ID A0A0N1HB09_9EURO Unreviewed; 1409 AA.
AC A0A0N1HB09;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AB675_7862 {ECO:0000313|EMBL:KPI41363.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI41363.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI41363.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI41363.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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:KPI41363.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000010; KPI41363.1; -; Genomic_DNA.
DR RefSeq; XP_018001326.1; XM_018148263.1.
DR STRING; 1664694.A0A0N1HB09; -.
DR GeneID; 28740143; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000038010; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
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; PF00106; adh_short; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR Pfam; PF13323; HPIH; 1.
DR Pfam; PF02460; Patched; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR PROSITE; PS00061; ADH_SHORT; 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:UP000038010};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 514..535
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 651..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 676..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 745..766
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 513..698
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1409 AA; 151464 MW; D6163536B94013D0 CRC64;
MTAAANSSSS RKRSVLITGC SDGGLGAALA LELHRRGLHV YATARNPNKM SQVKAQGIET
LTLDVLSPES ISAVSHKITQ LDILVNNAGG MYAMPISDLS ISKAKELFNL NVWSMIEVTQ
AFLPQLRASK GLVVNNTSTA AFFTLAYQST YNASKAAAIM FTDCLRIELA AFGIKVVDLK
TSSTTSQGYP NQALAGDVSL PAGSWYECAR DEVQKTMRGE RYPVQVTAET WAAQVSNDLL
KNDNPPSSIW RGTNAWAAWF TTRRPFALPE SMIRKMCGVN MVERLVAASA ESNDSWLNRN
VTSTLLTLSR IACQHPIHSI VAIALFASTS YVGLLQESLF DTGLPSLSKN GRLDTKALLK
GSRSLELSQN TDWKWLSHDN EPVPAVADDI DHLALTTFIF PDSSSAQLAP NAASVAFPSN
ITAVNVPSTS NVLSQFSQDS TLAFYFPYKN IVEFLRAVQE LPATRPADAA AADKRWVMKA
ARINGNGHAS YILWLQEGWS SFVDLLKHAE TLDIVIMALG YLSMHLTFIS LFVSMKRLGS
NAWLAVSVLF SSLFAFLFGL AVTTKLGVPI NMVLLSEGLP FLVVTVGFEK SIILTKAVLS
ASYDVRKKPS DKPAPNGNAI APASAAHAPP SIQDAIQLAV KETGFEIVRD YMIEIAILIA
GAATGVQGGL RQFCFLAAWI LFFDCVLLFT FYTTILCIKL EINRIKRHVA LRKALEEDGI
NRHSDKGSVF NIFGQKVKPN SVPKFKIWMV TGFVVINLVN LCTIPFRPTT NLKTPAAAIS
SVLTPAPIDP FKVAENGLDS IYVSAKSNHV ETYVTVLPPI KYELEPINPS TGGVDEFGFF
DHEYTDQFFN VVGGRVIESL LKSLEDPALS KWVLIALTLS VILNGYLFNA ARWSLKEPQT
PAVSPAVPVI SAPTSPVARR SKMINTEAAS DRSREECEAL LKEKKAAHLN DEELIDLSLR
GKIPGYAIEK TLEDPSLMTR LESFTRAVKV RRAVVSRTPA TRDITSLLES SKTPYKHFNY
ELVHGACCEN VIGYLPLPLG VAGPLLIDGE NFFIPMATTE GVLVASTSRG CKAINAGGGA
VTVVTGDGMT RGPCVGFPTL ARAGQAKVWL DSEDGRKTMT DAFNSTSRFA RLQSMKTALA
GTYLYIRFKT TTGDAMGMNM ISKGCEKALE VMSTVGGFDD MATISLSGNF CTDKKPAAVN
WIDGRGKAVV AEAIIPGDVV RNVLKSNVDA LVELNTSKNL IGSAMAGSIG GFNAHASNIV
TAVFLATGQD PAQNVESSNC ITIMKNNNGN LQISVSMPSI EVGTIGGGTI LEAQSSMLEM
LGVRGAHPTN PGDNSRKLAK IVAAAVLAGE LSLCSALAAG HLVRAHMAHN RSAAPTRAAT
PVSAAVEPFV RAQNGPAVPT GLRMTNGAR
//
