ID A0A1E5RKM1_9ASCO Unreviewed; 1037 AA.
AC A0A1E5RKM1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
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=AWRI3578_g2306 {ECO:0000313|EMBL:OEJ87394.1};
OS Hanseniaspora opuntiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ87394.1, ECO:0000313|Proteomes:UP000095605};
RN [1] {ECO:0000313|Proteomes:UP000095605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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:OEJ87394.1}.
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DR EMBL; LPNL01000004; OEJ87394.1; -; Genomic_DNA.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000095605; 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 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 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 Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 223..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 252..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 336..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 191..361
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1037 AA; 115047 MW; A4FE0C6103817D63 CRC64;
MPLLFKKTAV MGKPIAEFSK FAAKHPFQII LSTLLITAFA YVRVIEYFRN GWSLDTSSVF
HAMNLNQVES KDFLYNSSTN SLQPLNFTNG QIAANLEVYS TLPKIYVTEL EFKSTEPVKC
PIKEIDDITF ASTXNSRFVV QSQFDLPYTV SLDDVVYQLR PQKNKLLQFI NFATVLKECL
LEKLQTSDPT DVFVIGSAYL GMFYTFVKLF YDMRKTGGSK XWIGLFTLVS SGCALFLALY
FCIHVLEKPV TLLSLIEGLP FIVIIIGFKH KVKLAEFTLK EYSKSKFGNK TNVPSVMVYH
AMLQEGGRLV QDYAICLATF IGCAALTSFI EILQNFSYLV CLILVLDVVL TSTFFCSVLS
LKLEIQMINR STAMEQVLEE DGVLEETAEI ISGQNEVLEN ASIFTSHTII TFFKLAVLLA
FVFLHFYNFG YRWTYETFNS LYPKMSNDES MMYLLQKDFQ VDFDCIVFLV AKQYYEQPKL
IFHVEDYALL TYNYISLAIR DKYLSKFLLV CFLFSCSINV YLLNNARIHT TMTVKKFLNK
KLKKNEPVPV VKPVVYPTEG TRLSKNLSLE DDESEPVXSV EDALKXYKEG NVSTLNNREI
VSLVVNKHLP LYALEKQLKD TTRAVVVRRK ALAKLASAPL LETESLPYKY YDYDRVFGAC
CENVIGFMPL PVGVIGPMII DDVPYHIPMA TTEGCLVASA MRGCKAINAG GGVTTVLTKD
GMTRGPCVRF GSLKRSGMCK IWIDSEEGQS KIKKAFNSTS RFARLQNVQT ALAGDLLFLR
FRTTTGDAMG MNMISKGVEY ALKQMVEEFG WEDMEVVSVS GNYCMDKKPG AINWIEGRGK
SVVAEATIPK DVVSKVLKSE VKALVELNIS KNLIGSAMAG SVGGFNAHAS NLVTAVFLAL
GQDPAQNVES SNCITLMKET PEGDLRISVS MPSIEVGTIG GGTILGPQGA MLDLLGVRGP
HPTEPGTNSR QLAKIVASAV LAGELSLCSA LAAGHLVQSH MVHNRAKPVA DSSATAKEMS
EDKLKVLKEG SVTCIKS
//
