ID   ERG24_FUSVN             Reviewed;         485 AA.
AC   Q01447;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Delta(14)-sterol reductase;
DE            EC=1.3.1.70;
DE   AltName: Full=C-14 sterol reductase;
DE   AltName: Full=Sterol C14-reductase;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MP VI;
RA   Srinivas G., Vanetten H.D., Kasbekar D.P.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-
CC       8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC         4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC         Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC         ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 2/6.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR   EMBL; X94315; CAA63976.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01447; -.
DR   SMR; Q01447; -.
DR   UniPathway; UPA00770; UER00755.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050613; F:delta14-sterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001171; ERG24_DHCR-like.
DR   InterPro; IPR018083; Sterol_reductase_CS.
DR   Pfam; PF01222; ERG4_ERG24; 1.
DR   PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR   PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..485
FT                   /note="Delta(14)-sterol reductase"
FT                   /id="PRO_0000207496"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         346
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         350
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         373
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         378
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         385..386
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         457
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         461..465
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         472
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ   SEQUENCE   485 AA;  54597 MW;  45A828AD154B02B6 CRC64;
     MALKSSKAVS EEQHGYEFFG PPGAFAISFL LPVLVYVFNF VCNDISGCPA PSLLSPKTLS
     LDKLKQEVGW PQDGFAGLVS WEASAATAGY ILLSLILYRV LPAHEVEGTE LRSGGRLKYR
     LNTLYSSSFT LAILAAGTAA QGAEFPVWTF ISDNFIQILT ANTIFSYAVA TFVYVRSFSV
     KPGNKENREL AAGGHTGNML YDWFIGRELN PRVVIPLIGE VDLKEWLELR PGMMGWIIFN
     CSWCAQQYRN YGYVTDSSIC ITLVQAVYVF DSWWNEPAIL TTMDITTDGF GMMLAFGDIV
     WVPFVYSLQT RYLAVHPVSL GPVGLAVMLS LIGLGFYIFR SANSEKNNFR TNPNDPKVSQ
     LKYIQTKKGS KLLISGWWGI ARHINYLGDW IQSWPYCLPT GLAGYQILNA GAQAEGALVM
     RDGREVVQGE AKGWGMLITY FYILYFAILL IHRERRDDDK CHRKYGEDWE KYRKIVRYRI
     IPGIY