ID A0A1R0H5C6_9FUNG Unreviewed; 1157 AA.
AC A0A1R0H5C6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
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=AYI68_g1488 {ECO:0000313|EMBL:OLY84349.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY84349.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY84349.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY84349.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
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:OLY84349.1}.
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DR EMBL; LSSL01000533; OLY84349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0H5C6; -.
DR STRING; 133383.A0A1R0H5C6; -.
DR UniPathway; UPA00058; UER00103.
DR Proteomes; UP000187455; 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; 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:UP000187455};
KW Transmembrane {ECO:0000256|RuleBase:RU361219};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361219}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361219"
FT DOMAIN 273..448
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1157 AA; 126319 MW; B8ADBD73097242A3 CRC64;
MSALRKVFRF PIRNPIESIA FVLVVISIPL YWLWTSIKDE DVFRRPNLKF PGTSFTYIIE
NGEANLLQTD LSANFNSDYE ASSSSAELYT IIFRTHGAFD SRGILRKQYI QKVQSFVDEI
SNNSLDSFPN GEKISSKNIN QILDTKVVLS PFHSPAIPED RVSTYLDPEL SYLFLDKRTN
PSGGVTGAQA AVIAVYLNTT TSSQKAAAHS WWKQVSSQAP DFTFDYSKST GKSKENISSR
LIKDRSSLPL VAVISQNFLW RISDMLKQAN PSEISLVLFT YSIMFIFLIQ LFSTMNGLGS
KYSLGITVVV TQVAAVLLAF FSFKAFGLKI ESVILSESLP FLFISHGFDK HIILAKSTIL
SFVQNFKKSN SSKKSRNIIL MDQNEIMESG IKSCLPSLLK GYGIEFTILL AGCASGIQSV
RIVCLFSIFI LFFDAVFMFT TYISILTLKV NLMQTRISAL KKPSARSDAL KSINYKTLIS
EASSKDSKLI SRIKFLAIFA FLLMNFMDLK LSFAPSASKS SNNLPAKAFS FESTGYLQYD
SLIKPLVLNI SQSSPKDSSL HLFINVPTEY VVDPTKVSDG VVSSQLDKST FSFNAGLFKS
SINSVQLSAL LVISILLNIY FAFSKEPSKQ KVNRSKRNPI LNSLGLKKIG RSLIYPKMSL
ASNINTSSSN TDDSNTEESD PAKVVDLIPN NDIVQNEQPK IVVAGELSEK FEKVIYTFDE
NGKLDNASAA SLKLKLDLLN NNGPEGLLDQ EIVDLVIHGF VQQYALEGKL NDPTRAVKIR
RLVTFGKITG DLDSMNSLPY ESYDYSSVIG QCCENVIGYL PIPVGVAGPL LINDESLFIP
MATTEGALIA STSRGCKAIS LGGGVSSFLV NDGMTRGPCL EMSNLRSAYE LKTWADSEEG
FQELKQSFES TSRFAKLLSV KTTLAGRMCF IRFKTFTGDA MGMNMISKGT ENALRLILST
FEGSKVISIS GNYCTDKKPA SINWIDGRGK SIVAEAVIPE SVVSSVLKTS ISKLVEVNTK
KNLVGSAMAG AMGGFNAHAS NILTAIFLAT GQDPAQNVES SMCLTFMEQK GDDLVVSVTM
PCIEVGTIGG GTGLKPQQSC LSMLGCLGPN YDAPGSNAQR LAKIIAGTVM AGELSLLAAL
CTGDLVKSHI ALNRKAN
//
