HMDH_BLAGE
ID HMDH_BLAGE Reviewed; 856 AA.
AC P54960;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
DE Short=HMG-CoA reductase;
DE EC=1.1.1.34;
OS Blattella germanica (German cockroach) (Blatta germanica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Ectobiidae;
OC Blattellinae; Blattella.
OX NCBI_TaxID=6973;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8477698; DOI=10.1111/j.1432-1033.1993.tb17753.x;
RA Martinez-Gonzalez J., Buesa C., Piulachs M.D., Belles X., Hegardt F.G.;
RT "Molecular cloning, developmental pattern and tissue expression of 3-
RT hydroxy-3-methylglutaryl coenzyme A reductase of the cockroach Blattella
RT germanica.";
RL Eur. J. Biochem. 213:233-241(1993).
CC -!- FUNCTION: Synthesis of mevalonate for the production of non-sterol
CC isoprenoids, which are essential for growth differentiation.
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:0000255|PROSITE-ProRule:PRU10003};
CC -!- ACTIVITY REGULATION: The activity of HMG-CoA-reductase is suppressed by
CC exogenous mevalonate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; X70034; CAA49628.1; -; mRNA.
DR PIR; S30338; S30338.
DR AlphaFoldDB; P54960; -.
DR SMR; P54960; -.
DR UniPathway; UPA00058; UER00103.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 1.10.3270.10; -; 1.
DR Gene3D; 3.30.70.420; -; 1.
DR Gene3D; 3.90.770.10; -; 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; IPR004816; HMG_CoA_Rdtase_metazoan.
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 PANTHER; PTHR10572; PTHR10572; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; SSF55035; 1.
DR SUPFAM; SSF56542; SSF56542; 1.
DR TIGRFAMs; TIGR00920; 2A060605; 1.
DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; NADP;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..856
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase"
FT /id="PRO_0000114430"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 365..443
FT /note="Linker"
FT REGION 443..771
FT /note="Catalytic"
FT REGION 836..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 528
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 659
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 735
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 834
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 93157 MW; 833273836FC55AAA CRC64;
MVGRLFRAHG QFCASHPWEV IVATLTLTVC MLTVDQRPLG LPPGWGHNCI TLEEYNAADM
IVMTLIRCVA VLYSYYQFCH LQKLGSKYIL GIAGLFTVFS SFVFSSSVIN FLGSDVSDLK
DALFFFLLLI DLSKATVLAQ FALSSRSQDE VKHNIARGIA MLGPTITLDT VVETLVIGVG
MLSGVRRLEV LCCFACMSVI VNYVVFMTFY PACLSLILEL SRSGESGRPA WHDKSLIIKA
LHEEDQKPNP VVQRVKVIMS AGLMLVHAHR WVRCLSIALW PDLTSLRYFC THCDTGVSYS
RWSFASEGEE LPTVKLVTGD SVVNSNSTDD AQLHYYIMRW LTVSADHIVI LILLLALAVK
FVFFETRDEL TTTRGMDGWV EVSSPVEHKY VQTEQPSCSA PEQPLEEPPA SNRSIDECLS
VCKSDVGAQA LSDCEVMALV TSGHIAGYQL EKVVRNPERG VGIRRQILTK TADLKDALDN
LPYKNYDYLK VMGACCENVI GYMPVPVGVA GPLNLDGRLV HVPLATTEGC LVASTNRGMR
ALMRCGVTSR IVADGMTRGP VVRFPNIDRA SEAMLWMQVP YNFEQIKKNF DSTSRFARLS
KIHIRVAGRH LFIRFIATTG DAMGMNMLSK GTEVALAYVQ QVYPDMEILS LSGNFCTDKK
PAAVNWIEGR GKSVVCEAIV PADIIKSVLK TSVQALMDVN ITKNLIGSAV AGSIGGFNAH
AANIVTAIFI ATGQDPAQNV GSSNCMTLME PWGEDGKDLY VSCTMPSIEI GTIGGGTVLP
PQAACLDMLG VRGANEMCPG ENANTLARIV CGTVLAGELS LMSALAAGHL VKSHMRHNRS
SVSTSGSEPS TPACKS
