ID A0A0D2AS70_9PEZI Unreviewed; 1167 AA.
AC A0A0D2AS70;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 40.
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=PV09_00399 {ECO:0000313|EMBL:KIW09523.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW09523.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW09523.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW09523.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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}.
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DR EMBL; KN847529; KIW09523.1; -; Genomic_DNA.
DR RefSeq; XP_016219392.1; XM_016353135.1.
DR AlphaFoldDB; A0A0D2AS70; -.
DR SMR; A0A0D2AS70; -.
DR STRING; 253628.A0A0D2AS70; -.
DR GeneID; 27308372; -.
DR VEuPathDB; FungiDB:PV09_00399; -.
DR HOGENOM; CLU_001734_0_0_1; -.
DR InParanoid; A0A0D2AS70; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000053259; 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:UP000053259};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 249..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 303..323
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 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 248..424
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 461..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 125599 MW; 1B3917A0E286B32D CRC64;
MLGASFLPAR WRPADQSPQQ HRKPTWLSRK LNPYLTGVSR RATVHPIYTI VCVAVLASTT
YLGLLESSLF EARSSVQGSS ASVDFDSLLA GSKKLYASAE NDWSWLPVDS EIDKPVDDNI
ALITFVFPNS ISSTPQTAPR PASVPTPSNS TASILPCSTG RLQSMSQDAS LAYSMPFSEA
PSFLAASQEI PVSKAASQAR YSDDGSKTEE KKWIMKAVRS PGSGGVRRWM RNAWVDFVDL
LKNAETLDIV IMILGYISMH LTFVSLFLSM RRLGSNAWLA ISVLFSSCFA FLFALIVTTK
LGVSLNMVLL SEGLPFLVVT IGFEKPIILT KAVLAHALDR RWTEEKNGQS RSAAPPTIQY
AVQTAVKECG ADIVRDYLVE ICILICGAAS GVQGGLRQFC FLAAWILFFD CILLFTFYTS
ILTVKLEINR IKRHVALRKA LEDDGVSRKV AENVAASNEW PQLSRSRSSS DSSDPIDSDE
HPVFGRNARD SSIPRFKVMM VGGFVLINLL NLCSIPFRKT TGPLVSGLSS VVANPPIDPF
KVAGNGLESI LQSAQAKSRS VMVTVFAPIK YELEYPSVHY ATGKDDSTFF EGDYADQLYA
GVGGKVVEGV LKSFEDPVLS KWIVVALVMS LVLNGYLFNA ARWTIKEPSP PAQPPKESEV
MDQVPPRQVA NPEVVVAPPQ TPPQEAEVDG PVQSSGDGHQ RTREELEQMV KAKQAHLLSD
EELIDLASRG KIPGYALEKT LGDMTRAVKI RRAVVSRTPS TRETASFLEH SKLPYHHFDY
ERVLGACCEN VIGYMPLPLG VAGPVNIDGQ NFFLPMATTE GVLVASTSRG CKAINAGGGA
STVLTADGMT RGPCVKFESA RRAGEAKVWV DSDEGQKVMK DAFNSTSRFA RLQQLKTTIA
GNKLFIRFKT TTGDAMGMNM ISKGCEHALK VMSEEAGFDD MQIISLSGNF CTDKKPAAIN
WIDGRGKSVV AEATIPGDVV KSVLKTTVEA LVELNVSKNL VGSAMAGSIG GFNAHAANLV
AAIFIATGQD PAQVVESSNC ITLMENINGN LHISVSMPSI EVGTIGGGTI LEPQAAMLDL
LGVRGPHPTN PGDNARQLAR IIATAVLAGE LSLNAALAAG HLVRAHMAHN RSAVPSAAPS
RAATPAPSTP TTYAMREGLR LTAASGR
//
