ID W1QCU7_OGAPD Unreviewed; 1050 AA.
AC W1QCU7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=HPODL_01644 {ECO:0000313|EMBL:ESW97547.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW97547.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW97547.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) 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:ESW97547.1}.
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DR EMBL; AEOI02000009; ESW97547.1; -; Genomic_DNA.
DR RefSeq; XP_013933632.1; XM_014078157.1.
DR AlphaFoldDB; W1QCU7; -.
DR STRING; 871575.W1QCU7; -.
DR GeneID; 25771103; -.
DR KEGG; opa:HPODL_01644; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_0_0_1; -.
DR OMA; KKWIMRA; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000008673; Chromosome VI.
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 Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 287..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 483..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 173..339
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 1013..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 113444 MW; F29CF6266B7C439B CRC64;
MSSVLANVSA FLAQTCAKRP IHVIIGTALV ASITYLSILD HYASSLSIAS SQPVLFYHPS
GSSDYTKWSQ VENPSAYESA DHYSLTPFKF KRVGGADLPV HDNLLVGMEE NEKILLSDFA
STETLYEKFA TMTNKDGVQF KVRSIHRIGK YYEYLKSLFT KVEGLIKGAE PFDIILVTVA
YGAMWFTFAQ LFFEMKKLGS NFWLAFGSLL SSGIAFLFAL AIGIFLFNLK VPLISLSEGL
PFLVATIGFK HKIAFTKPVL KALRSESNTD IPKTISSVVK STTAIPLIKD QSIIIACFLL
CSILAPNLTG LMNFCIMAAL ILAVDLFFTF TFYSSILSLK AQINKVHKEI ELKQFLEEDG
INETVAESVA ASAELPTDLF RHNSNIVSFK VAMIVGFISL HLFALGTSWL YDDSADYQPI
NLFSTFSPSL SKSVAMNIPI GSHGTLITVM PTRVYSRVDW FTKTEDLALH FFERLSKAIS
DPLVGKFLFV LAGISVAINI YLLNATNAHI DETREIKKKE KKKQRAVEQR KVILKPAPSV
VIPRSSNSSS DDVKEAQIID EGFTDEQSGS DADSLEIKAL TPKRSLEELL GIMKAGNVKE
CSNEEVAELV TSGKLPLYAL EKQLEDKTRA VVVRRKAIAK LADAPVLNTG RLPWKHYDYD
RVFGACCENV IGFMPIPVGV AGPMIIDGVP YHIPMATTEG CLVASTMRGC KAINAGGGVQ
TVLTNDGMTR GPCISFPTLA RSGAAKMWLD SEEGQKVMKS AFNSTSRFAR LQHLQTAMAG
TLLFIRFKTT TGDAMGMNMI SKGVEYALNY MINECGFDDM EIISLSGNYC TDKKAAAINW
IEGRGKSVVA AAIVPAETVR KVLKSDVDAL VELNVSKNLI GSAMAGSVGG FNAHAANLVT
AVYLATGQDP AQNVESSNCI TLMNKLPNGD LQISVSMPSI EVGTIGGGTV LEPQGAMLEL
LGVKGPHPTE PGANARQLAK IVASAVLAAE LSLCSALAAG HLVQSHMTHN RKAPVAGTSA
VDTPATTASS SGSGDDMSRL KDGSKICIRS
//
