ID A0A3M2T5I5_9EURO Unreviewed; 1145 AA.
AC A0A3M2T5I5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=PHISP_04077 {ECO:0000313|EMBL:RMJ25058.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ25058.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ25058.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ25058.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMJ25058.1}.
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DR EMBL; RAQS01000141; RMJ25058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2T5I5; -.
DR STRING; 1960876.A0A3M2T5I5; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000272442; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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; IPR025583; HMG-CoA_N_dom.
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; PF13323; HPIH; 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; PS01192; HMG_COA_REDUCTASE_3; 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000272442};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 491..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 243..427
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 122726 MW; D355B6197816489C CRC64;
MAASFITRKF QPAGKGDDDA ESGWLKRQVT GGLQAISRRA CLHPIHTIVV IALLASTTYV
GLLEGSLFDT FKNPRNVAGQ VDVDTLLLGS RNLRLGENTA WKWQAEDAGM PEDRKTAQHL
ALTTFIFPDS TSKSASTAPA PDDVPLPTNA SIQSVPYTPN LFAPFSHDSS LAFTVPFDHV
AQLLKAMQEI PDLSADEDEA EQKKWIMRAA RGPADGSRRA VKLWMTDAWS SFVDLIKHAE
TIDIIIMALG YISMHLSFVS LFFSMRRLGS KFWLAATVLF SGVFAFLFGL LVTTKLGVPI
SVILLSEGLP FLVVTIGFEK PIILTRAVLN ASADVNRPTS RAGSSSQSNV SQATSGTPRS
IQDSIQTAIK EQGFEIVWGY CIEIAILALG AASGVQGGLR QFCFLAAWIL FFDCVLLFTF
YTTILCIKLE ITRIKRHVTL RKTLEEDGIT HRVAENVASS NDWPVAGTDN SGSVDTSIFG
RKIKSSSVRR FKILMVGGFV LVNVLNLSAI PFRNTGQGAG VPLLSRFSNV FTTTPIDPFK
VAENGLDSVY VSAKSQTLET VVTVVPPIKY KLEYPSVHYA APEETRSFDI EYTDQLIDAV
GGRVIESLLK SIEDPFISKW IIAALSLSII LNGYLFNAAR WSIKESETAP AASKAPPVAE
PKKVYPKIEL NHDGPKRSPE ECERLLKEKQ AALLTDEELI DLSLRGKIPG YALEKTMENE
GLMSRVDAFT RAVRIRRAVV ARTSATPTTG SLEKSKLPYK DYNYTLVHGA CCENVVGYLP
LPLGVAGPLT IDGQNYFIPM ATTEGVLVAG ASRGCKAINA GGGATTVLTA DGMTRGPCVG
FPTVARAAAA KVWIDSEEGK RIMTTAFNST SRFARLQYMR TALAGTYLFI RFKTTTGDAM
GMNMISKGVE RSLHVMATEC GFDDMATISV SGNFCTDKKP AAINWIDGRG KSVVAEAIVP
GEVVRSVLKS DVNALVELNT SKNLIGSAMA GSMGGFNAHA SNIVTAIFLA TGQDPAQNVE
SSSCITTMKN TDGNLQISVS MPSIEVGTIG GGTILEGQSA MLDVLGIRGS HPTNPGDNAR
MLARIVAASV LAGELSLCAA LAAGHLVNAH MALNRGTSSA GPTRSSTPVS AAVGAARGMA
MTAPK
//
