ID   ERG3_LEPMC              Reviewed;         356 AA.
AC   Q8J207;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 63.
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;
OS   Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=5022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12445649; DOI=10.1111/j.1574-6968.2002.tb11459.x;
RA   Griffiths K.M., Howlett B.J.;
RT   "Transcription of sterol delta 5,6-desaturase and sterol 14alpha-
RT   demethylase is induced in the plant pathogenic ascomycete, Leptosphaeria
RT   maculans, during treatment with a triazole fungicide.";
RL   FEMS Microbiol. Lett. 217:81-87(2002).
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; AY137770; AAN27998.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J207; -.
DR   UniPathway; UPA00768; UER00762.
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..356
FT                   /note="Delta(7)-sterol 5(6)-desaturase"
FT                   /id="PRO_0000117023"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          179..303
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           192..196
FT                   /note="Histidine box-1"
FT   MOTIF           205..209
FT                   /note="Histidine box-2"
FT   MOTIF           280..284
FT                   /note="Histidine box-3"
SQ   SEQUENCE   356 AA;  41708 MW;  789D803116DB800B CRC64;
     MDIVLEVCDT FLFDPLYATL LPAQASSFTA NATANATLSS IRQEPTAYAL PHASWQYEPA
     TKYFSIEPSK YAYMSSWPRD DWRRQALTLY LITWLFGVCV YYLFAGLSYL LVFDKATFNH
     PRYLKHQIKL EMKQANIAFP IMAIFTVPWF LAEVRGYSKL YDTTEKGPGR WYDYLQIPFF
     IAFTDLCIYW IHRGLHHPMV YKHIHKPHHK WIMPTPFASH AFHPIDGYAQ GLPYYIFPFL
     FPLSKIASVA FFVFVNIWTV LIHDGEYAHN SPIINGAACH TMHHLYFNYN YGQFTTLWDR
     LGGSYRKPND ELFKRELKMC QDEWNKQAKA VDMMVEQVEG ENDRSYQGEP ESKKVQ