ERG3_CANDC
ID ERG3_CANDC Reviewed; 386 AA.
AC Q8NJ57; B9W7Q0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Delta(7)-sterol 5(6)-desaturase;
DE EC=1.14.19.20;
DE AltName: Full=C-5 sterol desaturase;
DE AltName: Full=Ergosterol Delta(5,6) desaturase;
DE AltName: Full=Sterol-C5-desaturase;
GN Name=ERG3; ORFNames=CD36_04520;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12878500; DOI=10.1128/aac.47.8.2424-2437.2003;
RA Pinjon E., Moran G., Jackson C.J., Kelly S.L., Sanglard D., Coleman D.,
RA Suulivan D.J.;
RT "Molecular mechanisms of itraconazole resistance in Candida dubliniensis.";
RL Antimicrob. Agents Chemother. 47:2424-2437(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- FUNCTION: Catalyzes the introduction of a C-5 double bond in the B ring
CC of ergosterol. May contribute to the regulation of ergosterol
CC biosynthesis. {ECO:0000250|UniProtKB:P32353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:138130,
CC ChEBI:CHEBI:138131; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:P32353};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from
CC zymosterol: step 3/5.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AJ421248; CAD13131.1; -; Genomic_DNA.
DR EMBL; FM992688; CAX44711.1; -; Genomic_DNA.
DR RefSeq; XP_002417121.1; XM_002417076.1.
DR AlphaFoldDB; Q8NJ57; -.
DR STRING; 42374.XP_002417121.1; -.
DR EnsemblFungi; CAX44711; CAX44711; CD36_04520.
DR GeneID; 8044658; -.
DR KEGG; cdu:CD36_04520; -.
DR CGD; CAL0000162230; ERG3.
DR VEuPathDB; FungiDB:CD36_04520; -.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_3_0_1; -.
DR OrthoDB; 1249774at2759; -.
DR UniPathway; UPA00768; UER00762.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:UniProt.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Oxidoreductase; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Delta(7)-sterol 5(6)-desaturase"
FT /id="PRO_0000117021"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 214..337
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 226..230
FT /note="Histidine box-1"
FT MOTIF 239..243
FT /note="Histidine box-2"
FT MOTIF 314..318
FT /note="Histidine box-3"
SQ SEQUENCE 386 AA; 45646 MW; 64EDEE7FF2D05C11 CRC64;
MDIVLEICDY YLFDKVYADV FPKDGPVHEY LKPAIQSFSE INFPKLQNWD SFDTNSTLIS
SNNFNISNVN PATIPGYLLS KIASYQDKSE IYGLAPKFFP ATEFIDTSFL SRSNIFREVL
SLFIITTLFG WLLYFIVAYL SYVFVFDKKI FNHPRYLKNQ MSLEIKRATS AIPVMVLLTI
PFFLLELHGY SFLYEEINES TGGYKAILWQ IPKFILFTDC GIYFLHRWLH WPSVYKALHK
PHHKWIVCTP FASHAFHPVD GFFQSLPYHL YPLLFPLHKV LYLLLFTFVN FWTVMIHDGS
YWSNDPVVNG TACHTVHHLY FNYNYGQFTT LWDRLGNSYR RPDDSLFVKD QKKEEEKKIW
KEQTRQMEEI RGEVEGKVDD REYIDQ
