ID A0A1C1CLX1_9EURO Unreviewed; 1149 AA.
AC A0A1C1CLX1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=HMGR {ECO:0000313|EMBL:OCT49506.1};
GN ORFNames=CLCR_06581 {ECO:0000313|EMBL:OCT49506.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT49506.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT49506.1}.
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DR EMBL; LGRB01000010; OCT49506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CLX1; -.
DR STRING; 86049.A0A1C1CLX1; -.
DR VEuPathDB; FungiDB:CLCR_06581; -.
DR VEuPathDB; FungiDB:G647_09768; -.
DR eggNOG; KOG2480; Eukaryota.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000094526; 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:UP000094526};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 402..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 239..424
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 638..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 123479 MW; C65936EA2EA2A4FE CRC64;
MVRGSSLLPK QLRSLGKSDG WLNRTVTSNL LAVSSLACAH PIHTVVAIAL FASTSYVGLL
QESLFDSGLK SLQQNGRVDV EALLQGSRTL ELSEKTAWKW QFPEDSSVPQ VSLGPNHYAI
STFVFPDSSS NQLAPDVTAV STPANVTAIN IPTTSNLLSP ISHDTSLAFY TSFSELADFL
RTAQELPAQQ ARSEEQRKPS WFMKAARLNG NGPRGAYTTW FREGWTSFVD LLKHAETLDI
IIMSLGYLSM HLTFLSLFVS MKRLGSNAWL AVSVLFSSLF AFLFGLVTTT KLGVPINMVL
LSEGLPFLVV TVGFEKSIIL TKAVLSASYD KNRRSLENGS ANGGANGPVV APNSPSSIQD
AIQIAVRETG FEIVRDYAIE IAILILGAAS GIQGGLRQFC FLAAWILVFD CLLLFTFYAT
ILCIKLEINR IKRHVALRKA LEEDGINQRV AEDVATNNDW PTGQSGQAAG FNIFGQKIKA
NSVPKFKIWM VTGFVIINLV NLCTIPFRTA KAPGAAMPSV LTPAPIDPFK VAENGLDAIY
VTAKSQKQET YVTVLPPIKY ELDYPHLPRA DAADDLGFFD TDYTDQLLNV VGGRVIEGVL
SSLEDPVLSK WVLIALTLSL ILNGYLFNAA RWSLKEPQST TSSPAAQKAP ELELPLTPKP
RRTTVTAPAQ SQRSPAEREQ MLKEKKAAYL TDEELIDLSL KGKIPGYAIE KTLENAEVMS
RREAFVRAVK VRRAVVSRTP ATKHVAAGLE ISKAPYKDYN YELVHGACCE NVIGYLPLPL
GVAGPIIIDG LQYFLPMATT EGVLVASTSR GCKAINAGGG AVTVVTGDGM TRGPCVGFPT
LVRAGEAKVW LDSDEGQQRM REAFNSTSRF ARLQSMKTAM AGTYLYIRFK TTTGDAMGMN
MISKGVEKAL SVMATECGFE DMSTITISGN YCTDKKPAAV NWIDGRGKAV VAEAVIPADV
VRNVLKSDVD ALVELNVSKN LIGSAMAGSI GGFNAHASNI VTAIFLATGQ DPAQNVESSN
CITIMKNLNG NLQISVSMPS IEVGTIGGGT ILEAQSSMLE MLGVRGSHPT NPGDNARKLA
RIVAAGVLAG ELSLCSALAA GHLVKAHMAH NRSTVPTRAT TPVSAAVEPF LRAQNGPSIP
SSLKMTTGK
//
