ID A0A010RVD3_9PEZI Unreviewed; 1180 AA.
AC A0A010RVD3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 13-SEP-2023, entry version 43.
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=CFIO01_06610 {ECO:0000313|EMBL:EXF76233.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF76233.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF76233.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF76233.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-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:EXF76233.1}.
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DR EMBL; JARH01000861; EXF76233.1; -; Genomic_DNA.
DR RefSeq; XP_007600098.1; XM_007600036.1.
DR AlphaFoldDB; A0A010RVD3; -.
DR STRING; 1445577.A0A010RVD3; -.
DR KEGG; cfj:CFIO01_06610; -.
DR eggNOG; KOG2480; Eukaryota.
DR HOGENOM; CLU_001734_0_0_1; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000020467; 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:UP000020467};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 376..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 485..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 241..423
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 668..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 127347 MW; 95B024544E68A75A CRC64;
MISSTLLPRR FRGEQPAAQA AAPSWVNKKI TPALKFLSKL ACSHPIHTVV IVAVLASTSY
VGLLQESLFD ATISVRTADW SSLVEGSRRL QAGPETAWKW QNVEPEASIA GEVDHQALLT
LVFPESQSPE SINTAPRTHA VPIPQNLSIT SLPSTSNSLT TYSQDSALAF AVPYSQAAEF
LSVAQEIPDA TSDETETMHG KEKKMWIMKA AKVHTRNSLV QWARNGWTEF LDLLKNAEAL
DIFIMVLGYL SMHLTFVSLF LSMRRMGSNF WLFTNVLFSS VFAFLFGLLV TTKLGVPITM
VLLSEGLPFL VVTIGFEKNI ILTRAVLSHA VEHRRPQENK DDRKSSKKSD VSSPNVIQYA
VQAAIKEKGY DIVKDYAIEI GILVLGAASG VQGGLQQFCF LAAWILFFDC ILLFSFYTAI
LSIKLEINRI KRHVQMRRAL EDDGVSHRVA ENVAKSNDWP EFDGKAPKET SLFGKQMKSS
NVPKFKVLMV SGFVLINAIN ICTIPFRNSS SLPSLSSLTG GLSAVVTAPP VDPFKVASNG
LDAILESAKA NERPTVVTVL TPIKYELEYP SIHYALPSPA SKSGQKHQDE YDTFESYGMG
GRMVGSILKS LEDPVLSKWI IVALAMSVAL NGYLFNAARW GIKDPNVPDH QIDPKELARA
EKFNDTDSAT LPLGEYIPET PRPATPAETD DESEAKSGKP ATPVEQRTIA QLEKMIAEKR
VHEMTDQEIV GMSLRGKIPG YSLERTLKDF TRAVKIRRSI ISRTNATSDL TNGLERSKLP
YHNYNWERVF GACCENVVGY LPLPVGVAGP LVIDGQSYFI PMATTEGVLV ASASRGCKAI
NSGGGAVTVL TGDGMTRGPC VGFETLERAG AAKIWLDSEA GQNTMKKAFN STSNFARLQT
MKTALAGTNL YIRFKTTTGD AMGMNMISKG VEHALSVMAS EGFEDMSIVS VSGNYCTDKK
AAAINWIDGR GKSVVAEAII PADVVKNVLK SDVDTLVQLN VDKNLIGSAM AGSIGGFNAH
AANIVAAIFL ATGQDPAQVV ESANCITIMK NLRGSLQISV SMPSLEVGTL GGGTILEPQS
AMLDMLGVRG PHPTTPGENA RRLARIIAAG VLAGELSLCS ALAAGHLVRA HMQHNRSAPP
TRTNTPAPAS GTMTPVGLAM TSAVEKAAGK SAAAVERARR
//
