A0K3CMC0; -.
DR OMA; WTIIEYV; -.
DR OrthoDB; 208810at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863:SF1; FATTY ACID 2-HYDROXYLASE; 1.
DR PANTHER; PTHR12863; FATTY ACID HYDROXYLASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR PIRSF; PIRSF005149; IPC-B_HD; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR005149};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR005149-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR005149};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR005149};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR005149};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005149};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 164..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..91
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT BINDING 47
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:0000256|PIRSR:PIRSR005149-50"
FT BINDING 74
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:0000256|PIRSR:PIRSR005149-50"
SQ SEQUENCE 372 AA; 43584 MW; 828053A849223F63 CRC64;
MATAADRATK RTRIYLRSEV EKHNTAKDCW VVHNNRVYDV SQFLEDHPGG DDLILNWAGK
DITEVMQDPI EHSHSDSAYQ VLDEYQIGRL GQEECITNPD FEFTDDWHPD DTDNVKDWER
NQFLDLNRPL IMQVWNSDFS KAFYLQQVHQ PRHLPRPARL FGPWYLEIFT MTSWYVVPLI
WLPVAGYLLR QSIIQQTAAG LSTSTALSRS GACFLVGNVI WTFLEYTMHR FLFHIDEHLP
DRPFFLMLHF LLHGIHHYIP MDRMRLVMPP LLFFALQTPF TKLAHKLFPA WMANGIISGA
FVFYVAYDVM HYALHHTKLP EYVRKQKSYH MEHHYKEPEL GFGVTSPFWD RVFGTTFVSR
PKDAPPKLSA KA
//
