ID G1XJ45_ARTOA Unreviewed; 383 AA.
AC G1XJ45;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ceramide very long chain fatty acid hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN ORFNames=AOL_s00097g372 {ECO:0000313|EMBL:EGX46946.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX46946.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX46946.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX46946.1}.
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DR EMBL; ADOT01000174; EGX46946.1; -; Genomic_DNA.
DR RefSeq; XP_011124507.1; XM_011126205.1.
DR AlphaFoldDB; G1XJ45; -.
DR STRING; 756982.G1XJ45; -.
DR GeneID; 22895424; -.
DR eggNOG; KOG0539; Eukaryota.
DR HOGENOM; CLU_034756_0_1_1; -.
DR InParanoid; G1XJ45; -.
DR OMA; WTIIEYV; -.
DR OrthoDB; 208810at2759; -.
DR Proteomes; UP000008784; 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:UP000008784};
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 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..90
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT BINDING 46
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 73
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 383 AA; 43292 MW; 8C98338ACD5215D8 CRC64;
MITTMPSANL PTFTLAELAK NHSSKKSCYV TLGTKVYDLT DFLPDHPGGD DLILDYAGKD
ISDIIADPQS HVHSDAAYEI LDDSLVGFLS PEDAKLANGS ANGSTNGAAK TSAVPNGNPT
YEATGMSTAE DLSVETDITN DFKTHKFIDL DKPMFMQVWR GRFSKEFYLK QVHRPRHYKG
GDSAPLFGNF LEPLSKTAWY VIPIIWLPCV AYGLWMAGQG LTPEKLALCF ASGIAIWTLV
EYVLHRFLFH LDEYLPDNNV AITLHFLLHG IHHYLPMDRY RLVMPPTLFI ALATPFWKLA
HTLFAHNWYV GTGVFCGGIF GYICYDLTHY FLHHKKLPSY YQELKKYHLQ HHFADYENGF
GVTSRFWDRI FGTELPPLPQ KTA
//
