ID A0A423VUV1_9PEZI Unreviewed; 1171 AA.
AC A0A423VUV1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
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=VPNG_09317 {ECO:0000313|EMBL:ROV94842.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROV94842.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROV94842.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROV94842.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
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:ROV94842.1}.
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DR EMBL; LKEB01000074; ROV94842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VUV1; -.
DR STRING; 1230097.A0A423VUV1; -.
DR InParanoid; A0A423VUV1; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000285146; 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:UP000285146};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 371..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 482..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 243..418
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 659..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 125629 MW; E0DEFE8D7D6A68FD CRC64;
MIAASLLPSR FRGEQPASQV QPPSWLNIKV TPFLRSVSKL TSSHPIHTIG VVALLASSSY
LGLLEEKLFD ATRAVRKADW PSLAEGSRSL QVGPESGWKW QSRDSDAELG SDVDHLALLT
LVFPDSLSDD GPRTAPSLNT IPLQQNLSII SLPSTSNSLT TYSQETSLAL TVPYFQAPEF
LAAAQEIPDA VPGQETPETE HGKEKKMWIM KAAKVNPQNS IIEWVRNGWL DFLDLLKNAE
TLDITIMVLG YISMHLTFVS LFLSMRRMGS NFWLAATTLF SSAFAFMFSL VVVTKLGVPI
SMVLLSEGLP FLVITIGFEK NITLTRAVLN HSLEHKALQE KNGNKGTSSN AIQSAIQVAI
SEKGYDIVKD YAIEIVILTL GAASGVQGGL QQFCFLAAWI LFFDCILLFT FYTAILCIKL
EINRIKRHVE MRRALEDDGV SRRVAENVAQ SNEWPRADGK DKPSTSLFGQ QFKSSSVPKF
KVLMVGGFVL INAINLCTIP FRSTDSLTTI TSWAGGLGGL VTNPPVDPFK VASNGLDTIL
TQAIANNQPV VVTILTPIKY ELEYPSVHYG KAAETSAEEE ADGSYVMGGP LVGSFLKSLE
DPVLSKWIVI ALAMSVALNG YLFNAARWGI KDPNVPDHPI DVKELARAQR FNDSDASLAP
VVRSDGLGRQ PPREAGPPTP APTDDEGDAS AIKRVESTLS IVSDGPQRPM PELLALLAEK
RISEMTDEEV VGLALKGKIP GHSLERTLKD CTRAVKVRRS IISRTRATSD NTNGLERSKL
PYQHYNWDLV LGACCENVIG YMPLPVGVAG PLVVDGQSYF IPMATTEGVL VASANRGCKA
INAGGGAVTV LTADGMTRGP CVAFETLERT GAAKLWLDSD AGQIAMKKAF NSTSRFARLA
SMTSTIAGTN LYIRFKSTTG DAMGMNMISK GVEHALSVMA NEHDFQDMQI VSVSGNYCID
KKPSAINWIQ GRGKSVVAEA IIPGDVVKSV LKTDVDTLVE LNINKNLIGS AMAGSVGGFN
AQAANLVAAI FIATGQDPAQ VVESANCITI MKNLRGSLQI SVSMPSIEVG TLGGGTILEP
QSAMLDLLGV RGPHPITPGE NARRLSRIVA SIVLAGELSL NAALAAGHLV KAHMAHNRSA
PPTRSSTPAP TAAAGLTMTS MSAAAVERAK R
//
