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Database: UniProt
Entry: A0A2K0WQQ5_GIBNY
LinkDB: A0A2K0WQQ5_GIBNY
Original site: A0A2K0WQQ5_GIBNY 
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
//
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