ID A0A2K0WQQ5_GIBNY Unreviewed; 383 AA.
AC A0A2K0WQQ5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Ceramide very long chain fatty acid hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN ORFNames=FNYG_02236 {ECO:0000313|EMBL:PNP84607.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP84607.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP84607.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP84607.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PNP84607.1}.
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DR EMBL; MTQA01000039; PNP84607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WQQ5; -.
DR STRING; 42673.A0A2K0WQQ5; -.
DR OrthoDB; 208810at2759; -.
DR Proteomes; UP000236664; 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 InterPro; IPR013087; Znf_C2H2_type.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW 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|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW 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:UP000236664};
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 196..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..85
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 94..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
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 68
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; 43991 MW; 66D9499A76427570 CRC64;
MPGRTLPTFT RAEVEAHNSG DSCYVTIGNK VYDITDFVED HPGGPEYILE YAGRDIEEIL
KDSDSHTHSD SAYEILDESL VGFLVSEKAV NGHANGKANG NGNAKLPNGE ANGDANGSVH
PRTGMSCAED LSKDTDYNLD YKKNKFLDLN RPLFPQIWFG GFSKEFYLDQ VHRPRHYKGG
QSAPLFGNFL EPLSKTAWWV VPMIWLPCVA YGTWVASQGF DNQLYTLGYW LFGVFFWTII
EYVLHRFLFH LDYYLPDNRV GITLHFILHG IHHYLPMDKY RLVMPPTLFA ALAAPFWRFA
HAVLFHNWYA ACAAYCGGIF GYVCYDLTHY FLHHQDLPLW YKELKKYHLA HHFLDYELGF
GVTSKFWDSV FGTELIYNTK KTK
//