ID A0A1X2GXL3_9FUNG Unreviewed; 1095 AA.
AC A0A1X2GXL3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=DM01DRAFT_1297659 {ECO:0000313|EMBL:ORX62839.1};
OS Hesseltinella vesiculosa.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX62839.1, ECO:0000313|Proteomes:UP000242146};
RN [1] {ECO:0000313|EMBL:ORX62839.1, ECO:0000313|Proteomes:UP000242146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX62839.1,
RC ECO:0000313|Proteomes:UP000242146};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX62839.1}.
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DR EMBL; MCGT01000001; ORX62839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2GXL3; -.
DR STRING; 101127.A0A1X2GXL3; -.
DR OrthoDB; 816560at2759; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000242146; 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; 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; 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:UP000242146};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 236..400
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 609..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 118408 MW; 67C0EE1A3212CD06 CRC64;
MSLLPRGSTR GLTSSYASLV GKGIHRVAQV SARHPIEMIV SVLMAASFAY FYLFNLARSS
DLFIGTRSAT AHLSPAIVYS AQGEPFGLMP DTAGAPVKLA VKQVLITSAP SRHESRPAVR
QFQHLIENDI YVPDNSAHQF NYQGLCYKTS HDQCLTVQPF TTTNNDYLIP LVFNTSTHVR
HNLADIWEHK VATLPSSEFI SSSSASQENA FLWVMIVSRN IFFHLCEMIK VADNVDIVVV
LVGYVMAIST VISLYLNMRS MGSRYTLATA VVVNGLFSFM LGFLTVHMLG IKVHASTLAE
ALPFLVVTIG FERHFKLTKS VLMAHKKSPV PKQTIWKTLL MAVDIVAFPL ARDCCIEILV
LCLGAKSGIG GLREFCLLSA ILLAFDLFFM FTWYTAVLAL KLELGRIREI NTLGDDNASL
FVSPVSQAKK DLIEKTVVKA LSNNDADVFG KDDVKANDPL IGRIKLLLIA GFVGMQVLNI
CSTFESGPQL DVTQPAVADL LHTLLDAYKM DTNAVFPVMV EVSPSVLFHT ARSRWQLFPD
TIVQPLASLF DVYDVYIQHP VISKWLTVAL FVSLFLNTYL FNVVRQPKPT AATTPLTMDN
TQATKLPVAP APARVPSPAV HPPTHRRQHH RRHQNNDDQP IRSLESCMTL LHSPDELHDE
EIVTLVQAGK MAPYALEKTL GDFERAVSIR RSLISRASMT KTLEASALPL ENYHYDKVMG
ACCENVIGYM PLPVGIAGPM NIDGDLIHIP MATTEGCLVA STARGCKAIN AGGGAATVVT
ADGMTRGPCV EFPSAVRAAT CKLWLEAEGY SIITDAFNST SRFARVRKLK MAIAGKLLFI
RFSTTTGDAM GMNMISKGCE KALSVLQEHF EDMQIISLSG NYCTDKKPAA INWIEGRGKS
VVSEAVIPGS VVEKVLKTSV AALVELNTSK NLIGSAMAGS IGGFNAHAAN ILTAVYLATG
QDPAQNVESS NCITLMKAVN DGQDLHISCT MPSIEVGTIG GGTILPPQRS MLDLLGVSGP
HPDQPGKNAQ RLARIICAAV MAGELSLLSA LAAGHLVKAH MAHNRGTTAA PVTPSTTPAN
GGATPTPELG TCIRS
//
