ERG24_SEPLY
ID ERG24_SEPLY Reviewed; 512 AA.
AC O13597;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 65.
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;
GN Name=ERG3;
OS Septoria lycopersici (Tomato leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Septoria.
OX NCBI_TaxID=39703;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Aparna K.;
RL Submitted (JUL-1997) 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 {ECO:0000250}.
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; Y14389; CAA74747.1; -; Genomic_DNA.
DR AlphaFoldDB; O13597; -.
DR SMR; O13597; -.
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..512
FT /note="Delta(14)-sterol reductase"
FT /id="PRO_0000207498"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 380
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 384
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 407
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 412
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 419..420
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 484
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 488..492
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 499
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 512 AA; 57578 MW; 169A756E60C0E963 CRC64;
MARTKATARK TVPAQQEAHG YEFGGPIGAS LISFGLPIAC YAFGFLCNDV SGCPPPSLLS
PSKLFTPPTL SNKVPWQHAL DTLAAEVGWP GWSGLINTEA VLGVFFWYGL SLLLWVLLPA
HEVEGTELRT GGRLKYRFNA CLSAVTIFVA CAAGTIVRGP DFQVWTFINR NYIQLLTVNI
IIAYALAIYV YLKSFEVKAG NTEQRELAAG GHSGHILYDW YMGRELNPRI TIPFIGEVDI
KSFMELRPGM IGWVLLDLAF AAKQYKSYGY ITDSMRKWTP LLLGIHVLTI HPVIVIISQS
VYVFDALYME PAILTTMDLT TDGFGFMLSF GDLVWVPFIY SIQAKYLSVH PVALGPLYVA
LILTIQATGY YIFRATNNDK NIFRTNPNDP KVAHLKYIET GTGSRLLTTG WWGTARHINY
LGDWLMSWSY CLPTLAAGYK LTPTILFENS RLVSTDGMKG AGIPITYFYM LYFAILLIHR
ERRDEAKCRR KYGAHWEKYC QIVRWRILPG VY
