ID W0TEE1_KLUMD Unreviewed; 1073 AA.
AC W0TEE1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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|EMBL:BAO40469.1};
GN ORFNames=KLMA_40445 {ECO:0000313|EMBL:BAO40469.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO40469.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO40469.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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; AP012216; BAO40469.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TEE1; -.
DR SMR; W0TEE1; -.
DR VEuPathDB; FungiDB:KLMA_40445; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000065495; Chromosome 4.
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 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 308..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 332..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 192..360
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 543..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 117385 MW; 44D175973187211E CRC64;
MPVLFKQFKH MAKPFAYVAR FSAKHPIHVI LVTLLFAATT YLSVIEYYFN GWTIENKTVS
YHGSNSANSL KHDSLHFHYT PKDSQWSALS EEDFEKMKYQ STPLAHYYLL GFEFHSDNES
LVLPEIEGNV YEEGSIKYLL TDEPVISKTL KSKDDTTWTL RAHRHKLLDV KAGVLALYKE
LEERINSAEP FDIFIVGSAY VAMVYTLISL FLDMRVTGSK FWIALAAIIN SGSAFFMALY
TSQKIYHRPV TALSLIEGLP FVIVVVGFKD KIKLAKYVVD QFKRFDVSQK VTTYQVVYDA
MIQEGGRLVQ DHLLCVIAFG GCSIYASSLS ALSNFCFFCG LLLAYDLILT SSFFAAVLAL
KLEISIIHKA TTIKQTLEED GVVPSTAGII SKSETLKKNR VLKSSSSLLV GKLLFVTGFI
GFNLYNFGTR WTYETFSSLY SKSHTNELPA FVTSIIAKEN SEAVVSLVPP QFYEPAKTYF
QVEDGVLSLI RYISVAIRDR FVSKVLIFAL IMSASINVYL LNAARIHTEL TANDIQKKRA
AKLVPKPYSN HNEKQSPSSS ASNETKVETV TERMPVVASI QHEIDTESDS DNGSSEVRPV
EELVDVLKSG DVKSLSNREV VSLVVANKLP LYALEKQLGD TTRAVVVRRK ALAILADAPV
LATERLPYKN YDYNRVFGAC CENVIGYMPL PVGVIGPLMI DGVYYHIPMA TTEGCLVASA
MRGCKAINSG GGVTTVLTKD GMTRGPCVRF PSLKRAGACK IWLDSEEGQN KIKKAFNSTS
RFARLQHVQT ALAGDLLFIR FRTTTGDAMG MNMISKGVEF SLHQMVEEYG WKDMEIVSVS
GNYCMDKKPA AINWIEGRGK SVVAEANIPG DVVRKVLKSD VKALVDLNIS KNLIGSAMAG
SIGGFNAHAS NLVTAVYLAL GQDPAQNVES SNCMTLMKEV DGDLRISVSM PSIEVGTIGG
GTILEPQSAM LDLLGVRGPH PTEPGKNARQ LAKIVASAVM AGELSLCSAL AAGHLVQSHM
VHNRAKQPVA TGAGAPVSGP GPVSTPAIAT NGKELSAEQL KTLKEGSVIC IKS
//
