ID B6K500_SCHJY Unreviewed; 1060 AA.
AC B6K500;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase {ECO:0000256|RuleBase:RU361219};
DE Short=HMG-CoA reductase {ECO:0000256|RuleBase:RU361219};
DE EC=1.1.1.34 {ECO:0000256|RuleBase:RU361219};
GN Name=hmg1 {ECO:0000313|JaponicusDB:SJAG_03715};
GN ORFNames=SJAG_03715 {ECO:0000313|EMBL:EEB08557.2};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08557.2, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB08557.2, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
CC Evidence={ECO:0000256|RuleBase:RU361219};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC {ECO:0000256|RuleBase:RU361219}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361219}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU361219}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00007661, ECO:0000256|RuleBase:RU361219}.
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DR EMBL; KE651167; EEB08557.2; -; Genomic_DNA.
DR RefSeq; XP_002174850.2; XM_002174814.2.
DR AlphaFoldDB; B6K500; -.
DR STRING; 402676.B6K500; -.
DR EnsemblFungi; EEB08557; EEB08557; SJAG_03715.
DR GeneID; 7052231; -.
DR JaponicusDB; SJAG_03715; hmg1.
DR VEuPathDB; FungiDB:SJAG_03715; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_0_0_1; -.
DR OMA; KKWIMRA; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblFungi.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 1.10.3270.10; HMGR, N-terminal domain; 1.
DR Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR InterPro; IPR023282; HMG_CoA_Rdtase_N.
DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR InterPro; IPR000731; SSD.
DR NCBIfam; TIGR00533; HMG_CoA_R_NADP; 1.
DR PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR PANTHER; PTHR10572:SF24; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361219};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361219};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU361219};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361219};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 270..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 323..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 348..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 428..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 211..375
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1060 AA; 115357 MW; 5113615C733BF18E CRC64;
MKDNPNMLYR CAARYPIQVI VTVFILAAFS YVSFFDTITR QELPALARTL EQWNLFDRLP
KNKGEPAPYL VAESSFDSET GAQNWELVFE TDNENQVDYG LIEVFRPAGQ ETTFSMGFLE
THVNASAESF TSGRDSYVKL GTSNMSLLNT VMPIKSAQKV VEETPSISDL LLQRLLPAIQ
KHTFSLTWTL RFLGNAWMHV FKLASHASTT ELVLVGTAYV CMIVSIISLL TNMRRLGSRI
WLSVSALLCV MIAIQLAISC QQVIGGHVDF YSVVEAVPFI VNAIGFEKPL SLARAVIPEC
SIKSTNPLHE EVAKACSRAT KPLLRHFGVS MLVLGVFSYV NFGVNQFAFF TTVLVIEMLL
NVTFFVSFLT LKLELRRFKV SSNLHKALVE EGFSESTATS VVRSSEQQTK SNVEKGFSIK
RCIASIRTVL LIGFVGINLF KLCSVSFPSY KNLSNSNQCM PLSTYNLDVT VNFFKQNAFQ
SVLAKLPAQV HEHATRVRFL PPIICQAPPP ATKSESYSVL KDIYRLFTGT VLPKWFMIGF
AFSIAANVYL LNVARVYIQK SNNSNKPAKT KEKIVEVVKR IHVSTPSAAP PVTDPKDVVV
RPLTECVELY KGGKVSELND EEIVSLVLAK KIPLYALEKV LKDLERAVYI RRIAVSRTSS
TKTLETSAIP VYNFDYARVL NACCENVIGY MPLPLGVAGP LIIDGKSYYI PLATTEGALV
ASAMRGCKAI NAGGGATTIL TRDEMARGPC ITFPTLSRAG FAKMWLDSPE GQEVVKNAFN
STSRFARLQH LKTALAGTRL YVRFCTSTGD AMGMNMISKG VEHALAVMCN EAGFEDMKVV
SVSGNYCTDK KPAAINWIEG RGKSVVAEAI VPAKAVESIL KTTVDDLVQL NINKNLIGSA
MAGCVGGFNA HAANLVTAIF LATGQDPAQN VESSNCITLM DNVNGNLRIS VSMPSIEVGT
IGGGTVLEPQ AAMLDLLGVR GPHPTNPGSN ARQLARIVAA GVMAGELSLC SALASGHLVK
SHIGLNRSAL NTPVAGTSAN KQPPVDLLSA INRARQPAKN
//
