ID A0A094B6C8_9PEZI Unreviewed; 1050 AA.
AC A0A094B6C8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 37.
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};
DE Flags: Fragment;
GN ORFNames=V494_04810 {ECO:0000313|EMBL:KFY37311.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY37311.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY37311.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY37311.1}.
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DR EMBL; JPJW01001628; KFY37311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094B6C8; -.
DR STRING; 1420907.A0A094B6C8; -.
DR HOGENOM; CLU_001734_0_0_1; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000029288; 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; 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:UP000029288};
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..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 294..314
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 239..421
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1050
FT /evidence="ECO:0000313|EMBL:KFY37311.1"
SQ SEQUENCE 1050 AA; 112459 MW; A97E1E0FBBB80F71 CRC64;
MIASLLPARF RGPQDTKTNA QPGWLNKNIT PLLQALSRKA CMHPIHTVVI VAFLASTTYM
GLLEGSLDGF PTAGKADWGS LVEGSRQLYA GKDTAWKWQA QDADAPIPSE AERLALLTFV
FPGSLSSSSP DAPLSHTVPL PDNLSITSLP STSNPLASIS QDSTLAFSIP YTQAPEFLAS
AQEIPNVDSE AESLGSQEQK LWIMRAAKAS GASSGSLRLW AVSAWSKFVD LLKNAETLDI
FIMVLGYIAM HLTFVSLFLS MRRMGSNFWL ATTVLFSSSF SFLFGLIVTT KLGVPINMVL
LSEGLPFLVV TIGFEKAIVL TKAVLSVAVD SRRAPAPNSP DSGKDDKEGT SPPSIQHAVQ
VAIKEKGFEI VRDYAIEIAI LIAGAVSGVQ GGLQQFCFLA AWILFFDCIL LFTFYTSILS
IKLEVNRIKR HVALRRALED DGLSQRLAEN VAQSNDWPRP GGEADGKTNI FGRKVKDSSV
PKFKVLMVTG FVIVNVINLA TIPFRSSKNS SAASSVSGIA TPGFSALDPF KVASSGLDAI
LATAKSSGTP TVVTVLSPIK YSLEYPSIHY ATHHGQRGPY SIEYGGSASD YGMGGRVVDS
LLKSLEDPVL SKWIMVALVL SVVLNGYLFN AARWSIKEPE TPTLAIDPIA LEKAQRLTED
RAAPPAQFDE STRPTDRLPT PANTDDEGDL VILPKATANG SAALRRTPEQ VDKMLLDKRA
PELNDKELIE LSLSGKLPGY ALERTLKDTT RAVKIRRAVV ARTAATSHTT SLLEGSKLPY
EHYNWDRVLG ACCENVIGYM PLPVGVAGPI VIDGQSYFLP MATTEGVLVA STSRGAKAIN
AGGGAITVLT GDGMTRGPCI GFDTLERAGA AKNWLDSEAG QKTMKKAFDS TSRFARLQTM
KTAIAGTYLY IRFKTSTGDA MGMNMISKGV EHALKVMSTE SGFDDMQIIS VSGNYCTDKK
PAAINWIDGR GKGVVAEAII PADVVRKVLK SEVDALVELN ISKNLIGSAM AGSIGGFNAH
AGNIVTAIFL ATGQDPAQNV ESSNCITIMK
//
