ID W9XRW3_9EURO Unreviewed; 1149 AA.
AC W9XRW3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 42.
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=A1O1_06916 {ECO:0000313|EMBL:EXJ83297.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ83297.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ83297.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ83297.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-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:EXJ83297.1}.
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DR EMBL; AMWN01000006; EXJ83297.1; -; Genomic_DNA.
DR RefSeq; XP_007725983.1; XM_007727793.1.
DR AlphaFoldDB; W9XRW3; -.
DR STRING; 1182541.W9XRW3; -.
DR GeneID; 19161782; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_0_0_1; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000019484; 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 Reference proteome {ECO:0000313|Proteomes:UP000019484};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 483..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 238..421
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 637..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 123260 MW; 534F2178DF8B178A CRC64;
MRGSSLLPKQ LRSLGRSDSW LNRTVTSGLL ALSHTACQHP IHTIVVLALL ASTSYVGLLQ
ESLFDTGVKT IQQNGRVDVE ALLKGSRTLE LSEKTAWKWD FADDYGVPQV SLGADHYALV
TLLFPDSSSL QLAPEAHDVP IPSNITATNV PTTSNLLSPI SHDTSLAFYT SFSEVADFLR
AAQELPARNT ESEGNGDGVW LMKAARLNGL GSRGSYRAWL SEGWSSFVDL VKHAETLDII
IMSLGYLSMH LTFISLFVSM KRLGSNAWLA ISVLFSSLFA FLFGLVTTTK LGVPINMVLL
SEGLPFLVVT IGFEKSIILT KAVLSASYDT SRRPDSSANG AATGPFAQPY AASSIPDAIQ
MAVKDTGFEV VRDYAIEIAV LILGAASGVQ GGLRQFCFLA AWILAYDCLL LFTFYTTILC
IKLEINRIKR HVALRKALEE DGINQRVAEN VATNNDWPSG QSDQGAGFNI FGQKIKASSV
PKFKIWMVTG FVIVNIINLC TIPFRTASSV KATGPTIPSM LTPAPIDPFK VAENGLDAIY
VAAKSKKIDT FVTVLPPIKY ELDYPSLHQP GAQDDLGFFE HEYTDQFLNV MGGRVIEGVL
KSLEDPVLSK WVLIALTLSL ILNGYLFNAA RWSLKEPHST TSSPSAPKPP QLELPQAPKP
KPVDLAGANE LTRSQAECEQ MLKEKNAAYL TDEELIDLSM RGKIPGYAIE KTLENPEAMT
RLESFVRAVK VRRAVVSRTP ATKRFAGVLE SSKVPYKDYN YELVLGACCE NVIGYLPLPL
GVAGPLTIDG QSYFLPMATT EGVLVAGVSR GCKAINAGGG AVTILTNDGM TRGPCVGFPT
LARAAEAKVW LDSEDGWRRI RDAFNSTSRF ARLQSLKTAL AGTYLYIRFK TTTGDAMGMN
MISKGVEKAL SVMSTECGFD DMSTIAVSGN YCTDKKAAAI NWIDGRGKGV VAEAIIPGDV
VRSVLKSDVN ALVELNIAKN LIGSAMAGSI GGFNAHAANI VAAMFLATGQ DPAQVVESGN
CITVMKNNNG NLQISVSMPS LEVGTIGGGT ILEAQSTMLE MLGVRGAHPT NPGDNARQLA
RIISAGVLAG ELSLCSALAA GHLVRAHMAH NRSAAPTRTS TPVSAAVEPF LRAQNGPSIP
SSLKMTNGR
//
