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Delta(7)-sterol 5(6)-desaturase (EC 1.14.19.20) (C-5 sterol desaturase) (Ergosterol Delta(5,6) desaturase) (Sterol-C5-desaturase)

 ERG3_CANDC              Reviewed;         386 AA.
Q8NJ57; B9W7Q0;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
10-MAY-2017, entry version 77.
RecName: Full=Delta(7)-sterol 5(6)-desaturase;
EC=1.14.19.20;
AltName: Full=C-5 sterol desaturase;
AltName: Full=Ergosterol Delta(5,6) desaturase;
AltName: Full=Sterol-C5-desaturase;
Name=ERG3; ORFNames=CD36_04520;
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF
3949 / NRRL Y-17841) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=573826;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12878500; DOI=10.1128/AAC.47.8.2424-2437.2003;
Pinjon E., Moran G., Jackson C.J., Kelly S.L., Sanglard D.,
Coleman D., Suulivan D.J.;
"Molecular mechanisms of itraconazole resistance in Candida
dubliniensis.";
Antimicrob. Agents Chemother. 47:2424-2437(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
PubMed=19745113; DOI=10.1101/gr.097501.109;
Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D.,
Harris D., Aslett M., Barrell J.F., Butler G., Citiulo F.,
Coleman D.C., de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J.,
Munro C.A., Pain A., Poulter R.T., Rajandream M.A., Renauld H.,
Spiering M.J., Tivey A., Gow N.A.R., Barrell B., Sullivan D.J.,
Berriman M.;
"Comparative genomics of the fungal pathogens Candida dubliniensis and
Candida albicans.";
Genome Res. 19:2231-2244(2009).
-!- FUNCTION: Catalyzes the introduction of a C-5 double bond in the B
ring of ergosterol. May contribute to the regulation of ergosterol
biosynthesis. {ECO:0000250|UniProtKB:P32353}.
-!- CATALYTIC ACTIVITY: A Delta(7)-sterol + 2 ferrocytochrome b5 +
O(2) + 2 H(+) = a Delta(5,7)-sterol + 2 ferricytochrome b5 + 2
H(2)O. {ECO:0000250|UniProtKB:P32353}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol
from zymosterol: step 3/5.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding.
-!- SIMILARITY: Belongs to the sterol desaturase family.
{ECO:0000305}.
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EMBL; AJ421248; CAD13131.1; -; Genomic_DNA.
EMBL; FM992688; CAX44711.1; -; Genomic_DNA.
RefSeq; XP_002417121.1; XM_002417076.1.
STRING; 573826.XP_002417121.1; -.
EnsemblFungi; CAX44711; CAX44711; CD36_04520.
GeneID; 8044658; -.
KEGG; cdu:CD36_04520; -.
CGD; CAL0000162230; ERG3.
eggNOG; KOG0872; Eukaryota.
eggNOG; COG3000; LUCA.
HOGENOM; HOG000200579; -.
KO; K00227; -.
OrthoDB; EOG092C3V4R; -.
UniPathway; UPA00768; UER00762.
Proteomes; UP000002605; Chromosome 1.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR006694; Fatty_acid_hydroxylase.
Pfam; PF04116; FA_hydroxylase; 1.
3: Inferred from homology;
Complete proteome; Endoplasmic reticulum; Iron; Lipid biosynthesis;
Lipid metabolism; Membrane; Oxidoreductase; Steroid biosynthesis;
Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
Transmembrane; Transmembrane helix.
CHAIN 1 386 Delta(7)-sterol 5(6)-desaturase.
/FTId=PRO_0000117021.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TRANSMEM 272 292 Helical. {ECO:0000255}.
MOTIF 226 230 Histidine box-1.
MOTIF 239 243 Histidine box-2.
MOTIF 314 318 Histidine box-3.
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


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