ID   DHCR7_MIMIV             Reviewed;         447 AA.
AC   Q5UQI4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Probable 7-dehydrocholesterol reductase;
DE            Short=7-DHC reductase;
DE            EC=1.3.1.21;
DE   AltName: Full=Sterol Delta(7)-reductase;
GN   Name=DHCR7; OrderedLocusNames=MIMI_R807;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Production of cholesterol by reduction of C7-C8 double bond
CC       of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC).
CC       {ECO:0000250|UniProtKB:Q9UBM7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH;
CC         Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113,
CC         ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21;
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV51067.1; -; Genomic_DNA.
DR   RefSeq; YP_003987339.1; NC_014649.1.
DR   SMR; Q5UQI4; -.
DR   GeneID; 9925469; -.
DR   KEGG; vg:9925469; -.
DR   OrthoDB; 29578at10239; -.
DR   UniPathway; UPA00063; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR001171; ERG24_DHCR-like.
DR   PANTHER; PTHR21257:SF38; 7-DEHYDROCHOLESTEROL REDUCTASE; 1.
DR   PANTHER; PTHR21257; DELTA(14)-STEROL REDUCTASE; 1.
DR   Pfam; PF01222; ERG4_ERG24; 1.
PE   3: Inferred from homology;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Probable 7-dehydrocholesterol reductase"
FT                   /id="PRO_0000207508"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         337
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         341
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         367
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         372
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         379..380
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         419
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         423..427
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         434
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ   SEQUENCE   447 AA;  51692 MW;  F338970A8F7AA48D CRC64;
     MNSYQTNTAT SWGRNHIPTL LDNLTTAAMF MFCPFIILVF YLITYGEYLG SIGDFYLDII
     NGDWQTIWSN IPSFKINVLG ACLLWIVFQL ILSKLPDTIH RFVPHYVGGI KAGHITPAGN
     LVYYNINGLQ AFIITHVLVI MSCYYGLFSP TIIMDNWGSI FWSVNIIGYL ITFLAYFKAL
     TFSSHPSDNK FTGKLFYDIV MGIEFNPEIF GTDLKLFFNG RPGIIAWNLI NLSCAMKQYE
     NFGYVSNSMI LVIILQLIYI VDFFYNENWY VHTVDIAHDH FGWMLAWGDT VWLPFGYTLQ
     AGYLMNNPID LSTGFFNLVF VMGIIGYIIF RTANYQKDKY RSNTQGVKYI PCTYQTADGL
     NRASKLIYSG LWGVSRHMNY TGDIILSTAY CLACGFSHFI PYFYCVYMTI LLVTRCLRDE
     QRCSRKYGKY WKMYTKRVPY RFIPGIY
//