ID A0A0P7BRD5_9HYPO Unreviewed; 1238 AA.
AC A0A0P7BRD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=AK830_g3499 {ECO:0000313|EMBL:KPM42982.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM42982.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM42982.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM42982.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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:KPM42982.1}.
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DR EMBL; LKCW01000039; KPM42982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BRD5; -.
DR STRING; 78410.A0A0P7BRD5; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000050424; 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:UP000050424};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 292..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 450..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 534..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 291..472
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 718..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 133407 MW; 591117CDB959920A CRC64;
MAAPNTRPNA GPAILIPDLH SRLDQAANHP RDNQCCRRRR VTFSDPLETM ASFLPRRFRG
ETTGPATPTP SWASKRLTPL VQYLSRLACS HPIHTVVIVA VLASTSYVGL LQESLFSIDV
SGASVGKADW SSLIEGSRVL LVNPDNGWKW QGVSPDSAAA AEAEHLALLT LVFPDTLSTD
SPSTAPHSHH VPIPTNLSIT SLPSTENSFT AYSQDSILAY ALPYLEGPEF LAAAQEIPDE
DAEETETPHG REKKMWIMKA AKVITRNTVI HWFSDTWTGF LDLLKNAETL DIVIMLLGYI
AMHLTFVSLF LSMRRMGSKF WLGICTLFSS VFAFLFGLAV TTKLGVPISV ILLSEGLPFL
VVTIGFEKNI VLTRAVMSHA VEHRRAQLKS SKSGKRSAER TNENMIQYAV RAAIKDKGFE
IVRDYAIEIL ILVLGAASGV QGGLQHFCFM AAWILFFDCI LLFTFYTAIL SIKLEINRIK
RHVDMRMALE DDGVSRRVAE NVASSNDEWP GVNGGDKNSS LFGRKSSSVP KFKVLMILGF
ILVNIINLCS IPFRNPSSLS NLRSLATSLG GLVSPLTVDP FKVASNGLDT ILAAAKANNR
PTLVTILTPI KYELEYPSVH YALGSALNGS GSSVDDGFSK FHGYGVGGRV VGGLLKSLED
PVLSKWIIVA LALSVGLNGY LFNVARWGIK DPNVPEHPID RSELARAQRF NDTSAATLPL
GEYVPPTPQR TEPSTPAVTD DESVDMLQMT KARPSTAINR PNRPNAELEQ LQREGRVPEM
SDEEVVSMSM RGKIPGYALE KTLKDFTRAV KIRRTIISRT KATSDLTHVL EQSKLPYEHY
NWERVFGACC ENVIGYLPLP VGVAGPLVID GQSYFIPMAT TEGVLVASTS RGSKAINSGG
GAVTVLTADG MTRGPCVSFE TLERAGAAKL WLDSEAGQTV MKKAFNSTSR FARLQHMKTA
LAGTNLYIRF KTTTGDAMGM NMISKGVEHA LDVMANEAGF DDMQIISISG NYCSDKKAAA
LNWIDGRGKG VVAEAIIPAD VVKNVLKSDV DSLVELNIAK NLIGSAMAGS VGGFNAHAAN
IVAAIFLATG QDPAQVVESA NCITIMKNLR GSLQISVSMP SLEVGTLGGG TILEPQSAML
DMLGVRGSHP TNPGDNARRL ARIIAAATLA GELSLCSALA AGHLVKAHMT HNRSAAPSRS
TTPAPPPQSP VSLAMTSAQE RSASTTSMSA AAVQRSKR
//
